@article{diaz_foegeding_lila_2021, title={Whey protein-polyphenol aggregate particles mitigate bar hardening reactions in high protein bars}, volume={138}, ISSN={["1096-1127"]}, DOI={10.1016/j.lwt.2020.110747}, abstractNote={Formulating high protein bars is a challenge since concentrated proteins can negatively affect texture and reduce shelf life, causing the products to be unacceptable for consumers. This study examined the functionality of protein-polyphenol aggregate particles formulated with whey protein isolate (WPI) and polyphenol-rich cranberry juice (or imitation juice) in model high protein bars. Differences in texture and structure of protein bars during 43 days of storage at 32 °C were dependent on the type of protein (unmodified WPI or aggregate particle) and the drying technique (freeze-drying or spray-drying) used in particle formation. Bars prepared with WPI-cranberry spray-dried particles (WPI–C SD) were softer and less elastic than those formulated with unmodified WPI or polyphenol-free (WPI-IC FD, WPI-IC SD) particles (firmness range 0.09–0.85 kPa). Bars formulated with WPI-cranberry freeze-dried particles (WPI–C FD) were softer than control bars made with WPI; but, only up until 31 days of storage, and less elastic than control bars up until 11 days. The addition of protein-polyphenol particles not only increased the nutritional content of the protein bars, but also inhibited rheological and structural changes, and could be used as a novel approach for functional delivery of protein in the formulation of high protein bars.}, journal={LWT-FOOD SCIENCE AND TECHNOLOGY}, author={Diaz, Joscelin T. and Foegeding, E. Allen and Lila, Mary Ann}, year={2021}, month={Mar} }
 @article{foegeding_2020, title={Basic, applied, and developmental R&D should be under one roof}, volume={85}, ISSN={["1750-3841"]}, DOI={10.1111/1750-3841.14559}, number={8}, journal={JOURNAL OF FOOD SCIENCE}, author={Foegeding, E. Allen}, year={2020}, month={Aug}, pages={2264–2264} }
 @article{foegeding_2020, title={Celebrating reviewers-The 2020 Manfred Kroger Outstanding Reviewer Award winner}, volume={85}, ISSN={["1750-3841"]}, DOI={10.1111/1750-3841.14551}, number={6}, journal={JOURNAL OF FOOD SCIENCE}, author={Foegeding, E. Allen}, year={2020}, month={Jun}, pages={1618–1618} }
 @article{foegeding_2020, title={Dear authors, reviewers, and editors: Thank you!}, volume={85}, ISSN={["1750-3841"]}, DOI={10.1111/1750-3841.14547}, number={5}, journal={JOURNAL OF FOOD SCIENCE}, author={Foegeding, E. Allen}, year={2020}, month={May}, pages={1383–1383} }
 @misc{carter_foegeding_drake_2020, title={Invited review: Astringency in whey protein beverages}, volume={103}, ISSN={["1525-3198"]}, DOI={10.3168/jds.2020-18303}, abstractNote={Astringency is the sensation of mouth drying and puckering, and it has also been described as a loss of lubrication in the mouth. Astringency is perceived as an increase in oral friction or roughness. Astringency caused by tannins and other polyphenols has been well documented and studied. Whey proteins are popular for their functional and nutritional quality, but they exhibit astringency, particularly under acidic conditions popular in high acid (pH 3.4) whey protein beverages. Acids cause astringency, but acidic protein beverages have higher astringency than acid alone. Whey proteins are able to interact with salivary proteins, which removes the lubricating saliva layer of the mouth. Whey proteins can also interact directly with epithelial tissue. These various mechanisms of astringency limit whey protein ingredient applications because astringency is undesirable to consumers. A better understanding of the causes of whey protein astringency will improve our ability to produce products that have high consumer liking and deliver excellent nutrition.}, number={7}, journal={JOURNAL OF DAIRY SCIENCE}, author={Carter, B. G. and Foegeding, E. A. and Drake, M. A.}, year={2020}, month={Jul}, pages={5793–5804} }
 @article{franks_jeltema_luck_beckley_foegeding_vinyard_2020, title={Morphological and masticatory performance variation of mouth behavior groups}, volume={51}, ISSN={["1745-4603"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-85074800855&partnerID=MN8TOARS}, DOI={10.1111/jtxs.12483}, abstractNote={Abstract}, number={2}, journal={JOURNAL OF TEXTURE STUDIES}, author={Franks, Erin M. and Jeltema, Melissa and Luck, Paige J. and Beckley, Jacqueline and Foegeding, E. Allen and Vinyard, Christopher J.}, year={2020}, month={Apr}, pages={343–351} }
 @article{li_ndiaye_corbin_foegeding_ferruzzi_2020, title={Starch-phenolic complexes are built on physical CH-pi interactions and can persist after hydrothermal treatments altering hydrodynamic radius and digestibility of model starch-based foods}, volume={308}, ISSN={["1873-7072"]}, DOI={10.1016/j.foodchem.2019.125577}, abstractNote={Leveraging phenolic complexation to optimize starch functionality and digestibility is restrained by the obscurity of their physicochemical nature and molecular basis. To define starch-phenolic complexes under hydrothermal treatments, maize amylopectin and potato starch were complexed with caffeic acid, ferulic acid and gallic acid. Starch hydrothermal stability and digestibility were measured by differential scanning calorimeter and Englyst's method, respectively. While monosaccharide compositions and glycosidic linkages were analyzed by GC-MS, hydrodynamic radius and proton magnetic resonance of gelatinized complexes were measured by dynamic light scattering and NMR respectively. Compared with native starches, starch-phenolic complexes were not chemically modified and had modestly lower estimated glycemic indexes and significantly lower gelatinization temperatures (p < 0.05). Starch-phenolic complexes also had significantly lower levels of phenolic proton intensities and hydrodynamic radii relative to the control starch-phenolic mixtures (p < 0.05). These results suggested that phenolics may complex with starch through non-covalent CH-π bonds along α-(1 → 4) glycosidic chains.}, journal={FOOD CHEMISTRY}, author={Li, Min and Ndiaye, Cheikh and Corbin, Sydney and Foegeding, E. Allen and Ferruzzi, Mario G.}, year={2020}, month={Mar} }
 @article{silva_carloni_cheung_cottone_donnini_foegeding_gulzar_jacquier_lobaskin_mackernan_et al._2020, title={Understanding and Controlling Food Protein Structure and Function in Foods: Perspectives from Experiments and Computer Simulations}, volume={11}, ISSN={["1941-1421"]}, DOI={10.1146/annurev-food-032519-051640}, abstractNote={ The structure and interactions of proteins play a critical role in determining the quality attributes of many foods, beverages, and pharmaceutical products. Incorporating a multiscale understanding of the structure–function relationships of proteins can provide greater insight into, and control of, the relevant processes at play. Combining data from experimental measurements, human sensory panels, and computer simulations through machine learning allows the construction of statistical models relating nanoscale properties of proteins to the physicochemical properties, physiological outcomes, and tastes of foods. This review highlights several examples of advanced computer simulations at molecular, mesoscale, and multiscale levels that shed light on the mechanisms at play in foods, thereby facilitating their control. It includes a practical simulation toolbox for those new to in silico modeling. }, journal={ANNUAL REVIEW OF FOOD SCIENCE AND TECHNOLOGY, VOL 11}, author={Silva, Fernando Luis and Carloni, Paolo and Cheung, David and Cottone, Grazia and Donnini, Serena and Foegeding, E. Allen and Gulzar, Muhammad and Jacquier, Jean Christophe and Lobaskin, Vladimir and MacKernan, Donal and et al.}, year={2020}, pages={365–387} }
 @article{wagoner_cakir-fuller_shingleton_drake_foegeding_2020, title={Viscosity drives texture perception of protein beverages more than hydrocolloid type}, volume={51}, ISSN={["1745-4603"]}, DOI={10.1111/jtxs.12471}, abstractNote={Abstract}, number={1}, journal={JOURNAL OF TEXTURE STUDIES}, author={Wagoner, Ty B. and Cakir-Fuller, Esra and Shingleton, Rebecca and Drake, MaryAnne and Foegeding, E. Allen}, year={2020}, month={Feb}, pages={78–91} }
 @article{cubides_eklund_foegeding_2019, title={Casein as a Modifier of Whey Protein Isolate Gel: Sensory Texture and Rheological Properties}, ISBN={1750-3841}, DOI={10.1111/1750-3841.14933}, abstractNote={AbstractThe objective of this study was to determine if casein could be used to adjust the structure of whey protein gels and alter targeted textural properties. Secondarily, we sought to determine if specific structural and mechanical properties were associated with sensory texture terms. Heat set gels were made from whey proteins alone or combined with casein in micellar or dispersed form at pH 6.0 and 5.5. Replacing the whey protein with casein produced a gel breakdown pattern that was more cohesive during mastication with increased moisture retention. Additionally, casein addition reduced gel strength but minimally altered recoverable energy (an indicator of elasticity). Structural breakdown patterns were shifted from brittle‐ to ductile‐like fracture for gels containing dispersed casein at pH 5.5 or micellar casein at pH 6.0. Shifts in microstructure observed by confocal microscopy could not explain the changes in mechanical or sensory textures. The differentiating sensory attributes among treatments were adhesiveness, cohesiveness of mass, tackiness, firmness, fracturability, and deformability. Most notably, adding casein increased cohesiveness while maintaining water holding properties. Sensory texture properties could be explained by a combination of macroscopic structural changes (appearance), fracture properties, and postfracture breakdown pattern. Overall, it was demonstrated that casein can be used to alter whey protein gel structure such that sensory firmness and fracturability are decreased and cohesiveness is increased, while preventing a large increase in moisture release.}, journal={JOURNAL OF FOOD SCIENCE}, author={Cubides, Yvette T. Pascua and Eklund, Peter R. and Foegeding, E. Allen}, year={2019} }
 @article{koc_drake_vinyard_essick_velde_foegeding_2019, title={Emulsion filled polysaccharide gels: Filler particle effects on material properties, oral processing, and sensory texture}, volume={94}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2019.03.018}, abstractNote={Addition of filler particles is a common approach to alter food structure and thereby change sensory properties. The goal of this investigation was to determine how filler particles alter oral processing patterns and sensory texture perception of two model food gels with distinct mechanical properties. Agar gels (brittle) and κ-carrageenan-locust bean gum gels (ductile) were formulated to have similar strength (fracture stress) but different deformability (fracture strain). Increasing the phase volume of oil droplets decreased fracture stress and stress intensity factor of both filled gels, while the main effect on fracture strain and fracture surface energy was observed for the highly deformable κ-carrageenan-locust bean. Adding oil had general effects of decreasing sensory hardness and particle size and increasing the rate of breakdown. Furthermore, agar gel texture was more sensitive to adding oil, with changes observed in several textural properties of agar gels with no corresponding change in κ-carrageenan-locust bean gels. Adding oil did not change the oral processing pattern based on distance and velocity of jaw movement, along with temporal aspects of each chewing cycle. However, jaw velocity and movement were adjusted for differences in gel type. κ-carrageenan-locust bean gels generally required more muscle activity to prepare for swallowing, and increasing oil content decreased overall muscle activity for both gels. These results imply that gel structure, rather than the amount of oil filler, determined the oral processing pattern.}, journal={FOOD HYDROCOLLOIDS}, author={Koc, Hicran and Drake, MaryAnne and Vinyard, Christopher J. and Essick, Gregory and Velde, Fred and Foegeding, E. Allen}, year={2019}, month={Sep}, pages={311–325} }
 @article{triani_foegeding_2019, title={Heat stability of whey protein ingredients based on state diagrams}, volume={91}, ISSN={["1879-0143"]}, DOI={10.1016/j.idairyj.2018.12.006}, abstractNote={A state diagram approach was used to compare heat stability among whey protein ingredients. Solutions were thermal processed and solubility, turbidity, and colloidal structure (sol, precipitate, or gel) were plotted against the variables of pH (3–7) and protein concentration (1–10%, w/w) to form state diagrams. Each of the whey protein ingredients produced state diagrams with unique patterns in the protein concentrations associated with colloidal structures and in heat stability regions. Relative heat stability among ingredients depended on the pH-thermal processing combination, in that patterns observed at pH ≤ 4.5 were not equivalent to patterns produced at pH > 4.5. Heating at temperatures of <100 °C for extended time did not produce the same results as heating at > 100 °C for short times. State diagrams were able to differentiate among the whey protein ingredients, but absolute values were determined by the heating treatment.}, journal={INTERNATIONAL DAIRY JOURNAL}, author={Triani, Rini and Foegeding, E. Allen}, year={2019}, month={Apr}, pages={25–35} }
 @article{wagoner_cakir-fuller_drake_foegeding_2019, title={Sweetness perception in protein-polysaccharide beverages is not explained by viscosity or critical overlap concentration}, volume={94}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2019.03.010}, abstractNote={It is generally reported that in random coil polysaccharide solutions, increasing polymer concentration above the critical overlap concentration (c*) results in decreased taste perception due to a high degree of polymer entanglement and resultant poor mixing efficiency with saliva in the mouth. However, these reports are commonly based on aqueous solutions of polymers and it is unknown if this phenomenon applies to more complex fluids containing protein and fat, or if taste suppression can be explained on the basis of an altered temporal profile of taste. In this study, the effects of carboxymethyl cellulose (CMC) concentration (0.15–1.50% w/w) on sensory texture and sweet taste perception (6.0% w/w sucrose) were evaluated. Zero-shear viscosity of CMC solutions ranged from 5.5 to 133 mPa s, and c* was experimentally determined to be 0.67% w/w. Three concentrations above c* were tested and only the highest (1.5% CMC) caused a significant (p < 0.05) reduction in sweet taste. Moreover, when combined with milk protein concentrate to approximate the macromolecular profile of reduced fat milk, perceived sweet taste slightly increased with viscosity. Time intensity evaluations revealed a large variation in temporal perception of sweet taste among individual panelists, with time to maximum intensity ranging from 4.8 to 33.5 s. The results indicate that the critical overlap taste suppression observed in aqueous solutions of polysaccharides did not apply to a more complex fluid microstructure containing a combination of protein and fat.}, journal={FOOD HYDROCOLLOIDS}, author={Wagoner, Ty B. and Cakir-Fuller, Esra and Drake, MaryAnne and Foegeding, E. Allen}, year={2019}, month={Sep}, pages={229–237} }
 @article{morell_tarrega_allen foegeding_fiszman_2018, title={Impact of composition and texture of protein-added yogurts on oral activity}, volume={9}, ISSN={["2042-650X"]}, DOI={10.1039/c8fo01483c}, abstractNote={Understanding how oral processing is altered in response to changes in the composition and mechanical properties of food provides useful information to design food with improved satiating capacity which is largely influenced by oral exposure.}, number={10}, journal={FOOD & FUNCTION}, author={Morell, Pere and Tarrega, Amparo and Allen Foegeding, Edward and Fiszman, Susana}, year={2018}, month={Oct}, pages={5443–5454} }
 @article{foegeding_plundrich_schneider_campbell_lila_2018, title={Protein-polyphenol particles for delivering structural and health functionality (Reprinted from Food Hydrocolloids, vol 72, pg 163-173, 2017)}, volume={78}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2018.02.047}, abstractNote={Dietary proteins and polyphenols contribute both nutritive and extra-nutritional (disease-preventing and metabolism-enhancing) benefits, and can participate in food structure formation and stabilization. There is a desire to increase consumption of proteins and polyphenols based on health considerations, and one approach is to form protein-polyphenol particles that combine both health and structural functionality in food products. The roles of proteins and polyphenols individually, or when bound together, are discussed in terms of health benefits (nutrition, disease prevention, satiety, allergy alleviation) and impact on food structure. The overall goal should be a rational design of protein-polyphenol particles to ensure a positive contribution to food quality, protein nutrition, and delivery of a health-relevant dose of polyphenols to the gastrointestinal tract.}, journal={FOOD HYDROCOLLOIDS}, author={Foegeding, E. Allen and Plundrich, Nathalie and Schneider, Margaret and Campbell, Caroline and Lila, Mary Ann}, year={2018}, month={May}, pages={15–25} }
 @article{sharma_munro_dessev_wiles_foegeding_2018, title={Strain hardening and anisotropy in tensile fracture properties of sheared model Mozzarella cheeses}, volume={101}, ISSN={["1525-3198"]}, DOI={10.3168/jds.2017-13126}, abstractNote={We studied the tensile fracture properties of model Mozzarella cheeses with varying amounts of shear work input (3.3-73.7 kJ/kg). After manufacture, cheeses were elongated by manual rolling at 65°C followed by tensile testing at 21°C on dumbbell-shaped samples cut both parallel and perpendicular to the rolling direction. Strain hardening parameters were estimated from stress-strain curves using 3 different methods. Fracture stress and strain for longitudinal samples did not vary significantly with shear work input up to 26.3 kJ/kg and then decreased dramatically at 58.2 kJ/kg. Longitudinal samples with shear work input <30 kJ/kg demonstrated significant strain hardening by all 3 estimation methods. At shear work inputs <30 kJ/kg, strong anisotropy was observed in both fracture stress and strain. After a shear work input of 58.2 kJ/kg, anisotropy and strain hardening were absent. Perpendicular samples did not show strain hardening at any level of shear work input. Although the distortion of the fat drops in the cheese structure associated with the elongation could account for some of the anisotropy observed, the presence of anisotropy in the elongated nonfat samples reflected that shear work and rolling also aligned the protein structure.}, number={1}, journal={JOURNAL OF DAIRY SCIENCE}, author={Sharma, Prateek and Munro, Peter A. and Dessev, Tzvetelin T. and Wiles, Peter G. and Foegeding, E. Allen}, year={2018}, month={Jan}, pages={123–134} }
 @article{wagoner_foegeding_2018, title={Surface energy and viscoelasticity influence caramel adhesiveness}, volume={49}, ISSN={["1745-4603"]}, DOI={10.1111/jtxs.12298}, abstractNote={Abstract}, number={2}, journal={JOURNAL OF TEXTURE STUDIES}, author={Wagoner, Ty B. and Foegeding, Edward Allen}, year={2018}, month={Apr}, pages={219–227} }
 @article{campbell_foegeding_velde_2017, title={A comparison of the lubrication behavior of whey protein model foods using tribology in linear and elliptical movement}, volume={48}, ISSN={["1745-4603"]}, DOI={10.1111/jtxs.12278}, abstractNote={Abstract}, number={4}, journal={JOURNAL OF TEXTURE STUDIES}, author={Campbell, Caroline L. and Foegeding, E. Allen and Velde, Fred}, year={2017}, month={Aug}, pages={335–341} }
 @article{foegeding_stieger_velde_2017, title={Moving from molecules, to structure, to texture perception}, volume={68}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2016.11.009}, abstractNote={The two main food biopolymers, proteins and polysaccharides, are used in many foods to form structures that are the basis of product identity and quality. One of the main factors determining food quality is texture. A simplistic view of food is that molecules are assembled into structures, and the breakdown of structures during oral processing determines texture. There have been great advancements in understanding mechanisms for how proteins and polysaccharides assemble into structures, and factors determining the mechanical properties of the structures. In contrast, the understanding of how breakdown of structures during oral processing produces specific textural properties is still incomplete. Structuring processes based on protein-polysaccharide mixtures and emulsion gels are evaluated regarding structure formation and texture perception. It is shown that these systems can be designed to modulate specific textural properties. Finally, future trends in this area are discussed.}, journal={FOOD HYDROCOLLOIDS}, author={Foegeding, E. Allen and Stieger, Markus and Velde, Fred}, year={2017}, month={Jul}, pages={31–42} }
 @article{plundrich_bansode_foegeding_williams_lila_2017, title={Protein-bound Vaccinium fruit polyphenols decrease IgE binding to peanut allergens and RBL-2H3 mast cell degranulation in vitro}, volume={8}, ISSN={["2042-650X"]}, DOI={10.1039/c7fo00249a}, abstractNote={Peanut allergy is a worldwide health concern.}, number={4}, journal={FOOD & FUNCTION}, author={Plundrich, Nathalie J. and Bansode, Rishipal R. and Foegeding, E. Allen and Williams, Leonard L. and Lila, Mary Ann}, year={2017}, month={Apr}, pages={1611–1621} }
 @article{foegeding_plundrich_schneider_campbell_lila_2017, title={Protein-polyphenol particles for delivering structural and health functionality}, volume={72}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2017.05.024}, abstractNote={Dietary proteins and polyphenols contribute both nutritive and extra-nutritional (disease-preventing and metabolism-enhancing) benefits, and can participate in food structure formation and stabilization. There is a desire to increase consumption of proteins and polyphenols based on health considerations, and one approach is to form protein-polyphenol particles that combine both health and structural functionality in food products. The roles of proteins and polyphenols individually, or when bound together, are discussed in terms of health benefits (nutrition, disease prevention, satiety, allergy alleviation) and impact on food structure. The overall goal should be a rational design of protein-polyphenol particles to ensure a positive contribution to food quality, protein nutrition, and delivery of a health-relevant dose of polyphenols to the gastrointestinal tract.}, journal={FOOD HYDROCOLLOIDS}, author={Foegeding, E. Allen and Plundrich, Nathalie and Schneider, Margaret and Campbell, Caroline and Lila, Mary Ann}, year={2017}, month={Nov}, pages={163–173} }
 @article{wagoner_foegeding_2017, title={Whey protein-pectin soluble complexes for beverage applications}, volume={63}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2016.08.027}, abstractNote={There is a strong interest in the consumption of beverages containing whey proteins due to implications in health outcomes such as increased satiety and metabolic regulation. However, low thermal stability limits the conditions under which whey protein beverages can be formulated. Studies have shown that at a narrow pH range near the protein isoelectric points, whey proteins and polysaccharides self assemble into soluble complexes (SCs) that exhibit unique functionality. This study investigated the formation and thermal stability of SCs under conditions relevant to beverage applications. Complexes were formed at pH 5 using whey protein isolate (WPI; 1–6% w/w) and high-methoxyl pectin (HMP; 0.125–0.75% w/w) and then heat-set at 85 °C for 25 min. Hydrodynamic properties, particle size distribution, ζ–potential, and dispersion viscosity were evaluated before and after heat-setting. Mean particle diameter ranged from 300 to 715 nm for unheated SCs, and 230 nm to 1 μm for heat-set SCs. Heat-setting SCs led to a significant (p < 0.05) reduction in intrinsic viscosity from 93.6 mL/g to 79.5 mL/g, suggesting conformational changes that favor a smaller hydrodynamic size. Dispersions of SCs exhibited decreased apparent viscosity, consistent with the lower intrinsic viscosity and smaller particle size. Heat-set SCs (4% WPI, 0.5% HMP) remained as sub-micron particles (d = 303–829 nm) after pH adjustment (pH 4–7) and thermal processing (142 °C for 6 s), indicating that WPI and HMP can be heat-set into complexes with enhanced colloidal stability in beverage applications.}, journal={FOOD HYDROCOLLOIDS}, author={Wagoner, Ty B. and Foegeding, E. Allen}, year={2017}, month={Feb}, pages={130–138} }
 @article{campbell_daubert_drake_foegeding_2016, title={An ISO-Protein Model Food System for Evaluating Food Texture Effects}, volume={47}, ISSN={["1745-4603"]}, DOI={10.1111/jtxs.12182}, abstractNote={Abstract}, number={5}, journal={JOURNAL OF TEXTURE STUDIES}, author={Campbell, Caroline L. and Daubert, Christopher R. and Drake, Maryanne and Foegeding, E. Allen}, year={2016}, month={Oct}, pages={377–391} }
 @article{wagoner_luck_foegeding_2016, title={Caramel as a Model System for Evaluating the Roles of Mechanical Properties and Oral Processing on Sensory Perception of Texture}, volume={81}, ISSN={["1750-3841"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84959510916&partnerID=MN8TOARS}, DOI={10.1111/1750-3841.13237}, abstractNote={Abstract}, number={3}, journal={JOURNAL OF FOOD SCIENCE}, author={Wagoner, Ty B. and Luck, Paige J. and Foegeding, E. Allen}, year={2016}, month={Mar}, pages={S736–S744} }
 @article{campbell_foegeding_harris_2016, title={Cocoa and Whey Protein Differentially Affect Markers of Lipid and Glucose Metabolism and Satiety}, volume={19}, ISSN={["1557-7600"]}, DOI={10.1089/jmf.2015.0044}, abstractNote={Food formulation with bioactive ingredients is a potential strategy to promote satiety and weight management. Whey proteins are high in leucine and are shown to decrease hunger ratings and increase satiety hormone levels; cocoa polyphenolics moderate glucose levels and slow digestion. This study examined the effects of cocoa and whey proteins on lipid and glucose metabolism and satiety in vitro and in a clinical trial. In vitro, 3T3-L1 preadipocytes were treated with 0.5-100 μg/mL cocoa polyphenolic extract (CPE) and/or 1-15 mM leucine (Leu) and assayed for lipid accumulation and leptin production. In vivo, a 6-week clinical trial consisted of nine panelists (age: 22.6 ± 1.7; BMI: 22.3 ± 2.1) consuming chocolate-protein beverages once per week, including placebo, whey protein isolate (WPI), low polyphenolic cocoa (LP), high polyphenolic cocoa (HP), LP-WPI, and HP-WPI. Measurements included blood glucose and adiponectin levels, and hunger ratings at baseline and 0.5-4.0 h following beverage consumption. At levels of 50 and 100 μg/mL, CPE significantly inhibited preadipocyte lipid accumulation by 35% and 50%, respectively, and by 22% and 36% when combined with 15 mM Leu. Leu treatment increased adipocyte leptin production by 26-37%. In the clinical trial, all beverages significantly moderated blood glucose levels 30 min postconsumption. WPI beverages elicited lowest peak glucose levels and HP levels were significantly lower than LP. The WPI and HP beverage treatments significantly increased adiponectin levels, but elicited no significant changes in hunger ratings. These trends suggest that combinations of WPI and cocoa polyphenols may improve markers of metabolic syndrome and satiety.}, number={3}, journal={JOURNAL OF MEDICINAL FOOD}, author={Campbell, Caroline L. and Foegeding, E. Allen and Harris, G. Keith}, year={2016}, month={Mar}, pages={219–227} }
 @article{wilson_luck_woods_foegeding_morgenstern_2016, title={Comparison of jaw tracking by single video camera with 3D electromagnetic system}, volume={190}, ISSN={["1873-5770"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84975832612&partnerID=MN8TOARS}, DOI={10.1016/j.jfoodeng.2016.06.008}, abstractNote={The breakdown of food during chewing is both a physical process and a sensory experience. In trying to understand the differing sensory responses of consumers to food products it is useful to be able to measure their physical chewing action. In this paper we report the results of a comparison between a simple 2D video jaw tracking method with a 3D method using the JT-3D™ Jaw Tracker (BioRESEARCH Assoc., Inc., Milwaukee), on four model gel systems. The video and JT3D systems gave similar values for number of chews, chewing time, chewing cycle time, chewing frequency, opening velocity, and proportion of crossed/crescent/circle shaped cycles. Although timing of the three phases of a chew and vertical and lateral movement were different between the two methods, the effect of the different model gels on these parameters are similar in direction by the two methods for vertical and lateral movement, and opening and closing velocity and closing time. Our study demonstrates that for sensory evaluation of foods and consumer preference, where large numbers of participants are required to cover the variation in human populations, the simple 2D video method allows jaw movement to be tracked with sufficient accuracy to detect the effects produced by different foods.}, journal={JOURNAL OF FOOD ENGINEERING}, author={Wilson, Arran and Luck, Paige and Woods, Carmel and Foegeding, E. Allen and Morgenstern, Marco}, year={2016}, month={Dec}, pages={22–33} }
 @article{wagoner_vardhanabhuti_foegeding_2016, title={Designing Whey Protein-Polysaccharide Particles for Colloidal Stability}, volume={7}, ISSN={["1941-1421"]}, DOI={10.1146/annurev-food-041715-033315}, abstractNote={ Interactions between whey proteins and polysaccharides, in particular the formation of food-grade soluble complexes, are of interest because of potential functional and health benefits. A specific application that has not received much attention is the use of complexes for enhanced colloidal stability of protein sols, such as protein-containing beverages. In beverages, the primary goal is the formation of complexes that remain dispersed after thermal processing and extended storage. This review highlights recent progress in the area of forming whey protein–polysaccharide soluble complexes that would be appropriate for beverage applications. Research in this area indicates that soluble complexes can be formed and stabilized that are reasonably small in size and possess a large surface charge that would predict colloidal stability. Selection of specific proteins and polysaccharides can be tailored to desired conditions. The principal challenges involve overcoming restrictions on protein concentration and ensuring that protein remains bioavailable. }, journal={ANNUAL REVIEW OF FOOD SCIENCE AND TECHNOLOGY, VOL 7}, author={Wagoner, Ty and Vardhanabhuti, Bongkosh and Foegeding, E. Allen}, year={2016}, pages={93–116} }
 @article{smith_foegeding_drake_2016, title={Flavor and Functional Characteristics of Whey Protein Isolates from Different Whey Sources}, volume={81}, ISSN={["1750-3841"]}, DOI={10.1111/1750-3841.13248}, abstractNote={Abstract}, number={4}, journal={JOURNAL OF FOOD SCIENCE}, author={Smith, T. J. and Foegeding, E. A. and Drake, M. A.}, year={2016}, month={Apr}, pages={C849–C857} }
 @article{schneider_esposito_lila_foegeding_2016, title={Formation of whey protein–polyphenol meso-structures as a natural means of creating functional particles}, volume={7}, ISSN={2042-6496 2042-650X}, url={http://dx.doi.org/10.1039/C5FO01499A}, DOI={10.1039/c5fo01499a}, abstractNote={Whey proteins provide structure and nutritional properties in food, while berry juices are thought to have biological activity that can impart anti-inflammatory health effects.}, number={3}, journal={Food & Function}, publisher={Royal Society of Chemistry (RSC)}, author={Schneider, Margaret and Esposito, Debora and Lila, Mary Ann and Foegeding, E. Allen}, year={2016}, pages={1306–1318} }
 @article{luck_varum_foegeding_2015, title={Charge related astringency of chitosans}, volume={48}, ISSN={["1873-7137"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84924240333&partnerID=MN8TOARS}, DOI={10.1016/j.foodhyd.2015.02.024}, abstractNote={Chitosan is a biopolymer that can be used in food applications such as forming edible coatings and nanoparticles. It is a linear polysaccharide composed of neutral (acetylated) and positively (deacetylated) sugar units and can be prepared with varying content of the two units. One factor limiting the use of chitosan is causing an unacceptable level of astringency. We hypothesized that astringency was related to the positive charge density and that decreasing the charge density would decrease astringency. Chitosans with fraction of acetylated units (FA) ranging from 0.01 to 0.49 (percentage degree of acetylation from 1 to 49) were analyzed for astringency using a time intensity sensory method. In addition, the ability of chitosans to precipitate saliva proteins was determined. Increasing FA from 0.01 to 0.49 caused a decrease in maximum astringency sensation from 10.9 to 7.2. Mucins and other saliva proteins were precipitated by chitosans but a simple association with astringency intensity was not observed. It can be concluded that altering the charge density of chitosans is a means to alter chitosan astringency.}, journal={FOOD HYDROCOLLOIDS}, author={Luck, Paige and Varum, Kjell M. and Foegeding, E. Allen}, year={2015}, month={Jun}, pages={174–178} }
 @article{uram-tuculescu_cooper_foegeding_vinyard_de kok_essick_2015, title={Electromyographic Evaluation of Masticatory Muscles in Dentate Patients Versus Conventional and Implant-Supported Fixed and Removable Denture Wearers- A Preliminary Report Comparing Model Foods}, volume={28}, ISSN={["1942-4426"]}, DOI={10.11607/ijp.3931}, abstractNote={PURPOSE
To evaluate differences in masticatory muscle function during chewing of model foods designed to differ in fracture strength between dentate subjects (n = 5, ages 59 to 68 years) versus patients treated with a maxillary conventional complete denture opposing natural dentition or one of the following types of mandibular complete dentures: conventional, implant-supported overdenture, implant-supported fixed denture (n = 20, ages 45 to 83 years). The authors hypothesized that denture wearers would differ in duration of chewing, frequency of chewing, and masticatory muscle activity while preparing a bolus for swallowing.


MATERIALS AND METHODS
Surface electromyography was recorded bilaterally from the masseter, anterior temporalis, and anterior digastric. Masticatory muscle activity was evaluated using scaled values of the area under the electromyographic curve, while subjects chewed agar-based model foods with different fracture strengths. Chewing duration and frequency also were calculated from electromyographic recordings. Mixed model analysis of variance with "subject" as a random factor was used during statistical analysis. Logarithmic transformation was required to achieve normalization of residuals for the duration of chewing and the relative masticatory muscles activity, but not for the chewing frequency.


RESULTS
Relative masticatory muscle activity was 2.57 times higher for the denture wearers than for the dentate subjects during chewing of model foods (P < .0001). The reduction in masticatory muscle activity from the 1st to the 10th chewing cycle was proportionally less in magnitude and occurred more gradually for denture wearers compared to dentate subjects. While chewing sequence duration increased with food fracture strength, it did not differ significantly in treatment versus dentate groups. Chewing cycle frequency did not differ between groups or with food fracture strength.


CONCLUSIONS
The observed increases in relative masticatory muscle activity for denture wearers compared to the dentate subjects during oral food processing likely reflect supplemental mechanical efforts to accommodate the use of dentures for preparing a bolus for swallowing.}, number={1}, journal={INTERNATIONAL JOURNAL OF PROSTHODONTICS}, author={Uram-Tuculescu, Sorin and Cooper, Lyndon F. and Foegeding, E. Allen and Vinyard, Christopher J. and De Kok, Ingeborg J. and Essick, Gregory}, year={2015}, pages={79–92} }
 @article{foegeding_2015, title={Food Protein Functionality-A New Model}, volume={80}, ISSN={["1750-3841"]}, DOI={10.1111/1750-3841.13116}, abstractNote={Abstract}, number={12}, journal={JOURNAL OF FOOD SCIENCE}, author={Foegeding, E. Allen}, year={2015}, month={Dec}, pages={C2670–C2677} }
 @article{ryan_foegeding_2015, title={Formation of soluble whey protein aggregates and their stability in beverages}, volume={43}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2014.05.025}, abstractNote={The objectives of this work were to 1) determine the role of pH in forming thermally stable whey protein isolate (WPI) soluble aggregates (SA), 2) evaluate the functionality of SA formed under a range of conditions, and 3) evaluate SA stability in a model beverage. Whey protein isolate SA were formed using two sources of WPI at pH 6.5 or 7.5, and thermal stability was tested in the presence of 30–60 mM NaCl or 15–30 mM CaCl2. Soluble aggregates from the two sources of WPI exhibited physicochemical and functional differences over the range of conditions investigated. Soluble aggregates formed at pH 7.5, 7% w/w protein, by heating statically at 90 °C for 10 min exhibited lower turbidity and viscosity, and higher solubility when thermally treated in solutions containing salt for both types of WPI, and were more sensitive to CaCl2. Soluble aggregates and a model beverage containing the SA were prepared at pilot scale and evaluated for shelf stability. Soluble aggregates were formed under continuous flow at pH 6.5, 7% w/w WPI, added at 5% w/w to the beverage, and thermally processed. Over nine weeks of storage at 22.5 °C, the beverage with SA had lower turbidity, aggregate size, and viscosity; and the aggregates had a more negative zeta potential. Results indicate that SA can be used to improve thermal and storage stability in beverages containing salts, and that solution and heating conditions can be optimized for improved thermal stability.}, journal={FOOD HYDROCOLLOIDS}, author={Ryan, Kelsey N. and Foegeding, E. Allen}, year={2015}, month={Jan}, pages={265–274} }
 @article{barden_osborne_mcmahon_foegeding_2015, title={Investigating the filled gel model in Cheddar cheese through use of Sephadex beads}, volume={98}, ISSN={["1525-3198"]}, DOI={10.3168/jds.2014-8597}, abstractNote={Cheese can be modeled as a filled gel whereby milkfat globules are dispersed in a casein gel network. We determined the filler effects using Sephadex beads (GE Healthcare Life Sciences, Pittsburgh, PA) as a model filler particle. Ideally, such a model could be used to test novel filler particles to replace milkfat in low-fat cheese. Low-filler (6% particles), reduced-filler (16%), and full-filler (33%) cheeses were produced using either Sephadex beads of varying sizes (20 to 150 μm diameter) or milkfat. Small- and large-strain rheological tests were run on each treatment at 8, 12, and 18 wk after cheese manufacturing. Differences in rheological properties were caused primarily by the main effects of filler volume and type (milkfat vs. Sephadex), whereas filler size had no obvious effect. All treatments showed a decrease in deformability and an increase in firmness as filler volume increased above 25%, although the beads exhibited a greater reinforcing effect and greater energy recovery than milkfat.}, number={3}, journal={JOURNAL OF DAIRY SCIENCE}, author={Barden, L. M. and Osborne, J. A. and McMahon, D. J. and Foegeding, E. A.}, year={2015}, month={Mar}, pages={1502–1516} }
 @article{plundrich_white_dean_davis_foegeding_lila_2015, title={Stability and immunogenicity of hypoallergenic peanut protein-polyphenol complexes during in vitro pepsin digestion}, volume={6}, ISSN={["2042-650X"]}, DOI={10.1039/c5fo00162e}, abstractNote={Allergenic peanut proteins are relatively resistant to digestion, and if digested, metabolized peptides tend to remain large and immunoreactive, triggering allergic reactions in sensitive individuals.}, number={7}, journal={FOOD & FUNCTION}, author={Plundrich, Nathalie J. and White, Brittany L. and Dean, Lisa L. and Davis, Jack P. and Foegeding, E. Allen and Lila, Mary Ann}, year={2015}, pages={2145–2154} }
 @article{qiu_smith_foegeding_drake_2015, title={The effect of microfiltration on color, flavor, and functionality of 80% whey protein concentrate}, volume={98}, DOI={10.3168/jds.2014-9174}, abstractNote={The residual annatto colorant in fluid Cheddar cheese whey is bleached to provide a neutral-colored final product. Currently, hydrogen peroxide (HP) and benzoyl peroxide are used for bleaching liquid whey. However, previous studies have shown that chemical bleaching causes off-flavor formation, mainly due to lipid oxidation and protein degradation. The objective of this study was to evaluate the efficacy of microfiltration (MF) on norbixin removal and to compare flavor and functionality of 80% whey protein concentrate (WPC80) from MF whey to WPC80 from whey bleached with HP or lactoperoxidase (LP). Cheddar cheese whey was manufactured from colored, pasteurized milk. The fluid whey was pasteurized and fat separated. Liquid whey was subjected to 4 different treatments: control (no bleaching; 50°C, 1 h), HP (250 mg of HP/kg; 50°C, 1 h), and LP (20 mg of HP/kg; 50°C, 1 h), or MF (microfiltration; 50°C, 1 h). The treated whey was then ultrafiltered, diafiltered, and spray-dried to 80% concentrate. The entire experiment was replicated 3 times. Proximate analyses, color, functionality, descriptive sensory and instrumental volatile analysis were conducted on WPC80. The MF and HP- and LP-bleached WPC80 displayed a 39.5, 40.9, and 92.8% norbixin decrease, respectively. The HP and LP WPC80 had higher cardboard flavors and distinct cabbage flavor compared with the unbleached and MF WPC80. Volatile compound results were consistent with sensory results. The HP and LP WPC80 were higher in lipid oxidation compounds (especially heptanal, hexanal, pentanal, 1-hexen-3-one, 2-pentylfuran, and octanal) compared with unbleached and MF WPC80. All WPC80 had >85% solubility across the pH range of 3 to 7. The microstructure of MF gels determined by confocal laser scanning showed an increased protein particle size in the gel network. MF WPC80 also had larger storage modulus values, indicating higher gel firmness. Based on bleaching efficacy comparable to chemical bleaching with HP, flavor, and functionality results, MF is a viable alternative to chemical or enzymatic bleaching of fluid whey.}, number={9}, journal={Journal of Dairy Science}, author={Qiu, Y. and Smith, T. J. and Foegeding, E. A. and Drake, M. A.}, year={2015}, pages={5862–5873} }
 @article{foegeding_vinyard_essick_guest_campbell_2015, title={Transforming Structural Breakdown into Sensory Perception of Texture}, volume={46}, ISSN={["1745-4603"]}, DOI={10.1111/jtxs.12105}, abstractNote={Abstract}, number={3}, journal={JOURNAL OF TEXTURE STUDIES}, author={Foegeding, E. Allen and Vinyard, Christopher J. and Essick, Gregory and Guest, Steve and Campbell, Caroline}, year={2015}, month={Jun}, pages={152–170} }
 @article{wagoner_ward_foegeding_2015, title={Using State Diagrams for Predicting Colloidal Stability of Whey Protein Beverages}, volume={63}, ISSN={["1520-5118"]}, DOI={10.1021/acs.jafc.5b00633}, abstractNote={A method for evaluating aspects of colloidal stability of whey protein beverages after thermal treatment was established. Three state diagrams for beverages (pH 3-7) were developed representing protein solubility, turbidity, and macroscopic state after two ultrahigh-temperature (UHT) treatments. Key transitions of stability in the state diagrams were explored using electrophoresis and chromatography to determine aggregation propensities of β-lactoglobulin, α-lactalbumin, bovine serum albumin, and glycomacropeptide. The state diagrams present an overlapping view of high colloidal stability at pH 3 accompanied by high solubility of individual whey proteins. At pH 5, beverages were characterized by poor solubility, high turbidity, and aggregation/gelation of whey proteins with the exception of glycomacropeptide. Stability increased at pH 6, due to increased solubility of α-lactalbumin. The results indicate that combinations of state diagrams can be used to identify key regions of stability for whey protein containing beverages.}, number={17}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Wagoner, Ty B. and Ward, Loren and Foegeding, E. Allen}, year={2015}, month={May}, pages={4335–4344} }
 @misc{mil_foegeding_windhab_perrot_linden_2014, title={A complex system approach to address world challenges in food and agriculture}, volume={40}, ISSN={["1879-3053"]}, DOI={10.1016/j.tifs.2014.07.005}, abstractNote={The quality and amount of the world food supply is crucial to the well-being of every human on the planet in the basic sense that we need food to live. It also has a profound impact on world economy, international trade, and global political stability. The choice of land used for agriculture, and the livestock and plants raised on the land, will impact the sustainable use of global resources. On a global scale, there are communities where insufficient food causes nutritional deficiencies, and at the same time, there are other communities eating too much food leading to obesity. Both conditions have accompanying diseases with associated financial consequences. The above issues relate to various scales, from local to global, and to a range of scientific disciplines. Moreover, their various elements are part of an interdependent, continuously changing, and adaptive system. This implies that the response of a combination of individual elements cannot usually be inferred from the response of each individual element or subsystem. This makes the identification of an appropriate intervention to change one or more elements a complex problem. We propose that a complex system approach should be used to address the global challenges of the agriculture and food system. The complex system approach accounts for the needs of stakeholders and policymakers in the agriculture and food system, and helps to determine which research programs will enable stakeholders to better anticipate and respond to emerging developments in the world. Moreover, the approach will enable them to determine effective intervention strategies to simultaneously optimise and safeguard their interests and the interests of the environment. The approach is formulated in terms of a roadmap of procedures. It encompasses an array of methods utilised in an integrative multi-scale and inter-disciplinary way.}, number={1}, journal={TRENDS IN FOOD SCIENCE & TECHNOLOGY}, author={Mil, H. G. J. and Foegeding, E. A. and Windhab, E. J. and Perrot, N. and Linden, E.}, year={2014}, month={Nov}, pages={20–32} }
 @article{koc_cakir_vinyard_essick_daubert_drake_osborne_foegeding_2014, title={ADAPTATION OF ORAL PROCESSING TO THE FRACTURE PROPERTIES OF SOFT SOLIDS}, volume={45}, ISSN={["1745-4603"]}, DOI={10.1111/jtxs.12051}, abstractNote={Abstract}, number={1}, journal={JOURNAL OF TEXTURE STUDIES}, author={Koc, H. and Cakir, E. and Vinyard, C. J. and Essick, G. and Daubert, C. R. and Drake, M. A. and Osborne, J. and Foegeding, E. A.}, year={2014}, month={Feb}, pages={47–61} }
 @article{kehoe_foegeding_2014, title={The characteristics of heat-induced aggregates formed by mixtures of beta-lactoglobulin and beta-casein}, volume={39}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2014.01.019}, abstractNote={The role of β-casein as a molecular chaperone in modifying the aggregation of β-lactoglobulin was investigated. Using size-exclusion chromatography coupled with a multi-angle laser light scattering detector and dynamic light scattering, it was found that the size of the aggregates formed when β-casein was present was reduced. Transmission electron microscopy images showed that β-casein & β-lactoglobulin mixtures produced smaller globular aggregates, with more uniform size distribution, than β-lactoglobulin alone. The viscosity of the solutions after heat treatment was minimally altered by the presence of β-casein. The surface hydrophobicity of the aggregates formed when β-casein was present did not differ from those formed in β-lactoglobulin. β-Casein was present in all the aggregate fractions in significant quantities, suggesting the formation of mixed β-casein-β-lactoglobulin aggregates with a lower propensity for growth or forming secondary aggregates.}, journal={FOOD HYDROCOLLOIDS}, author={Kehoe, J. J. and Foegeding, E. A.}, year={2014}, month={Aug}, pages={264–271} }
 @article{kroger_foegeding_reynolds_2013, title={75 Years of IFT: Journal reviews and hypotheses}, volume={78}, number={11}, journal={Journal of Food Science}, author={Kroger, M. and Foegeding, E. A. and Reynolds, W. N.}, year={2013}, pages={III-} }
 @article{luck_vardhanabhuti_yong_laundon_barbano_foegeding_2013, title={Comparison of functional properties of 34% and 80% whey protein and milk serum protein concentrates}, volume={96}, ISSN={["0022-0302"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84882905470&partnerID=MN8TOARS}, DOI={10.3168/jds.2013-6617}, abstractNote={This study compared the functional properties of serum protein concentrate (SPC) with whey protein concentrate (WPC) made from the same milk and with commercial WPC. The experimental SPC and WPC were produced at 34% or 80% protein from the same lot of milk. Protein contents of WPC and SPC were comparable; however, fat content was much lower in SPC compared with WPC and commercial WPC. The effect of drying methods (freeze vs. spray drying) was studied for 34% WPC and SPC. Few differences due to drying method were found in turbidity and gelation; however, drying method made a large difference in foam formation for WPC but not SPC. Between pH 3 and 7, SPC was found to have lower turbidity than WPC; however, protein solubility was similar between SPC and WPC. Foaming and gelation properties of SPC were better than those of WPC. Differences in functional properties may be explained by differences in composition and extent of denaturation or aggregation.}, number={9}, journal={JOURNAL OF DAIRY SCIENCE}, author={Luck, P. J. and Vardhanabhuti, B. and Yong, Y. H. and Laundon, T. and Barbano, D. M. and Foegeding, E. A.}, year={2013}, month={Sep}, pages={5522–5531} }
 @article{koc_vinyard_essick_foegeding_2013, title={Food Oral Processing: Conversion of Food Structure to Textural Perception}, volume={4}, ISSN={["1941-1421"]}, DOI={10.1146/annurev-food-030212-182637}, abstractNote={ Food oral processing includes all muscle activities, jaw movements, and tongue movements that contribute to preparing food for swallowing. Simultaneously, during the transformation of food structure to a bolus, a cognitive representation of food texture is formed. These physiological signals detected during oral processing are highly complex and dynamic in nature because food structure changes continuously due to mechanical and biochemical breakdown coupled with the lubricating action of saliva. Multiple and different sensations are perceived at different stages of the process. Although much work has focused on factors that determine mechanical (e.g., rheological and fracture) and sensory properties of foods, far less attention has been paid to linking food transformations that occur during oral processing with sensory perception of texture. Understanding how food structure influences specific patterns of oral processing and how these patterns relate to specific textural properties and their cognitive representations facilitates the design of foods that are nutritious, healthy, and enjoyable. }, journal={ANNUAL REVIEW OF FOOD SCIENCE AND TECHNOLOGY, VOL 4}, author={Koc, H. and Vinyard, C. J. and Essick, G. K. and Foegeding, E. A.}, year={2013}, pages={237–266} }
 @misc{pascua_koc_foegeding_2013, title={Food structure: Roles of mechanical properties and oral processing in determining sensory texture of soft materials}, volume={18}, ISSN={["1879-0399"]}, DOI={10.1016/j.cocis.2013.03.009}, abstractNote={There is a desire to alter food composition to make foods healthier and at the same time not diminish sensory quality. This requires an understanding of key elements of food structure associated with texture perception. Texture, in part, is perceived during oral processing of food. Knowledge of structure–oral processing–texture interrelations could be utilized to develop or prevent specified textural attributes. Overall, the investigation of structure–oral processing–texture interrelations is just starting as a research focus. Factors including non-universal and inconsistent sensory terminology, omission of consideration for structural changes incurred by oral processes, and the lack of cross-disciplinary investigations hamper progress in this field. Consideration of these factors in future investigations on sensory texture will increase the applicability of their findings and bring us closer to understanding the contribution of food structure to sensory texture.}, number={4}, journal={CURRENT OPINION IN COLLOID & INTERFACE SCIENCE}, author={Pascua, Yvette and Koc, Hicran and Foegeding, E. Allen}, year={2013}, month={Aug}, pages={324–333} }
 @article{foegeding_2013, title={New direction for the journal of food science: Same goals, higher standards}, volume={78}, DOI={10.1111/j.1750-3841.12080}, abstractNote={As a runner who used to compete in races, it is interesting to see how records have changed over the years. A quick look at the Wkipedia entry for Marathon World Records produced the following information (http://en.wikipedia.org/wiki/ Marathon_world_record_progression). Jonny Hayes, an American, set the Marathon record in 1908 with a time of 2 hours 55 minutes and 18 seconds. I can fantasize that I could have run in that 1908 race and produced a respectable showing. Jump to present time, and the record is 2 hours 3 minutes and 38 seconds, set by Patrick Makau of Kenya at the 2011 Berlin Marathon. Most people cannot run a quarter mile at this pace; let alone 26.2 miles. It goes to show what focused training on an athletically gifted individual can do to improve athletic performance. There is a parallel in science. Each new publication should build on the foundation of knowledge found in the literature and add new information. This does not rule out the need for experiments that confirm a current hypothesis or scientific principle; however, a simple confirmation of experimental results without adding some element that is unique to the literature is often met with a rejection. The editors of the Journal of Food Science have just finished revising the Aim and Scope of the journal and the descriptions of appropriate material for individual sections (Concise Reviews and Hypotheses in Food Science; Food Chemistry; Food Engineering and Physical Properties; Food Microbiology and Safety; Sensory and Food Quality; Nanoscale Food Science, Engineering, and Technology; Health, Nutrition, and Food; and Toxicology and Chemical Food Safety). It should also be noted that the descriptions for our sister publications, Journal of Food Science Education and Comprehensive Reviews in Food Science and Food Safety, have also been revised. The intent was to clearly and precisely elucidate what is acceptable and unacceptable for publication. Like many journals, we receive far more manuscripts than we can publish. Based on previous submission levels, we will need to reject > 75% of the manuscripts submitted in 2013 to stay within our restrictions on number of pages for a yearly volume. This means that many manuscripts, with no flaws in experimental design or data interpretation, will be rejected because their findings were not new, were not unique, or had a minor impact on the science of food. Most people would agree that Science is one of the preeminent journals publishing original scientific articles. In determining if your manuscript is qualified to be published in Science, they provide the following information: “Science’s Mission: Science seeks to publish those papers that are most influential in their fields or across fields and that will significantly advance scientific understanding. Selected papers should present novel and broadly important data, syntheses, or concepts. They should merit the recognition by the scientific community and general public provided by publication in Science, beyond that provided by specialty journals.” (http://www.sciencemag.org/site/feature/ contribinfo/prep/gen_info.xhtml). To paraphrase Science’s mission to our specialty journal, the Journal of Food Science seeks to publish papers that are most influential in the array of specific fields (see list of sections above) comprising the broad discipline of Food Science. Selected papers should present novel and important data, syntheses, or concepts that broadly cover Food Science and are not specific to a limited audience. As an author, I am keenly aware of the disappointment in having a manuscript rejected for “not of sufficient impact for publication.” However, just as in running a marathon, the level of performance that merits recognition continues to increase. We are simply raising our standards to select the highest quality manuscripts. The editors of the Journal of Food Science are committed to make this the preeminent journal that covers the array of disciplines that is Food Science. Keep those good manuscripts coming in, and we will do our best to get them published.}, number={2}, journal={Journal of Food Science}, author={Foegeding, E. A.}, year={2013}, pages={VI-} }
 @article{melito_daubert_foegeding_2013, title={Relating Large Amplitude Oscillatory Shear and Food Behavior: Correlation of Nonlinear Viscoelastic, Rheological, Sensory and Oral Processing Behavior of Whey Protein Isolate/-Carrageenan Gels}, volume={36}, ISSN={["1745-4530"]}, DOI={10.1111/jfpe.12015}, abstractNote={Abstract}, number={4}, journal={JOURNAL OF FOOD PROCESS ENGINEERING}, author={Melito, H. S. and Daubert, C. R. and Foegeding, E. A.}, year={2013}, month={Aug}, pages={521–534} }
 @article{melito_daubert_foegeding_2013, title={Relationships between Nonlinear Viscoelastic Behavior and Rheological, Sensory and Oral Processing Behavior of Commercial Cheese}, volume={44}, ISSN={["1745-4603"]}, DOI={10.1111/jtxs.12021}, abstractNote={Abstract}, number={4}, journal={JOURNAL OF TEXTURE STUDIES}, author={Melito, H. S. and Daubert, C. R. and Foegeding, E. A.}, year={2013}, month={Aug}, pages={253–288} }
 @misc{ryan_zhong_foegeding_2013, title={Use of Whey Protein Soluble Aggregates for Thermal StabilityA Hypothesis Paper}, volume={78}, ISSN={["1750-3841"]}, DOI={10.1111/1750-3841.12207}, abstractNote={Abstract}, number={8}, journal={JOURNAL OF FOOD SCIENCE}, author={Ryan, Kelsey N. and Zhong, Qixin and Foegeding, Edward A.}, year={2013}, month={Aug}, pages={R1105–R1115} }
 @article{melito_daubert_foegeding_2012, title={Creep and large-amplitude oscillatory shear behavior of whey protein isolate/kappa-carrageenan gels}, volume={22}, number={6}, journal={Applied Rheology}, author={Melito, H. S. and Daubert, C. R. and Foegeding, E. A.}, year={2012}, pages={296–309} }
 @article{cakir_koc_vinyard_essick_daubert_drake_foegeding_2012, title={EVALUATION OF TEXTURE CHANGES DUE TO COMPOSITIONAL DIFFERENCES USING ORAL PROCESSING}, volume={43}, ISSN={["0022-4901"]}, DOI={10.1111/j.1745-4603.2011.00335.x}, abstractNote={ABSTRACTReplacement of ingredients or reformulating existing products can significantly change textural characteristics. Our aim was to investigate the effects of sensory input from different textures on adaptation of the chewing pattern. Jaw muscle activity and kinematic measures of mastication were collected by electromyography and a three‐dimensional jaw tracking system during chewing of Cheddar cheeses (varying fat content) and caramels (two levels of total fat and sweetened condensed milk). Reducing fat in cheese is associated with increased sensory firmness, springiness and decreased cohesiveness. Oral processing adjusted to decreased fat content with increased closing muscle (temporalis and masseter) activity, a shorter cycle duration and increased power stroke time. Increased adhesiveness in caramels was associated with increased closing and opening muscle activity, longer cycle duration and increased jaw movement. It was shown that changes in composition that produced changes in sensory texture change oral processing parameters of muscle activity and jaw movement.}, number={4}, journal={JOURNAL OF TEXTURE STUDIES}, author={Cakir, Esra and Koc, Hicran and Vinyard, Christopher J. and Essick, Gregory and Daubert, Christopher R. and Drake, Maryanne and Foegeding, E. Allen}, year={2012}, month={Aug}, pages={257–267} }
 @article{jervis_campbell_wojciechowski_foegeding_drake_barbano_2012, title={Effect of bleaching whey on sensory and functional properties of 80% whey protein concentrate}, volume={95}, ISSN={["1525-3198"]}, DOI={10.3168/jds.2011-4967}, abstractNote={Whey is a highly functional food that has found widespread use in a variety of food and beverage applications. A large amount of the whey proteins produced in the United States is derived from annatto-colored Cheddar cheese. Color from annatto is undesirable in whey and must be bleached. The objective of this study was to compare 2 commercially approved bleaching agents, benzoyl peroxide (BP) and hydrogen peroxide (HP), and their effects on the flavor and functionality of 80% whey protein concentrate (WPC80). Colored and uncolored liquid wheys were bleached with BP or HP, and then ultrafiltered, diafiltered, and spray-dried; WPC80 from unbleached colored and uncolored Cheddar whey were manufactured as controls. All treatments were manufactured in triplicate. The WPC80 were then assessed by sensory, instrumental, functionality, color, and proximate analysis techniques. The HP-bleached WPC80 were higher in lipid oxidation compounds (specifically hexanal, heptanal, octanal, nonanal, decanal, dimethyl disulfide, and 1-octen-3-one) and had higher fatty and cardboard flavors compared with the other unbleached and BP-bleached WPC80. The WPC80 bleached with BP had lower norbixin concentrations compared with WPC80 bleached with HP. The WPC powders differed in Hunter color values (L, a, b), with bleached powders being more white, less red, and less yellow than unbleached powders. Bleaching with BP under the conditions used in this study resulted in larger reductions in yellowness of the powders made from whey with annatto color than did bleaching with HP. Functionality testing demonstrated that whey bleached with HP treatments had more soluble protein after 10 min of heating at 90°C at pH 4.6 and pH 7 than the no-bleach and BP treatments, regardless of additional color. Overall, HP bleaching caused more lipid oxidation products and subsequent off-flavors compared with BP bleaching. However, heat stability of WPC80 was enhanced by HP bleaching compared with control or BP-bleached WPC80.}, number={6}, journal={JOURNAL OF DAIRY SCIENCE}, author={Jervis, S. and Campbell, R. and Wojciechowski, K. L. and Foegeding, E. A. and Drake, M. A. and Barbano, D. M.}, year={2012}, month={Jun}, pages={2848–2862} }
 @article{leksrisompong_lanier_foegeding_2012, title={Effects of Heating Rate and pH on Fracture and Water-Holding Properties of Globular Protein Gels as Explained by Micro-Phase Separation}, volume={77}, ISSN={["1750-3841"]}, DOI={10.1111/j.1750-3841.2011.02550.x}, abstractNote={Abstract:  The effect of heating rate and pH on fracture properties and held water (HW) of globular protein gels was investigated. The study was divided into 2 experiments. In the 1st experiment, whey protein isolate (WPI) and egg white protein (EWP) gels were formed at pH 4.5 and 7.0 using heating rates ranging from 0.1 to 35 °C/min and holding times at 80 °C up to 240 min. The 2nd experiment used one heating condition (80 °C for 60 min) and probed in detail the pH range of 4.5 to 7.0 for EWP gels. Fracture properties of gels were measured by torsional deformation and HW was measured as the amount of fluid retained after a mild centrifugation. Single or micro‐phase separated conditions were determined by confocal laser scanning microscopy. The effect of heating rate on fracture properties and HW of globular protein gels can be explained by phase stability of the protein dispersion and total thermal input. Minimal difference in fracture properties and HW of EWP gels at pH 4.5 compared with pH 7.0 were observed while WPI gels were stronger and had higher HW at pH 7.0 as compared to 4.5. This was due to a mild degree of micro‐phase separation of EWP gels across the pH range whereas WPI gels only showed an extreme micro‐phase separation in a narrow pH range. In summary, gel formation and physical properties of globular protein gels can be explained by micro‐phase separation.}, number={2}, journal={JOURNAL OF FOOD SCIENCE}, author={Leksrisompong, Phanin N. and Lanier, Tyre C. and Foegeding, E. Allen}, year={2012}, month={Feb}, pages={E60–E67} }
 @article{barden_drake_foegeding_2012, title={IMPACT OF SAMPLE THICKNESS ON DESCRIPTIVE TEXTURE ANALYSIS OF CHEDDAR CHEESE}, volume={27}, ISSN={["1745-459X"]}, DOI={10.1111/j.1745-459x.2012.00392.x}, abstractNote={Abstract}, number={4}, journal={JOURNAL OF SENSORY STUDIES}, author={Barden, L. M. and Drake, M. A. and Foegeding, E. A.}, year={2012}, month={Aug}, pages={286–293} }
 @article{cakir_vinyard_essick_daubert_drake_foegeding_2012, title={Interrelations among physical characteristics, sensory perception and oral processing of protein-based soft-solid structures}, volume={29}, ISSN={["0268-005X"]}, DOI={10.1016/j.foodhyd.2012.02.006}, abstractNote={Oral processing is essential in breaking down the physicochemical structure of the food and thus important to the sensory perception of food in the mouth. To have an understanding of protein-based, soft-solid texture perception, a multidisciplinary approach was applied that combined studies of food microstructure with mechanical properties, sensory evaluation, and oral physiology. Model foods were developed by combining ion-induced micro-phase separation and protein-polysaccharide phase separation and inversion. Activities of masseter, anterior temporalis and anterior digastric muscles during oral processing were recorded by electromyography (EMG), while jaw movement amplitudes, durations, and velocities were simultaneously collected by a three-dimensional jaw tracking system (JT-3D). Changes in the microstructure of mixed gels significantly altered the characteristics of the chewing sequence, including the muscle activities, number of chews, chewing duration and chewing frequency. Mechanical attributes related to structural breakdown and sensory perception of firmness were highly correlated with the amount of muscle activity required to transform the initial structure into a bolus ready for swallowing. Chewing frequency was linked to mechanical properties such as recoverable energy, fracture strain and water holding capacity of the gels. Increased adhesiveness and moisture release also resulted in slower chewing frequency. Evaluation of oral processing parameters at various stages (i.e., first cycle, first 5 cycles, and last 3 cycles) was found to be a useful method to investigate the dynamic nature of sensory perception at first bite, during chewing and after swallowing. The study showed that muscle activity and jaw movement can be used to understand the links between physical properties of foods and sensory texture.}, number={1}, journal={FOOD HYDROCOLLOIDS}, author={Cakir, Esra and Vinyard, Christopher J. and Essick, Gregory and Daubert, Christopher R. and Drake, MaryAnne and Foegeding, E. Allen}, year={2012}, month={Oct}, pages={234–245} }
 @article{ryan_vardhanabhuti_jaramillo_zanten_coupland_foegeding_2012, title={Stability and mechanism of whey protein soluble aggregates thermally treated with salts}, volume={27}, DOI={10.1016/j.foodhyd.2011.11.006}, abstractNote={The formation of whey protein aggregates, often termed soluble aggregates, with specific physicochemical properties has been shown to result in improved functionality in gels, foams, emulsions, encapsulation, films and coatings. This work evaluated the potential of whey protein soluble aggregates to improve thermal stability in the presence of salts and determine the mechanism of improved thermal stability. Solutions of whey protein isolate (WPI) or β-lactoglobulin (β-lg) (7% w/w, pH 6.8) were heated for 10 min at 90 °C to form soluble aggregates. Native proteins and soluble aggregates were diluted to 3% w/w in solutions containing 0–108 mM NaCl and thermally treated (90 °C, 5 min). Turbidity, solubility, and viscosity were evaluated, in addition to ζ-potential and So (surface hydrophobicity). Size exclusion chromatography coupled with multi-angle laser light scattering (SEC-MALLS) and dynamic light scattering were used to determine aggregate size and transmission electron microscopy (TEM) was used to evaluate aggregate shape. Use of soluble aggregates improved thermal stability due to their altered aggregate shape and higher charge, and resulted in final aggregates that were smaller and less dense, leading to reduced viscosity and turbidity, and increased solubility compared to native proteins. It is concluded that soluble aggregates formed under the appropriate conditions to produce the desirable physicochemical properties can be used to improve whey protein thermal stability with a possible application in beverages.}, number={2}, journal={Food Hydrocolloids}, author={Ryan, K. N. and Vardhanabhuti, B. and Jaramillo, D. P. and Zanten, J. H. and Coupland, J. N. and Foegeding, E. A.}, year={2012}, pages={411–420} }
 @article{cakir_daubert_drake_vinyard_essick_foegeding_2012, title={The effect of microstructure on the sensory perception and textural characteristics of whey protein/kappa-carrageenan mixed gels}, volume={26}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2011.04.011}, abstractNote={The objective of the study was to understand how physical and structural properties of food translate into sensory perception. A range of gels with different structures were developed by combined mechanisms of ion-induced micro-phase separation of whey proteins, whey protein/к-carrageenan phase separation and network inversion. Descriptive sensory analysis was used to assess textural attributes of gels during the oral processing phases of first compression by tongue, first bite, mastication, and post swallow. Large deformation properties and fracture behavior of the gels were determined by uniaxial compression and single-edge notched bend tests. Mechanical properties at varying stages of deformation (before, during and after fracture) and sensory properties at different stages of oral processing (first compression, first bite and after 5–8 chews) followed similar trends based on the change in microstructure. Recoverable energies of gels were in agreement with springiness and compressibility evaluated at first compression in the mouth before biting. Young’s modulus together with fracture properties, including critical energy release rate and fracture toughness, varied among different microstructures along with firmness. After the fracture point, the speed of macroscopic breakdown determined the fracture type of the gels, which was related to the degree of fracturability at the first bite. Overall, five out of six microstructures were discriminated in sensory texture properties. It was demonstrated that defined physical and sensorial properties of soft-solid foods can be generated by modifying the gel microstructure through colloidal interactions.}, number={1}, journal={FOOD HYDROCOLLOIDS}, author={Cakir, Esra and Daubert, Christopher R. and Drake, Mary Anne and Vinyard, Christopher J. and Essick, Gregory and Foegeding, E. Allen}, year={2012}, month={Jan}, pages={33–43} }
 @article{cakir_khan_foegeding_2012, title={The effect of pH on gel structures produced using protein-polysaccharide phase separation and network inversion}, volume={27}, ISSN={["0958-6946"]}, DOI={10.1016/j.idairyj.2012.03.013}, abstractNote={Forming heat-induced gels through combined effects of micro-phase separation of whey protein isolate (WPI; 5%, w/v, 100 mm NaCl) by pH change (5.5, 6.0, and 6.5), and addition of κ-carrageenan (0–0.3%, w/w), were evaluated. The microstructure of WPI gels was homogeneous at pH 6.0 and 6.5 and micro-phase separated at pH 5.5. Addition of 0.075% κ-carrageenan to WPI solutions caused the microstructure of the gel to switch from homogeneous (pH 6.0 and 6.5) to micro-phase separated; and higher concentrations led to inversion of the continuous network from protein to κ-carrageenan. Protein solutions containing 0.075% (w/w) κ-carrageenan produced gels with increased storage modulus (G′) at pH 6.5 and decreased G′ at pH 5.5. All gels containing 0.3% (w/w) κ-carrageenan had κ-carrageenan-continuous networks. It was shown that microstructural and rheological changes were different in WPI and κ-carrageenan mixed gels when micro-phase separation was caused by pH rather than ionic strength.}, number={1-2}, journal={INTERNATIONAL DAIRY JOURNAL}, author={Cakir, Esra and Khan, Saad A. and Foegeding, E. Allen}, year={2012}, month={Dec}, pages={99–102} }
 @article{melito_daubert_foegeding_2012, title={Validation of a large amplitude oscillatory shear protocol}, volume={113}, ISSN={["0260-8774"]}, DOI={10.1016/j.jfoodeng.2012.05.008}, abstractNote={Oscillatory shear rheology plays a valuable role in assessing rheological properties of viscoelastic materials. In the linear viscoelastic region (LVR), the stress response to a strain input comprises only the first harmonic. Beyond the LVR, higher-order harmonics have significant contributions, which are not accounted for in the traditional calculation of viscoelastic moduli. Previous study has developed a mathematical framework that accounted for higher-order harmonics during large amplitude oscillatory shear (LAOS), yielding a physical interpretation to nonlinear data. However, this protocol was not formally validated with model elastic and viscous systems. To that end, a model elastic solid and viscous liquid were tested using LAOS to compare the protocol to standard oscillatory data and the known nonlinear properties of both systems. Good agreement (α = 0.05) was shown between first-order harmonic viscoelastic moduli data for both systems in the linear region. The protocol correctly indicated linear-to-nonlinear transitions of the elastic system, strain-independent linear behavior of the viscous system, and strain-hardening behavior of the elastic system in the nonlinear region. These results indicate the validity of the protocol, which may be applied to food systems to give valuable insights into nonlinear behavior and elucidate structural keys to texture design.}, number={1}, journal={JOURNAL OF FOOD ENGINEERING}, author={Melito, H. S. and Daubert, C. R. and Foegeding, E. A.}, year={2012}, month={Nov}, pages={124–135} }
 @misc{foegeding_daubert_drake_essick_trulsson_vinyard_velde_2011, title={A COMPREHENSIVE APPROACH TO UNDERSTANDING TEXTURAL PROPERTIES OF SEMI- AND SOFT-SOLID FOODS}, volume={42}, ISSN={["1745-4603"]}, DOI={10.1111/j.1745-4603.2011.00286.x}, abstractNote={ABSTRACTFoods such as starch‐ or gelatine‐based desserts, cheese, and processed meats are considered semi‐solid or soft‐solid, viscoelastic materials. Oral processing of these foods starts with either biting a portion from a larger piece or placing a piece in the mouth. Specific textural elements of a food are evaluated by descriptive sensory analysis; however, the time and costs of sensory analysis have motivated the empirical development of mechanical tests that correlate with sensory analysis of texture. While food scientists were evaluating mechanical properties to understand subjective texture, material scientists were developing rheological and fracture‐mechanics approaches to understand material properties in general. Still another group of scientists have focused on the biological mechanisms involved in mastication, oral processing and oral sensation. Understanding the integration of physical, physiological and psychophysical elements of soft‐solid food texture is a relative new area of research and therefore the current understanding of this multidisciplinary approach will be reviewed.}, number={2}, journal={JOURNAL OF TEXTURE STUDIES}, author={Foegeding, E. A. and Daubert, C. R. and Drake, M. A. and Essick, G. and Trulsson, M. and Vinyard, C. J. and Velde, F.}, year={2011}, month={Apr}, pages={103–129} }
 @article{cakir_foegeding_2011, title={Combining protein micro-phase separation and protein-polysaccharide segregative phase separation to produce gel structures}, volume={25}, ISSN={["0268-005X"]}, DOI={10.1016/j.foodhyd.2011.02.002}, abstractNote={The ability of protein micro-phase separation and protein–polysaccharide segregative phase separation to generate a range of gel structures and textures was evaluated. Whey protein isolate/κ-carrageenan mixed gels were prepared with 13% (w/v) whey protein isolate, 0–0.6% (w/w) κ-carrageenan and 50, 100 or 250 mM NaCl. The microstructure of gels, determined by confocal laser scanning microscopy, varied from homogenous to protein continuous, bicontinuous, coarse stranded or κ-carrageenan continuous, depending on the κ-carrageenan concentration. Microstructure also varied from stranded to particulate (micro-phase separated) depending on the salt concentration. The rheological behavior of mixed gels corresponded to the shift in the continuous phase from protein to κ-carrageenan. At small concentrations of κ-carrageenan, where carrageenan-rich droplets were dispersed in a continuous protein-rich matrix, gel strength (fracture stress) and firmness (G′) increased due to increased local concentration of proteins caused by phase separation. At higher κ-carrageenan concentrations, gels were substantially less firm, weaker and less deformable (fracture strain). The change in the continuous phase from protein continuous to carrageenan continuous explained the major change in mechanical properties and water-holding properties. The shift in microstructure occurred at lower concentrations of κ-carrageenan when whey proteins were under micro-phase separation conditions. The results demonstrated how the combined mechanisms of ion-induced micro-phase separation of proteins and protein–polysaccharide phase separation and inversion can be used to alter gel structure and texture.}, number={6}, journal={FOOD HYDROCOLLOIDS}, author={Cakir, Esra and Foegeding, E. Allen}, year={2011}, month={Aug}, pages={1538–1546} }
 @article{andrewes_kelly_vardhanabhuti_foegeding_2011, title={Dynamic modelling of whey protein-saliva interactions in the mouth and relation to astringency in acidic beverages}, volume={21}, ISSN={["1879-0143"]}, DOI={10.1016/j.idairyj.2011.02.011}, abstractNote={Whey proteins in acidic beverages (pH < 4.5) are astringent, producing a dry mouth-feel. Astringency is thought to be caused by interaction of food components with saliva, often leading to aggregate formation. Such interactions decrease saliva lubrication, form rough particles, and probably increase friction on oral surfaces – changing mouth-feel. Dynamic in vitro models were constructed to reproduce the likely interaction of whey proteins with saliva in the mouth during the course of beverage ingestion. Aggregate formation in the models was examined for numerous whey protein solutions under different conditions. Trends observed in the models were consistent with previous reported sensory evaluations of whey protein astringency. For example, maximum turbidity changed little in the models with increasing protein concentration, consistent with literature describing little increase in astringency with increasing protein concentration. Modelling mouth conditions, to measure protein–saliva interactions, related to astringency better than mixing saliva and protein in simple ratios.}, number={8}, journal={INTERNATIONAL DAIRY JOURNAL}, author={Andrewes, P. and Kelly, M. and Vardhanabhuti, B. and Foegeding, E. A.}, year={2011}, month={Aug}, pages={523–530} }
 @article{mudgal_daubert_clare_foegeding_2011, title={Effect of Disulfide Interactions and Hydrolysis on the Thermal Aggregation of beta-Lactoglobulin}, volume={59}, ISSN={["1520-5118"]}, DOI={10.1021/jf101893v}, abstractNote={The roles of sulfhydryl/disulfide interactions and acid/pepsin hydrolysis on β-lactoglobulin (β-lg) thermal aggregation at acidic pH 3.35 and 2 were studied using rheology, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), transmission electron microscopy (TEM), and Western blotting. Pepsin promoted additional hydrolysis compared to the acid-hydrolyzed control sample based on a 12% increase in free amino groups. Hydrolysis with pepsin also resulted in an increase in the apparent viscosity by 2 logs upon heating 8% β-lg solutions at pH 3.35. Seemingly, hydrolysis promoted thermal aggregation of β-lg, correlating well with viscosity increases. Large microgels were observed in heated pepsin hydrolysates using TEM, supporting the increased viscosities of these dispersions. During thermal aggregation (85 °C, 3 h) of β-lg at pH 3.35, beyond the existence of limited disulfide interactions, acid hydrolysis and noncovalent interactions more likely play a crucial role in defining the functionality of acidified powdered modified whey ingredients.}, number={5}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Mudgal, Prashant and Daubert, Christopher R. and Clare, Debra A. and Foegeding, E. Allen}, year={2011}, month={Mar}, pages={1491–1497} }
 @article{mudgal_daubert_foegeding_2011, title={Effects of protein concentration and CaCl2 on cold-set thickening mechanism of beta-lactoglobulin at low pH}, volume={21}, ISSN={["1879-0143"]}, DOI={10.1016/j.idairyj.2010.11.014}, abstractNote={Abstract Effects of protein concentration and CaCl2 on the cold-thickening mechanism of a pH-modified β-lactoglobulin (β-lg) ingredient were studied. Flexible fibrillar networks were formed at pH 3.35, and more branching was observed with an increase in CaCl2 equating to an increase of ionic strength (I) of 60 m m . This increase in ionic strength of β-lg solutions led to an increased conversion of monomers to aggregates (>106 Da), especially at concentrations above 6.9% (w/w), the critical concentration (Cc) for this modified protein system. A more connected flexible fibrillar network was observed following freeze-drying, with increased viscosities of rehydrated modified powders as compared with modified solutions prior to drying. A small increase in I (∼10 m M ) at concentrations greater than Cc resulted in improved thickening with similar network characteristics and thus provided an option for manipulation of protein and CaCl2 concentration to obtain improved thickening behavior.}, number={5}, journal={INTERNATIONAL DAIRY JOURNAL}, author={Mudgal, P. and Daubert, C. R. and Foegeding, E. A.}, year={2011}, month={May}, pages={319–326} }
 @article{foegeding_davis_2011, title={Food protein functionality: A comprehensive approach}, volume={25}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2011.05.008}, abstractNote={Food protein functionality has classically been viewed from the perspective of how single molecules or protein ingredients function in solutions and form simple colloidal structures. Based on this approach, tests on protein solutions are used to produce values for solubility, thermal stability, gelation, emulsifying, foaming, fat binding and water binding to name a few. While this approach is beneficial in understanding the properties of specific proteins and ingredients, it is somewhat restricted in predicting performance in real foods where the complexities of ingredients and processing operations have a significant affect on the colloidal structures and therefore overall properties of the final food product. In addition, focusing on proteins as just biopolymers used to create food structures ignores the biological functions of proteins in the diet. These can be beneficial, as in providing amino acids for protein synthesis or bioactive peptides, or these can be detrimental, as in causing a food allergic response. This review will focus on integrating the colloidal/polymer and biological aspects of protein functionality. This will be done using foams and gels to illustrate colloidal/polymer aspects and bioactive peptides and allergenicity to demonstrate biological function.}, number={8}, journal={FOOD HYDROCOLLOIDS}, author={Foegeding, E. Allen and Davis, Jack P.}, year={2011}, month={Dec}, pages={1853–1864} }
 @article{leksrisompong_foegeding_2011, title={How Micro-Phase Separation Alters the Heating Rate Effects on Globular Protein Gelation}, volume={76}, ISSN={["1750-3841"]}, DOI={10.1111/j.1750-3841.2011.02092.x}, abstractNote={Abstract:  This study was conducted to determine how the combination of heating rate and pH can be used to alter viscoelastic properties and microstructure of egg white protein and whey protein isolate gels. Protein solutions (1% to 7% w/v protein, pH 3.0 to 8.5) were heated using a range of heating rates (0.2 to 60 °C/min) to achieve a final temperature of 80 °C. The gelation process and viscoelastic properties of formed gels were evaluated using small strain rheology. Single phase or micro‐phase separated solution conditions were determined by confocal laser scanning microscopy. In the single phase region, gels prepared by the faster heating rates had the lowest rigidity at 80 °C; however, a common G′ was achieved after holding for 4 h at 80 °C . On the other hand, under micro‐phase separation conditions, faster heating rates allowed phase separated particles to be frozen in the network prior to precipitation. Thus, gels produced by slower heating rates had lower rigidities than gels produced by faster heating rates. The effect of heating rate appears to depend on if the solution is under single phase or micro‐phase separated conditions.}, number={3}, journal={JOURNAL OF FOOD SCIENCE}, author={Leksrisompong, Phanin N. and Foegeding, Edward Allen}, year={2011}, month={Apr}, pages={E318–E327} }
 @article{kehoe_foegeding_2011, title={Inverse model construction for control implementation of macro fiber composite actuators operating in hysteretic regimes}, volume={59}, number={1}, journal={Journal of Agricultural and Food Chemistry}, author={Kehoe, J. J. and Foegeding, E. A.}, year={2011}, pages={349–355} }
 @article{mudgal_daubert_foegeding_2011, title={Kinetic study of beta-lactoglobulin thermal aggregation at low pH}, volume={106}, ISSN={["0260-8774"]}, DOI={10.1016/j.jfoodeng.2011.04.025}, abstractNote={Kinetics of β-lactoglobulin (β-lg) thermal aggregation at pH 3.35, 85 °C, and 2–8% w/w protein concentration was studied using high performance liquid chromatography (HPLC) coupled with multi-angle laser light scattering (MALS) and rheology. Rate of β-lg aggregation was found to be of first order with respect to the initial protein concentration, and the conversion of native-like β-lg monomers/dimers (<36 kDa) to aggregates increased with initial concentration and heating times. The size of the aggregates formed during heating was dependent on the initial protein concentration. A simple nucleation and growth model was described for the β-lg aggregation at pH 3.35, where nucleation was found to be a rate limiting step below the previously identified critical concentration, Cc ∼ 6.4% protein. Above the Cc, nucleation occurred quickly and was not rate limiting. Critical size of the nucleus varied with protein concentration, with larger critical size needed at lower protein concentrations.}, number={2}, journal={JOURNAL OF FOOD ENGINEERING}, author={Mudgal, P. and Daubert, C. R. and Foegeding, E. A.}, year={2011}, month={Sep}, pages={159–165} }
 @article{vardhanabhuti_cox_norton_foegeding_2011, title={Lubricating properties of human whole saliva as affected by beta-lactoglobulin}, volume={25}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2011.02.021}, abstractNote={The effect of β-lactoglobulin (β-LG) at pH 3.5 and 7.0 on lubricating property of saliva as related to astringency perception was investigated using tribology. Saliva was adsorbed onto surfaces of a rotating poly dimethylsiloxane (PDMS) ball and disc to form a film under conditions that mimic the rubbing contacts in the oral cavity (Bongaerts, Rossetti, & Stokes, 2007) and the lubricity of saliva films upon exposure to astringent compounds was measured. While addition of non-astringent β-LG at pH 7.0 slowly increased friction of saliva film between tribopair surfaces, β-LG at pH 3.5 rapidly increased the friction coefficients of saliva, similar to other astringent compounds (epigallocatechin gallate and alum). This supports the hypothesis that astringency of β-LG arises from the loss of lubrication of saliva which is in agreement with the well-accepted astringency model of polyphenols. Increasing β-LG concentration at pH 3.5 (0.5–10% w/w) caused a rapid increase in friction coefficient; however, at the highest protein concentration, the friction coefficient, although higher than observed for water, was below the values observed for the lower protein concentrations. This suggests that static tribology testing is different from the dynamic in-mouth system such that a simple relationship between friction and sensory astringency cannot be found for all conditions.}, number={6}, journal={FOOD HYDROCOLLOIDS}, author={Vardhanabhuti, B. and Cox, P. W. and Norton, I. T. and Foegeding, E. A.}, year={2011}, month={Aug}, pages={1499–1506} }
 @article{yang_rogers_berry_foegeding_2011, title={MODELING THE RHEOLOGICAL PROPERTIES OF CHEDDAR CHEESE WITH DIFFERENT FAT CONTENTS AT VARIOUS TEMPERATURES}, volume={42}, ISSN={["1745-4603"]}, DOI={10.1111/j.1745-4603.2011.00283.x}, abstractNote={ABSTRACTCheddar cheese consists of a gel phase with imbedded fat particles and can be represented as a particle‐filled gel. The storage modulus (G′) of Cheddar cheese containing different fat contents was fitted to 12 theoretical models for particle‐filled gels. Models that included the G′ of fat particles and their interactions best described cheese G′. The estimated G′ of fat particle (Gf′) was larger than that of gel matrix (Gm′) at 10, 15 and 20C, corresponding to a reinforcing effect of fat on cheese G′. However, Gf′ decreased at a faster rate than Gm′ with increasing temperature, resulting in a weakening effect at 25C. Cheese rheological properties were dominated by the solid fat phase at 10 and 15C and showed no significant change with aging. In contrast, cheese G′ at 20 and 25C decreased after aging cheeses for 12 weeks, corresponding to decreases of Gm′ as a result of changes in the protein network.}, number={5}, journal={JOURNAL OF TEXTURE STUDIES}, author={Yang, Xin and Rogers, Neal Robert and Berry, Tristan Kendricks and Foegeding, Edward Allen}, year={2011}, month={Oct}, pages={331–348} }
 @article{tang_chen_foegeding_2011, title={Mechanical and Water-Holding Properties and Microstructures of Soy Protein Isolate Emulsion Gels Induced by CaCl2, Glucono-delta-lactone (GDL), and Transglutaminase: Influence of Thermal Treatments before and/or after Emulsification}, volume={59}, ISSN={["1520-5118"]}, DOI={10.1021/jf104834m}, abstractNote={The mechanical properties, water-holding capacities (WHC), and microstructures of emulsion gels, induced by glucono-δ-lactone (GDL), CaCl(2), and microbial transglutaminase (MTGase) from unheated and heated soy protein isolate (SPI)-stabilized emulsions (at protein concentration 5%, w/v; oil volume fraction, 20%, w/v), were investigated and compared. The influence of thermal pretreatments (at 90 °C for 5 min) before and/or after emulsification was evaluated. Considerable differences in mechanical, water-holding, and microstructural properties were observed among various emulsion gels. The thermal pretreatment after emulsification increased the strength of the emulsion gels induced by GDL and CaCl(2), whereas in the case of MTGase, thermal pretreatments before and/or after emulsification on the contrary greatly inhibited gel network formation. The application of the enzyme coagulant exhibited much higher potential to form SPI-stabilized emulsion gels with higher mechanical strength than that of the other two coagulants. The WHC of the emulsion gels seemed to be not directly related to their gel network strength. Confocal laser scanning microscope analyses indicated that the network microstructure of the formed emulsion gels, mainly composed of aggregated protein-stabilized oil droplets and protein aggregate clumps, varied with the type of applied coagulants and emulsions. The differences in microstructure were basically consistent with the differences in mechanical properties of the gels. These results could provide valuable information for the formation of cold-set soy protein-stabilized emulsion gels.}, number={8}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Tang, Chuan-He and Chen, Ling and Foegeding, Edward Allen}, year={2011}, month={Apr}, pages={4071–4077} }
 @article{tang_sun_foegeding_2011, title={Modulation of Physicochemical and Conformational Properties of Kidney Bean Vicilin (Phaseolin) by Glycation with Glucose: Implications for Structure-Function Relationships of Legume Vicilins}, volume={59}, ISSN={["1520-5118"]}, DOI={10.1021/jf202517f}, abstractNote={The structure-function relationships of plant oligomeric globulins are still not fully recognized. The present work investigated the influence of glycation with glucose (at 1:50 and 1:100 protein/sugar molar ratios; incubation periods of 2.5, 5.0, and 10.0 h) on the physicochemical and conformational properties of kidney bean vicilin (phaseolin), with the aim of understanding the structure-function relationships of legume vicilins. Protein solubility (PS), surface charge (isoelectric point) and hydrophobicity (H0), and secondary, tertiary, and/or quaternary conformations, as well as the emulsifying activities (emulsifying activity and emulsion stability indices, EAI and ESI) were evaluated. The 2.5 h incubation period of glycation led to least PS and highest H0, and after that, the PS and H0, on the contrary, gradually changed with increasing incubation period. The glycation increased the α-helix content and highly ordered secondary structures (α-helix+β-strand), as evidenced by far-UV circular dichroism (CD) spectroscopy. Combined analyses of differential scanning calorimetry, intrinsic emission fluorescence, and near-UV CD spectroscopy indicated that phaseolin underwent a tertiary conformation unfolding and subsequent rearrangement process (to form a new tertiary conformation), whereas the quaternary conformational flexibility progressively increased upon increasing degree of glycation. The conformation rearrangement was more distinct at the 1:100 molar ratio than at the 1:50 counterpart. The glycation at 5.0 and 10.0 h periods considerably increased the EAI, but only at the 1:50 molar ratio was the ESI progressively increased with the incubation period. These results confirmed that besides surface properties (e.g., PS and H0), the flexibility in tertiary and/or quaternary conformations played a major role in the emulsifying properties of glycated vicilins. The findings would have important implications for understanding the structure-function relationships of legume oligomeric globulins, thus providing a direction to further improve the surface-related functional properties of these proteins.}, number={18}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Tang, Chuan-He and Sun, Xin and Foegeding, Edward Allen}, year={2011}, month={Sep}, pages={10114–10123} }
 @article{yang_foegeding_2011, title={The stability and physical properties of egg white and whey protein foams explained based on microstructure and interfacial properties}, volume={25}, ISSN={["0268-005X"]}, DOI={10.1016/j.foodhyd.2011.03.008}, abstractNote={The goal of this investigation was to determine if physical models, based on micro-scale (bubbles) and nano-scale (interface) properties, can be used to explain the macroscopic foaming properties of egg white protein (EWP) and whey protein isolate (WPI). Foam properties were altered by adding different amounts of sucrose (4.27–63.6 g/100 mL) and microstructures were observed using confocal laser scanning microscopy and bubbles were quantitatively measured using image analysis. Addition of sucrose decreased the initial bubble size, corresponding to higher foam stability and lower air phase fraction. EWP foams were composed of smaller bubbles and lower air phase fractions than WPI foams. Increased sucrose concentration caused a decreased liquid drainage rate due to a higher continuous phase viscosity and smaller bubble sizes. WPI foams had faster rates for liquid drainage and bubble coarsening than EWP foams. The differences were attributed to faster bubble disproportionation in WPI foams, caused by lower interfacial elasticity and lower liquid phase fractions. The experimentally fitted parameters for foam yield stress did not follow universal trends and were protein type dependent. EWP foams had higher yield stress than WPI foams due to smaller bubble sizes and higher interfacial elasticity. The yield stress of WPI foams increased slightly with addition of sucrose and cannot be accounted for based solely on model parameters. It appears that changes in stability of EWP and WPI foams can be explained based on physical models while unaccounted for protein-specific effects remain regarding foam yield stress.}, number={7}, journal={FOOD HYDROCOLLOIDS}, author={Yang, Xin and Foegeding, E. Allen}, year={2011}, month={Oct}, pages={1687–1701} }
 @article{barden_cakir_leksrisompong_ryan_foegeding_drake_2010, title={EFFECT OF FLAVOR ON PERCEIVED TEXTURE OF WHEY PROTEIN ISOLATE GELS}, volume={25}, ISSN={["1745-459X"]}, DOI={10.1111/j.1745-459x.2010.00274.x}, abstractNote={ABSTRACT This study investigated the role of flavor on trained panelist and consumer perception of texture properties. Whey protein isolate (WPI) gels were prepared with sodium chloride (25 mM) at different pH (pH 6.0 or 7.0), and calcium chloride concentrations (0 or 10 mM). The same gel treatments were produced with and without added flavor. Instrumental torsion analysis showed that flavor addition had no impact (P > 0.05) on fracture stress and strain. Texture properties of gels were evaluated by a trained descriptive panel and untrained consumers (n = 60) for their perception of gel firmness, fracturability, juiciness, mouth coating and overall disliking. Distinct texture properties among the gels were documented by both trained panelists and consumers (P < 0.05). Flavor addition did not influence (P > 0.05) texture perception. Therefore, flavor addition does not impact panelist (trained or untrained) ability to evaluate textural differences in WPI gels.}, number={3}, journal={JOURNAL OF SENSORY STUDIES}, author={Barden, L. M. and Cakir, E. and Leksrisompong, P. N. and Ryan, K. N. and Foegeding, E. A. and Drake, M. A.}, year={2010}, month={Jun}, pages={447–462} }
 @article{yang_foegeding_2010, title={Effects of sucrose on egg white protein and whey protein isolate foams: Factors determining properties of wet and dry foams (cakes)}, volume={24}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2009.09.011}, abstractNote={The effects of sucrose on the physical properties of foams (foam overrun and drainage ½ life), air/water interfaces (interfacial dilational elastic modulus and interfacial pressure) and angel food cakes (cake volume and cake structure) of egg white protein (EWP) and whey protein isolate (WPI) was investigated for solutions containing 10% (w/v) protein. Increasing sucrose concentration (0–63.6 g/100 mL) gradually increased solution viscosity and decreased foam overrun. Two negative linear relationships were established between foam overrun and solution viscosity on a log–log scale for EWP and WPI respectively; while the foam overrun of EWP decreased in a faster rate than WPI with increasing solution viscosity (altered by sucrose). Addition of sucrose enhanced the interfacial dilational elastic modulus (E′) of EWP but reduced E′ of WPI, possibly due to different interfacial pressures. The foam drainage ½ life was proportionally correlated to the bulk phase viscosity and the interfacial elasticity regardless of protein type, suggesting that the foam destabilization changes can be slowed by a viscous continuous phase and elastic interfaces. Incorporation of sucrose altered the volume of angel food cakes prepared from WPI foams but showed no improvement on the coarse structure. In conclusion, sucrose can modify bulk phase viscosity and interfacial rheology and therefore improve the stability of wet foams. However, the poor stability of whey proteins in the conversion from a wet to a dry foam (angel food cake) cannot be changed with addition of sucrose.}, number={2-3}, journal={FOOD HYDROCOLLOIDS}, author={Yang, Xin and Foegeding, E. Allen}, year={2010}, pages={227–238} }
 @inproceedings{vardhanabhuti_foegeding_2010, title={Evidence of interactions between whey proteins and mucin their implication on the astringency mechanism of whey proteins at low pH}, booktitle={Gums and Stabilisers for the Food Industry 15}, author={Vardhanabhuti, B. and Foegeding, E. A.}, year={2010}, pages={137–146} }
 @article{vardhanabhuti_khayankan_foegeding_2010, title={Formation of Elastic Whey Protein Gels at Low pH by Acid Equilibration}, volume={75}, ISSN={["1750-3841"]}, DOI={10.1111/j.1750-3841.2010.01647.x}, abstractNote={Abstract:  Whey protein gels have a weak/brittle texture when formed at pH ≤ 4.5, yet this pH is required to produce a high‐protein, shelf‐stable product. We investigated if gels could be made under conditions that produced strong/elastic textural properties then adjusted to pH ≤ 4.5 and maintain textural properties. Gels were initially formed at 15% w/w protein (pH 7.5). Equilibration in acid solutions caused gel swelling and lowered pH because of the diffusion of water and H+ into the gels. The type and concentration of acid, and presence of other ions, in the equilibrating solutions influenced pH, swelling ratio, and fracture properties of the gels. Swelling of gels decreased fracture stress (because of decreased protein network density) but caused little change to fracture strain, thus maintaining a desirable strong/elastic fracture pattern. We have shown that whey protein isolate gels can be made at pH ≤ 4.5 with a strong/elastic fracture pattern and the magnitude of this pattern can be altered by varying the acid type, acid concentration, pH of equilibrating solution, and equilibrating time.}, number={5}, journal={JOURNAL OF FOOD SCIENCE}, author={Vardhanabhuti, Bongkosh and Khayankan, Worarat and Foegeding, E. Allen}, year={2010}, pages={E305–E313} }
 @article{rogers_mcmahon_daubert_berry_foegeding_2010, title={Rheological properties and microstructure of Cheddar cheese made with different fat contents}, volume={93}, ISSN={["1525-3198"]}, DOI={10.3168/jds.2010-3494}, abstractNote={Reduced- and low-fat cheeses are desired based on composition but often fall short on overall quality. One of the major problems with fat reduction in cheese is the development of a firm texture that does not break down during mastication, unlike that observed in full-fat cheeses. The objective of this investigation was to determine how the amount of fat affects the structure of Cheddar cheese from initial formation (2 wk) through 24 wk of aging. Cheeses were made with target fat contents of 3 to 33% (wt/wt) and moisture to protein ratios of 1.5:1. This allowed for comparisons based on relative amounts of fat and protein gel phases. Cheese microstructure was determined by confocal scanning laser microscopy combined with quantitative image analysis. Rheological analysis was used to determine changes in mechanical properties. Increasing fat content caused an increase in size of fat globules and a higher percentage of nonspherical globules. However, no changes in fat globules were observed with aging. Cheese rigidity (storage modulus) increased with fat content at 10°C, but differences attributable to fat were not apparent at 25°C. This was attributable to the storage modulus of fat approaching that of the protein gel; therefore, the amount of fat or gel phase did not have an effect on the cheese storage modulus. The rigidity of cheese decreased with storage and, because changes in the fat phase were not detected, it appeared to be attributable to changes in the gel network. It appeared that the diminished textural quality in low-fat Cheddar cheese is attributed to changes in the breakdown pattern during chewing, as altered by fat disrupting the cheese network.}, number={10}, journal={JOURNAL OF DAIRY SCIENCE}, author={Rogers, N. R. and McMahon, D. J. and Daubert, C. R. and Berry, T. K. and Foegeding, E. A.}, year={2010}, month={Oct}, pages={4565–4576} }
 @article{kelly_vardhanabhuti_luck_drake_osborne_foegeding_2010, title={Role of protein concentration and protein-saliva interactions in the astringency of whey proteins at low pH}, volume={93}, ISSN={["1525-3198"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-77952051521&partnerID=MN8TOARS}, DOI={10.3168/jds.2009-2853}, abstractNote={Whey protein beverages are adjusted to pH <4.5 to enhance clarity and stability, but this pH level is also associated with increased astringency. The goal of this investigation was to determine the effects of protein concentration on astringency and interactions between whey and salivary proteins. Whey protein beverages containing 0.25 to 13% (wt/wt) beta-lactoglobulin and 0.017% (wt/wt) sucralose at pH 2.6 to 4.2 were examined using descriptive sensory analysis. Controls were similar pH phosphate buffers at phosphate concentrations equivalent to the amount of phosphoric acid required to adjust the pH of the protein solution. Changes in astringency with protein concentration depended on pH. At pH 3.5, astringency significantly increased with protein concentration from 0.25 to 4% (wt/wt) and then remained constant from 4 to 13% (wt/wt). Conversely, at pH 2.6, astringency decreased with an increase in protein concentration [0.5-10% (wt/wt)]. This suggests a complex relationship that includes pH and buffering capacity of the beverages. Furthermore, saliva flow rates increased with increasing protein concentrations, showing that the physiological conditions in the mouth change with protein concentration. Maximum turbidity of whey protein-saliva mixtures was observed between pH 4.6 and 5.2. Both sensory evaluation and in vitro study of interactions between beta-LG and saliva indicate that astringency of whey proteins is a complex process determined by the extent of aggregation occurring in the mouth, which depends on the whey protein beverage pH and buffering capacity in addition to saliva flow rate.}, number={5}, journal={JOURNAL OF DAIRY SCIENCE}, author={Kelly, M. and Vardhanabhuti, B. and Luck, P. and Drake, M. A. and Osborne, J. and Foegeding, E. A.}, year={2010}, month={May}, pages={1900–1909} }
 @article{vardhanabhuti_kelly_luck_drake_foegeding_2010, title={Roles of charge interactions on astringency of whey proteins at low pH}, volume={93}, ISSN={["1525-3198"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-77952066147&partnerID=MN8TOARS}, DOI={10.3168/jds.2009-2780}, abstractNote={Whey proteins are a major ingredient in sports drink and functional beverages. At low pH, whey proteins are astringent, which may be undesirable in some applications. Understanding the astringency mechanism of whey proteins at low pH could lead to developing ways to minimize the astringency. This study compared the astringency of beta-lactoglobulin (beta-LG) at low pH with phosphate buffer controls having the same amount of phosphate and at similar pH. Results showed that beta-LG samples were more astringent than phosphate buffers, indicating that astringency was not caused by acid alone and that proteins contribute to astringency. When comparing among various whey protein isolates (WPI) and lactoferrin at pH 3.5, 4.5, and 7.0, lactoferrin was astringent at pH 7.0 where no acid was added. In contrast, astringency of all WPI decreased at pH 7.0. This can be explained by lactoferrin remaining positively charged at pH 7.0 and able to interact with negatively charged saliva proteins, whereas the negatively charged WPI would not interact. Charge interactions were further supported by beta-LG or lactoferrin and salivary proteins precipitating when mixed at conditions where beta-LG, lactoferrin, or saliva themselves did not precipitate. It can be concluded that interactions between positively charged whey proteins and salivary proteins play a role in astringency of proteins at low pH.}, number={5}, journal={JOURNAL OF DAIRY SCIENCE}, author={Vardhanabhuti, B. and Kelly, M. A. and Luck, P. J. and Drake, M. A. and Foegeding, E. A.}, year={2010}, month={May}, pages={1890–1899} }
 @article{leksrisompong_barbano_foegeding_gerard_drake_2010, title={THE ROLES OF FAT AND PH ON THE DETECTION THRESHOLDS AND PARTITION COEFFICIENTS OF THREE COMPOUNDS: DIACETYL, delta-DECALACTONE AND FURANEOL}, volume={25}, ISSN={["1745-459X"]}, DOI={10.1111/j.1745-459x.2009.00264.x}, abstractNote={ABSTRACT The effect of fat and pH on the best estimate threshold (BET) of three prominent dairy product flavor compounds with varying physicochemical properties: diacetyl (2, 3‐butanedione), δ‐decalactone and furaneol (2,5‐dimethyl‐4‐hydroxy‐3[2H]‐furanone), in water, oil and oil‐in‐water model emulsions (at 10 and 20% fat at neutral and acidified pH 5.5) were investigated. The headspace‐matrix partition coefficients (KHS/matrix) of each compound in the different matrixes were established using gas chromatography–mass spectrometry. The particle size of the emulsions was controlled. Fat had the largest impact on the BET and partition coefficients of δ‐decalactone followed by diacetyl (P ≤ 0.05). Fat content did not affect the BET value of furaneol (P > 0.05) but some effects on partition coefficients were noted (P ≤ 0.05). BET values of the three compounds were unaffected by pH (P > 0.05), but differences in partition coefficients (P ≤ 0.05) were noted for diacetyl and furaneol.}, number={3}, journal={JOURNAL OF SENSORY STUDIES}, author={Leksrisompong, Pattarin and Barbano, David M. and Foegeding, Allen E. and Gerard, Patrick and Drake, Maryanne}, year={2010}, month={Jun}, pages={347–370} }
 @article{foegeding_cakir_koc_2010, title={Using dairy ingredients to alter texture of foods: Implications based on oral processing considerations}, volume={20}, ISSN={["1879-0143"]}, DOI={10.1016/j.idairyj.2009.12.013}, abstractNote={Food quality is directly linked to the food's appearance, texture and flavor. All three components must be in harmony for the food to be considered delicious. Understanding how various textures can be designed requires a comprehensive approach of evaluating food structure, oral processing and sensory evaluation. Oral processing considers the physiological processes in first bite, mastication and swallowing. Sensory stimuli during oral processing are used to determine the acceptance of texture. Recent research has focused on how milk proteins can be used to create desirable textures. Whey protein–polysaccharide mixtures were used to show how microstructure can be manipulated to produce a range of textures and control water release. The importance of microstructure in determining a variety of texture terms was demonstrated in whey protein emulsion gels. Finally, fat content in Cheddar cheese was shown to be critical to producing a desirable breakdown pattern. These and other applications will be discussed.}, number={9}, journal={INTERNATIONAL DAIRY JOURNAL}, author={Foegeding, E. Allen and Cakir, Esra and Koc, Hicran}, year={2010}, month={Sep}, pages={562–570} }
 @article{mudgal_daubert_foegeding_2009, title={Cold-set thickening mechanism of beta-lactoglobulin at low pH: Concentration effects}, volume={23}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2009.03.009}, abstractNote={There is an interest in developing protein based thickening agents for nutritional considerations. A procedure to convert whey protein concentrates or isolates into a pH modified cold-thickening ingredient was developed. Concentration effects on thickening mechanism of this whey protein ingredient were studied with a β-lactoglobulin model system at the pH of the modification procedure, 3.35. In this study, concentration effects on thermal aggregation of β-lactoglobulin were studied at low pH using capillary and rotational viscometry, transmission electron microscopy (TEM), and high performance liquid chromatography coupled with multi-angle laser light scattering (HPLC-MALS). From the results of capillary viscometry, a critical concentration (Cc ∼ 6.9% w/w) was identified below which no significant thickening functionality could be achieved. Microscopy revealed formation of flexible fibrillar network at pH 3.35 during heating at all concentrations. These flexible fibrils had a diameter of about 5 nm and persistence length of about 35 nm as compared to more linear and stiff fibrils formed at pH 2 and low ionic strength conditions. Under similar heating conditions at concentration above Cc, larger aggregates similar to microgels were observed compared to the concentration below Cc, where isolated fibrils with an average contour length of about 130 nm were observed. These microgels and apparently stronger interactions between aggregates at concentrations above Cc were seemingly responsible for thickening functionality of heated β-lactoglobulin solutions and subsequently modified powders. Further investigation of β-lactoglobulin aggregation at this pH may provide capability to mechanistically tailor the functional attributes of modified ingredients.}, number={7}, journal={FOOD HYDROCOLLOIDS}, author={Mudgal, P. and Daubert, C. R. and Foegeding, E. A.}, year={2009}, month={Oct}, pages={1762–1770} }
 @article{yang_berry_foegeding_2009, title={Foams Prepared from Whey Protein Isolate and Egg White Protein: 1. Physical, Microstructural, and Interfacial Properties}, volume={74}, ISSN={["1750-3841"]}, DOI={10.1111/j.1750-3841.2009.01179.x}, abstractNote={ABSTRACT:  Foams were prepared from whey protein isolate (WPI), egg white protein (EWP), and combinations of the 2 (WPI/EWP), with physical properties of foams (overrun, drainage 1/2 life, and yield stress), air/water interfaces (interfacial tension and interfacial dilatational elasticity), and foam microstructure (bubble size and dynamic change of bubble count per area) investigated. Foams made from EWP had higher yield stress and stability (drainage 1/2 life) than those made from WPI. Foams made from mixtures of EWP and WPI had intermediate values. Foam stability could be explained based on solution viscosity, interfacial characteristics, and initial bubble size. Likewise, foam yield stress was associated with interfacial dilatational elastic moduli, mean bubble diameter, and air phase fraction. Foams made from WPI or WPI/EWP combinations formed master curves for stability and yield stress when normalized according to the above‐mentioned properties. However, EWP foams were excluded from the common trends observed for WPI and WPI/EWP combination foams. Changes in interfacial tension showed that even the lowest level of WPI substitution (25% WPI) was enough to cause the temporal pattern of interfacial tension to mimic the pattern of WPI instead of EWP, suggesting that whey proteins dominated the interface. The higher foam yield stress and drainage stability of EWP foams appears to be due to forming smaller, more stable bubbles, that are packed together into structures that are more resistant to deformation than those of WPI foams.}, number={5}, journal={JOURNAL OF FOOD SCIENCE}, author={Yang, Xin and Berry, Tristan K. and Foegeding, E. Allen}, year={2009}, pages={E259–E268} }
 @article{berry_yang_foegeding_2009, title={Foams Prepared from Whey Protein Isolate and Egg White Protein: 2. Changes Associated with Angel Food Cake Functionality}, volume={74}, ISSN={["1750-3841"]}, DOI={10.1111/j.1750-3841.2009.01178.x}, abstractNote={ABSTRACT:  The effects of sucrose on the physical properties and thermal stability of foams prepared from 10% (w/v) protein solutions of whey protein isolate (WPI), egg white protein (EWP), and their combinations (WPI/EWP) were investigated in wet foams and angel food cakes. Incorporation of 12.8 (w/v) sucrose increased EWP foam stability (drainage 1/2 life) but had little effect on the stability of WPI and WPI/EWP foams. Increased stability was not due to viscosity alone. Sucrose increased interfacial elasticity (E ′) of EWP and decreased E′ of WPI and WPI/EWP combinations, suggesting that altered interfacial properties increased stability in EWP foams. Although 25% WPI/75% EWP cakes had similar volumes as EWP cakes, cakes containing WPI had larger air cells. Changes during heating showed that EWP foams had network formation starting at 45 °C, which was not observed in WPI and WPI/EWP foams. Moreover, in batters, which are foams with additional sugar and flour, a stable foam network was observed from 25 to 85 °C for batters made from EWP foams. Batters containing WPI or WPI/EWP mixtures showed signs of destabilization starting at 25 °C. These results show that sucrose greatly improved the stability of wet EWP foams and that EWP foams form network structures that remain stable during heating. In contrast, sucrose had minimal effects on stability of WPI and WPI/EWP wet foams, and batters containing these foams showed destabilization prior to heating. Therefore, destabilization processes occurring in the wet foams and during baking account for differences in angel food cake quality.}, number={5}, journal={JOURNAL OF FOOD SCIENCE}, author={Berry, Tristan K. and Yang, Xin and Foegeding, E. Allen}, year={2009}, pages={E269–E277} }
 @article{vardhanabhuti_yucel_coupland_foegeding_2009, title={Interactions between beta-lactoglobulin and dextran sulfate at near neutral pH and their effect on thermal stability}, volume={23}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2008.09.006}, abstractNote={The effect of interactions between β-lactoglobulin (β-LG) and dextran sulfate (DS) on thermal stability at near neutral pH was investigated. Samples containing 6% w/w β-LG and DS (Mw = 5–500 kDa) at different biopolymer weight ratios, pH (5.6–6.2), and NaCl concentrations (0–30 mM) were heated at 85 °C for 15 min. Turbidity results showed that the presence of DS at appropriate biopolymer weight ratio and pH significantly lowered the turbidity of heated β-LG. Solutions containing DS:β-LG weight ratios of 0.02 or less showed improved heat stability as indicated by decreased turbidity. Analysis of the unheated mixture by size exclusion chromatography coupled with multi-angle laser light scattering (SEC–MALLS) showed an interaction between β-LG and DS. The size of the aggregates increased as pH decreased. The β-LG–DS aggregates had a greater negative charge as seen from electrophoretic mobility measurement. Addition of 30 mM NaCl inhibited complex formation and the effect of DS on reducing the turbidity of heated β-LG, suggesting that the interaction was electrostatic in nature. Other than charge property, the amount and size of native aggregates appeared to be the major factor in determining how DS altered heat-induced aggregation. The presence of DS decreased denaturation temperature of β-LG, indicating that DS did not improve thermal stability of β-LG by stabilizing its native state but rather by altering its aggregation. The results provide information that will facilitate the application of whey proteins and polysaccharides as functional ingredients in foods and beverages.}, number={6}, journal={FOOD HYDROCOLLOIDS}, author={Vardhanabhuti, Bongkosh and Yucel, Umut and Coupland, John N. and Foegeding, E. Allen}, year={2009}, month={Aug}, pages={1511–1520} }
 @misc{harrington_foegeding_mulvihill_morris_2009, title={Segregative interactions and competitive binding of Ca2+ in gelling mixtures of whey protein isolate with Na+ kappa-carrageenan}, volume={23}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2008.03.007}, abstractNote={Gelling mixtures of Na+ κ-carrageenan with whey protein isolate (WPI) at pH 7.0 have been studied rheologically and by differential scanning calorimetry (DSC), with comparative measurements for the individual constituents of the mixtures. The concentration of WPI was held fixed at 10.0 wt% and carrageenan concentration was varied in the range 0.05–3.0 wt%. Ca2+ cations, which have been shown previously to be particularly effective in inducing gelation of κ-carrageenan, were introduced as CaCl2. The concentration of CaCl2 used in most of the experiments was 8 mM, but other concentrations were also studied. Mixtures were prepared in the solution state at 45 °C, and showed no evidence of either phase separation or complex formation. Rheological changes were monitored by low-amplitude oscillatory measurements of storage modulus, G′, during (i) cooling (1 °C/min) and holding at 5 °C, to induce gelation of the carrageenan in the presence of non-gelled WPI; (ii) heating and holding at 80 °C to dissociate the carrageenan network and induce gelation of WPI; (iii) cooling and holding again at 5 °C, to give composite networks with both components gelled; and (iv) re-heating to 80 °C to dissociate the carrageenan network. Gel structure was characterised further by creep–recovery measurements at the end of each holding period, and by torsion measurements at 5 °C, before and after thermal gelation of WPI. In 8 mM CaCl2, the presence of 10.0 wt% WPI promoted earlier gelation of κ-carrageenan during cooling, and displaced the disorder–order transition in DSC to higher temperature. These changes are attributed to segregative interaction with non-gelled WPI. The resulting networks, however, were weaker that those formed by κ-carrageenan alone, which was traced to binding of Ca2+ cations to the WPI. At higher concentrations of CaCl2, where availability of Ca2+ cations was no longer a limiting factor in gelation of the κ-carrageenan, the effect of segregative interactions could be seen as an increase in gel strength. On heating to gel the WPI, the presence of κ-carrageenan led to the earlier appearance of an aggregation exotherm in DSC and to network formation at shorter times, which can similarly be explained by enhanced self-association of denatured WPI in response to segregative interactions with disordered carrageenan. An initial large (∼10 fold) increase in gel strength with increasing concentration of carrageenan to ∼0.25 wt% was followed by a reduction at higher concentrations, attributed to excessive aggregation (incipient precipitation) of the WPI. The magnitude of the changes in G′ observed on subsequent cooling suggest that gelation of κ-carrageenan within the pores of an existing network of gelled WPI gives rise to a bicontinuous co-gel structure. Comparison of moduli at 80 °C before and after cooling to 5 °C demonstrated that formation and dissociation of the carrageenan network caused no disruption of the network of gelled WPI.}, number={2}, journal={FOOD HYDROCOLLOIDS}, author={Harrington, J. C. and Foegeding, E. A. and Mulvihill, D. M. and Morris, E. R.}, year={2009}, month={Mar}, pages={468–489} }
 @article{rogers_drake_daubert_mcmahon_bletsch_foegeding_2009, title={The effect of aging on low-fat, reduced-fat, and full-fat Cheddar cheese texture}, volume={92}, ISSN={["1525-3198"]}, DOI={10.3168/jds.2009-2156}, abstractNote={This study investigated the effects of aging and fat content on the texture of Cheddar cheese, both mechanical and sensory aspects, over a 9-mo aging period. Cheeses of 6, 16, and 33% fat were tested at 0.5, 3, 6, and 9 mo of aging. Cheeses were evaluated by a trained sensory panel using an established texture lexicon as well as instrumental methods, which were used to probe cheese structure. Sensory analysis showed that low-fat cheeses were differentiated from full-fat cheeses by being more springy and firm and this difference widened as the cheeses aged. In addition, full-fat cheeses broke down more during chewing than the lower fat cheeses and the degree of breakdown increased with aging. Mechanical properties were divided by magnitude of deformation during the test and separated into 3 ranges: the linear viscoelastic region, the nonlinear region, and fracture point. These regions represent a stress/strain response from low to high magnitude, respectively. Strong relationships between sensory terms and rheological properties determined in the linear (maximum compliance) and nonlinear (critical stress and strain and a nonlinear shape factor) regions were revealed. Some correlations were seen with fracture values, but these were not as high as terms related to the nonlinear region of the cheeses. The correlations pointed to strain-weakening behavior being the critical mechanical property. This was associated with higher fat content cheeses breaking down more as strain increased up to fracture. Increased strain weakening associated with an increase in fat content was attributed to fat producing weak points in the protein network, which became initiation sites for fracture within the structure. This suggests that fat replacers need to serve this functional role.}, number={10}, journal={JOURNAL OF DAIRY SCIENCE}, author={Rogers, N. R. and Drake, M. A. and Daubert, C. R. and McMahon, D. J. and Bletsch, T. K. and Foegeding, E. A.}, year={2009}, month={Oct}, pages={4756–4772} }
 @article{zhang_daubert_mulligan_foegeding_2008, title={Additive effects on the rheological behavior of alginate gels}, volume={39}, DOI={10.1111/j.1745-4603.2008.00159.x}, abstractNote={ABSTRACT The effects of dextran and glycerol on the rheological properties of 1.25% alginate gels were studied. Although the dextran and glycerol dramatically changed the viscosity of the alginate solution, the gelation kinetics was not affected. This observation may be attributed to the fact that the gelling process was controlled by the combination of carboxylic groups in alginate chains with Ca2
          +
          , and not by the diffusion process of alginate molecules and Ca2
          +
          through the viscous medium. The small‐strain shear modulus of alginate gels with either low molecular‐weight dextran (MW: 140,000 Da) or glycerol remained nearly constant, as did the large deformation and fracture properties. The addition of high molecular‐weight dextran (MW: 4–5 million Da) altered the small‐strain shear modulus and lowered the gel fracture stress of the alginate gels, while the fracture strain remained the same. The change in small‐strain shear modulus and large deformation and fracture properties for alginate gels with high MW dextran cannot simply be explained by the change in viscosity of the gel liquid phase. A plausible explanation for this behavior is that, in some manner, large dextran molecules influenced the alginate gel network. }, number={5}, journal={Journal of Texture Studies}, author={Zhang, J. and Daubert, C. R. and Mulligan, J. H. and Foegeding, E. A.}, year={2008}, pages={582–603} }
 @article{yong_foegeding_2008, title={Effects of Caseins on Thermal Stability of Bovine beta-Lactoglobulin}, volume={56}, ISSN={["1520-5118"]}, DOI={10.1021/jf801658u}, abstractNote={Casein fractions have been shown to act as molecular chaperones and inhibit aggregation of whey proteins in dilute solutions (< or =1% w/v). We evaluated if this approach would stabilize protein solutions at higher concentration and thermal processing temperatures desired for beverage applications. Mixtures of beta-lactoglobulin (BLG) (6% w/v) with either beta-casein (BCN) (0.01-2% w/v) or alpha s-casein (ACN) (2% w/v) were adjusted to pH 6.0 and heated (70-90 degrees C) for 20 min, cooled, and then analyzed to determine the degree of aggregation. Aggregation was determined by solution turbidity as optical density (OD) at 400 or 600 nm. The addition of 0.05% (w/v) BCN or greater caused a drop in turbidity for solutions heated at 70-90 degrees C. In contrast, inhibition was observed in BLG-ACN mixtures at 70 degrees C but not at > or =75 degrees C. Moreover, prolonged heating (90 min) of BLG with 2% (w/v) BCN (pH 6.0) at 90 degrees C produced a clear solution while BLG-ACN solutions formed translucent gels after heating for 15 min. The weight-averaged molar mass and root-mean-square (rms) radius of soluble aggregates were determined by size exclusion chromatography in conjunction with multiangle laser light scattering (SEC-MALS). SEC-MALS confirmed the turbidity results by showing that the BLG-BCN mixture (8% w/v protein) produced aggregates with lower molar mass and smaller rms radius (majority 20-40 nm). These results showed that BCN is a feasible component to stabilize higher concentrations of whey proteins in beverages.}, number={21}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Yong, Yie Hui and Foegeding, E. Allen}, year={2008}, month={Nov}, pages={10352–10358} }
 @article{vardhanabhuti_foegeding_2008, title={Effects of dextran sulfate, NaCl, and initial protein concentration on thermal stability of beta-lactoglobulin and alpha-lactalbumin at neutral pH}, volume={22}, DOI={10.1016/j.foodhvd.2007.03.003}, number={5}, journal={Food Hydrocolloids}, author={Vardhanabhuti, B. and Foegeding, E. A.}, year={2008}, pages={752–762} }
 @article{beecher_drake_luck_foegeding_2008, title={Factors regulating astringency of whey protein beverages}, volume={91}, ISSN={["1525-3198"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-47149106271&partnerID=MN8TOARS}, DOI={10.3168/jds.2008-1083}, abstractNote={A rapidly growing area of whey protein use is in beverages. There are 2 types of whey protein-containing beverages: those at neutral pH and those at low pH. Astringency is very pronounced at low pH. Astringency is thought to be caused by compounds in foods that bind with and precipitate salivary proteins; however, the mechanism of astringency of whey proteins is not understood. The effect of viscosity and pH on the astringency of a model beverage containing whey protein isolate was investigated. Trained sensory panelists (n = 8) evaluated the viscosity and pH effects on astringency and basic tastes of whey protein beverages containing 6% wt/vol protein. Unlike what has been shown for alum and polyphenols, increasing viscosity (1.6 to 7.7 mPa.s) did not decrease the perception of astringency. In contrast, the pH of the whey protein solution had a major effect on astringency. A pH 6.8 whey protein beverage had a maximum astringency intensity of 1.2 (15-point scale), whereas that of a pH 3.4 beverage was 8.8 (15-point scale). Astringency decreased between pH 3.4 and 2.6, coinciding with an increase in sourness. Decreases in astringency corresponded to decreases in protein aggregation as observed by turbidity. We propose that astringency is related to interactions between positively charged whey proteins and negatively charged saliva proteins. As the pH decreased between 3.4 and 2.6, the negative charge on the saliva proteins decreased, causing the interactions with whey proteins to decrease.}, number={7}, journal={JOURNAL OF DAIRY SCIENCE}, author={Beecher, J. W. and Drake, M. A. and Luck, P. J. and Foegeding, E. A.}, year={2008}, month={Jul}, pages={2553–2560} }
 @article{luck_foegeding_2008, title={The role of copper in protein foams}, volume={3}, ISSN={["1557-1858"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-43749110248&partnerID=MN8TOARS}, DOI={10.1007/s11483-008-9060-0}, number={2}, journal={FOOD BIOPHYSICS}, author={Luck, Paige J. and Foegeding, Edward A.}, year={2008}, month={Jun}, pages={255–260} }
 @article{zhang_daubert_foegeding_2007, title={A proposed strain-hardening mechanism for alginate gels}, volume={80}, ISSN={["0260-8774"]}, DOI={10.1016/j.jfoodeng.2006.04.057}, abstractNote={The non-linear viscoelastic properties of alginate gels were investigated using torsion and compression rheological tests. Like many biopolymers, alginate gels showed strain-hardening behavior during large deformation, and the degree of strain-hardening depended on gel composition. The strain-hardening behavior of alginate gels was attributed to the deformation of rod-like junction zones serving as physical crosslinks in the gel. A constitutive equation based on the deformation of junction zones and a Gaussian distribution network of chains was developed to predict deformation behavior. The resulting equation effectively described the experimental data during torsion and compression, supporting the proposed mechanism that strain-hardening originates from the deformation of alginate junction zones.}, number={1}, journal={JOURNAL OF FOOD ENGINEERING}, author={Zhang, Junhua and Daubert, Christopher R. and Foegeding, E. Allen}, year={2007}, month={May}, pages={157–165} }
 @article{whetstine_luck_drake_foegeding_gerard_barbano_2007, title={Characterization of flavor and texture development within large (291 kg) blocks of Cheddar cheese}, volume={90}, ISSN={["1525-3198"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-35748980863&partnerID=MN8TOARS}, DOI={10.3168/jds.2006-755}, abstractNote={Cheddar cheese is a natural product that has a variable flavor and texture profile. Many companies produce 291-kg blocks of Cheddar cheese, which are subsequently cut and shipped, or stored and subsequently cut. Previous research has shown that compositional differences exist within 291-kg blocks and that these differences may influence flavor and texture development. The objectives of this study were to systematically characterize flavor and texture differences within 291-kg blocks. On 2 different occasions, a 291-kg block was manufactured at each of 4 manufacturing facilities. After 7 d, the 291-kg blocks were sliced into sixteen 18-kg sample portions using a predetermined diagram, and each portion was labeled appropriately (outer corner, inner corner, etc.) and stored at 7 degrees C. Cheese from different locations within the 291-kg blocks was evaluated at 1, 4, 8, and 12 mo. At each time point, two 18-kg portions representing an inside and outside location with the 291-kg block cross-section (from inside to outside) were sampled. The moisture content was lower in the inner than outer locations within the 291-kg blocks. Protein hydrolysis was higher in the inner location and inner locations developed aged Cheddar flavors sulfur, nutty, and brothy more rapidly than the outer locations. However, plant-to-plant differences in aging were often larger than differences caused by block location. These differences were due to differences in cheese manufacturing practices among plants. Dynamic headspace results for flavor volatiles were consistent with descriptive sensory flavor results, documenting differences between inner and outer locations within 291-kg blocks. The inner locations were more fracturable and the outer locations were more cohesive and had more residual in the mouth. Inner locations had greater fracture strain than outer locations. Documenting the differences in aging of 291-kg blocks of Cheddar cheese is important in understanding how to make a consistent high-quality Cheddar cheese.}, number={7}, journal={JOURNAL OF DAIRY SCIENCE}, author={Whetstine, M. E. Carunchia and Luck, P. J. and Drake, M. A. and Foegeding, E. A. and Gerard, P. D. and Barbano, D. M.}, year={2007}, month={Jul}, pages={3091–3109} }
 @article{davis_foegeding_2007, title={Comparisons of the foaming and interfacial properties of whey protein isolate and egg white proteins}, volume={54}, ISSN={["1873-4367"]}, DOI={10.1016/j.colsurfb.2006.10.017}, abstractNote={Whipped foams (10%, w/v protein, pH 7.0) were prepared from commercially available samples of whey protein isolate (WPI) and egg white protein (EWP), and subsequently compared based on yield stress (τ0), overrun and drainage stability. Adsorption rates and interfacial rheological measurements at a model air/water interface were quantified via pendant drop tensiometry to better understand foaming differences among the ingredients. The highest τ0 and resistance to drainage were observed for standard EWP, followed by EWP with added 0.1% (w/w) sodium lauryl sulfate, and then WPI. Addition of 25% (w/w) sucrose increased τ0 and drainage resistance of the EWP-based ingredients, whereas it decreased τ0 of WPI foams and minimally affected their drainage rates. These differing sugar effects were reflected in the interfacial rheological measurements, as sucrose addition increased the dilatational elasticity for both EWP-based ingredients, while decreasing this parameter for WPI. Previously observed relationships between τ0 and interfacial rheology did not hold across the protein types; however, these measurements did effectively differentiate foaming behaviors within EWP-based ingredients and within WPI. Interfacial data was also collected for purified β-lactoglobulin (β-lg) and ovalbumin, the primary proteins of WPI and EWP, respectively. The addition of 25% (w/w) sucrose increased the dilatational elasticity for adsorbed layers of β-lg, while minimally affecting the interfacial rheology of adsorbed ovalbumin, in contrast to the response of WPI and EWP ingredients. These experiments underscore the importance of utilizing the same materials for interfacial measurements as used for foaming experiments, if one is to properly infer interfacial information/mechanisms and relate this information to bulk foaming measurements. The effects of protein concentration and measurement time on interfacial rheology were also considered as they relate to bulk foam properties. This data should be of practical assistance to those designing aerated food products, as it has not been previously reported that sucrose addition improves the foaming characteristics of EWP-based ingredients while negatively affecting the foaming behavior of WPI, as these types of protein isolates are common to the food industry.}, number={2}, journal={COLLOIDS AND SURFACES B-BIOINTERFACES}, author={Davis, J. P. and Foegeding, E. A.}, year={2007}, month={Feb}, pages={200–210} }
 @article{childs_daubert_stefanski_foegeding_2007, title={Factors regulating cheese shreddability}, volume={90}, ISSN={["0022-0302"]}, DOI={10.3168/jds.2006-618}, abstractNote={Two sets of cheeses were evaluated to determine factors that affect shred quality. The first set of cheeses was made up of 3 commercial cheeses, Monterey Jack, Mozzarella, and process. The second set of cheeses was made up of 3 Mozzarella cheeses with varying levels of protein and fat at a constant moisture content. A shred distribution of long shreds, short shreds, and fines was obtained by shredding blocks of cheese in a food processor. A probe tack test was used to directly measure adhesion of the cheese to a stainless-steel surface. Surface energy was determined based on the contact angles of standard liquids, and rheological characterization was done by a creep and recovery test. Creep and recovery data were used to calculate the maximum and initial compliance and retardation time. Shredding defects of fines and adhesion to the blade were observed in commercial cheeses. Mozzarella did not adhere to the blade but did produce the most fines. Both Monterey Jack and process cheeses adhered to the blade and produced fines. Furthermore, adherence to the blade was correlated positively with tack energy and negatively with retardation time. Mozzarella cheese, with the highest fat and lowest protein contents, produced the most fines but showed little adherence to the blade, even though tack energy increased with fat content. Surface energy was not correlated with shredding defects in either group of cheese. Rheological properties and tack energy appeared to be the key factors involved in shredding defects.}, number={5}, journal={JOURNAL OF DAIRY SCIENCE}, author={Childs, J. L. and Daubert, C. R. and Stefanski, L. and Foegeding, E. A.}, year={2007}, month={May}, pages={2163–2174} }
 @article{rosell_foegeding_2007, title={Interaction of hydroxypropylmethylcellulose with gluten proteins: Small deformation properties during thermal treatment}, volume={21}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2006.08.003}, abstractNote={The possible interaction between hydroxypropylmethylcellulose (HPMC) and gluten proteins has been investigated in order to understand the effect of the HPMC in bakery products. Dynamic oscillatory studies at small deformations indicated that the presence of varying concentrations of HPMC induces a softening effect (decrease in G′ and G″) in the gluten dough. During heating of HMPC–gluten mixtures, HPMC gelation only became evident when a minimum amount of HPMC was present (HPMC/gluten ratio was 0.075), conferring some strength to the gluten dough at 85 °C. The presence of HPMC did not modify the viscoelastic behaviour of gluten dough during cooling, however, at 25 °C, increased G′ and G″ were observed with HPMC. Gluten proteins increased their solubility in sodium dodecyl sulphate in the presence of HPMC, which besides the viscoelastic results, suggests that HPMC could interfere with the protein association and its further aggregation during heating, likely occupying the space of the proteins in the gluten network. Therefore, separate from interactions of starch and HPMC, the HPMC effect on bakery products could be partially due to the functional replacement of the gluten proteins in the gluten network. This effect is intensified after HPMC gelation, and also modifies the protein self-association during baking.}, number={7}, journal={FOOD HYDROCOLLOIDS}, author={Rosell, Cristina M. and Foegeding, Allen}, year={2007}, month={Oct}, pages={1092–1100} }
 @misc{foegeding_drake_2007, title={Invited review: Sensory and mechanical properties of cheese texture}, volume={90}, ISSN={["1525-3198"]}, DOI={10.3168/jds.2006-703}, abstractNote={Instrumental mechanical properties (instrumental tests that measure force and deformation over time) of cheese and cheese texture (sensory perception of cheese structure) are critical attributes. Accurate measurement of these properties requires both instrumental and sensory testing. Fundamental rheological and fracture tests provide accurate measurement of mechanical properties that can be described based on chemical and structural models. Sensory testing likewise covers a range of possible tests with selection of the specific test dependent of the specific goal desired. Establishing relationships between instrumental and sensory tests requires careful selection of tests and consideration and analysis of the results. A review of these tests and a critical analysis of establishing relationships between instrumental and sensory tests is presented.}, number={4}, journal={JOURNAL OF DAIRY SCIENCE}, author={Foegeding, E. A. and Drake, M. A.}, year={2007}, month={Apr}, pages={1611–1624} }
 @misc{foegeding_2007, title={Rheology and sensory texture of biopolymer gels}, volume={12}, ISSN={["1359-0294"]}, DOI={10.1016/j.cocis.2007.07.001}, abstractNote={Sensory texture perception is based on food structure and the mastication process. Real-time observations of crack growth and rheological measurements have shown different patterns of microstructural fracture. This has allowed for a reductive approach in consolidating a range of gels into characteristic microstructures and fracture patterns that can be linked to sensory texture.}, number={4-5}, journal={CURRENT OPINION IN COLLOID & INTERFACE SCIENCE}, author={Foegeding, E. Allen}, year={2007}, month={Oct}, pages={242–250} }
 @article{mcguffey_otter_zanten_foegeding_2007, title={Solubility and aggregation of commercial alpha-lactalbumin at neutral pH}, volume={17}, ISSN={["1879-0143"]}, DOI={10.1016/j.idairyj.2007.04.003}, abstractNote={The aggregation behavior of two commercial samples of α-lactalbumin (α-La) heated at 95 °C at neutral pH in a complex mineral salt environment was investigated. The objective was to understand the effects of variability between α-La samples and relative concentration of β-lactoglobulin (β-Lg) on aggregate size development, as measured by light scattering and turbidity development. The effect of protein net charge was evaluated with a solubility method and the role of thiol groups was evaluated by reaction with DTNB. The sample with the highest level of β-Lg had higher solubility at pH 6.75 and 6.8, yielded more reactive thiol groups, had a 25% faster first-order rate constant, and formed spherical aggregates with a much higher molecular weight than those produced in the sample containing less β-Lg. Adding increasing quantities of β-Lg to the samples generally decreased reversibility and altered the aggregation process; however, other factors appear to be involved in determining aggregate properties.}, number={10}, journal={INTERNATIONAL DAIRY JOURNAL}, author={McGuffey, Matthew K. and Otter, Donald E. and Zanten, John H. and Foegeding, E. Allen}, year={2007}, month={Oct}, pages={1168–1178} }
 @article{hamann_zhang_daubert_foegeding_diehl_2006, title={Analysis of compression, tension and torsion for testing food gel fracture properties}, volume={37}, ISSN={["1745-4603"]}, DOI={10.1111/j.1745-4603.2006.00074.x}, abstractNote={ABSTRACT}, number={6}, journal={JOURNAL OF TEXTURE STUDIES}, author={Hamann, Donald D. and Zhang, Junhua and Daubert, Christopher R. and Foegeding, E. Allen and Diehl, Kenneth C., Jr.}, year={2006}, month={Dec}, pages={620–639} }
 @article{foegeding_luck_davis_2006, title={Factors determining the physical properties of protein foams}, volume={20}, ISSN={["0268-005X"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-25844500998&partnerID=MN8TOARS}, DOI={10.1016/j.foodhyd.2005.03.014}, abstractNote={Protein foams are an integral component of many foods such as meringue, nougat and angel food cake. With all these applications, the protein foam must first obtain the desired level of air phase volume (foamability), and then maintain stability when subjected to a variety of processes including mixing, cutting and heating. Therefore, factors determining foamability and stability to mechanical and thermal processing are important to proper food applications of protein foams. We have investigated the effects of protein type, protein modification and co-solutes on overrun, stability and yield stress. The level of overrun generated by different proteins was: whey protein isolate hydrolysates >whey protein isolate=β-lactoglobulin=egg white>α-lactalbumin. The level of yield stress generated by different proteins was: egg white>whey protein isolate hydrolysates≥β-lactoglobulin>whey protein isolate>α-lactalbumin. Factors that decreased surface charge (pH∼pI or high ionic strength) caused a more rapid adsorption of protein at the air–water interface, generally increased dilatational viscoelasticity and increased foam yield stress. The elastic component of the dilatational modulus of the air–water interface was correlated with foam yield stress. The properties of foams did not predict performance in making angel food cakes. A model for foam performance in angel food cakes is proposed.}, number={2-3}, journal={FOOD HYDROCOLLOIDS}, author={Foegeding, EA and Luck, PJ and Davis, JP}, year={2006}, pages={284–292} }
 @misc{foegeding_2006, title={Food biophysics of protein gels: A challenge of nano and macroscopic proportions}, volume={1}, ISSN={["1557-1866"]}, DOI={10.1007/s11483-005-9003-y}, number={1}, journal={FOOD BIOPHYSICS}, author={Foegeding, E. Allen}, year={2006}, month={Mar}, pages={41–50} }
 @article{zhang_daubert_foegeding_2006, title={Polyacrylamide gels as elastic models for food gels: Fracture properties affected by dextran and glycerol}, volume={37}, DOI={10.1111/j.1745-4603.2006.00046.x}, abstractNote={ABSTRACT}, number={2}, journal={Journal of Texture Studies}, author={Zhang, J. H. and Daubert, C. R. and Foegeding, E. A.}, year={2006}, pages={200–220} }
 @article{daubert_hudson_foegeding_prabhasankar_2006, title={Rheological characterization and electrokinetic phenomena of charged whey protein dispersions of defined sizes}, volume={39}, ISSN={["1096-1127"]}, DOI={10.1016/j.lwt.2004.12.013}, abstractNote={A multi-step processing technique produced large colloidal particles from whey proteins, prompting instantaneous thickening upon hydration. Analysis of the rheological characteristics and zeta potential of the modified whey suspensions of defined particle sizes allowed investigation into the role of size on ingredient functionality. Preliminarily, the modified protein powders were sieved to achieve three size ranges, and analyzes were conducted on each of the three distributions and the non-sieved fractions. Following hydration, steady and oscillatory shear analyzes were performed using a controlled stress rheometer to determine rheological characteristics. Intrinsic viscosity was determined with a capillary viscometer and application of the Huggins equation. Zeta potential was calculated from colloidal electrophoretic mobility, measured with a ZetaPALS analyser. After thorough hydration, particle-size analysis revealed a size increase of >1.3 times for each fraction. When analysed on a protein basis, increasing particle size yielded an increase to intrinsic viscosity, flow behavior index, zero shear viscosity, and a decreased zeta potential and consistency coefficient. Knowledge of the interrelationship between zeta potential, rheological properties, and particle size of the modified whey ingredient will further advance an understanding of the functionality of this protein ingredient.}, number={3}, journal={LWT-FOOD SCIENCE AND TECHNOLOGY}, author={Daubert, CR and Hudson, HM and Foegeding, EA and Prabhasankar, P}, year={2006}, pages={206–215} }
 @article{barrangou_drake_daubert_foegeding_2006, title={Sensory texture related to large-strain rheological properties of agar/glycerol gels as a model food}, volume={37}, ISSN={["1745-4603"]}, DOI={10.1111/j.1745-4603.2006.00050.x}, abstractNote={ABSTRACT}, number={3}, journal={JOURNAL OF TEXTURE STUDIES}, author={Barrangou, Lisa M. and Drake, Mary Anne and Daubert, Christopher R. and Foegeding, E. Allen}, year={2006}, month={Jun}, pages={241–262} }
 @article{barrangou_daubert_foegeding_2006, title={Textural properties of agarose gels. I. Rheological and fracture properties}, volume={20}, ISSN={["0268-005X"]}, DOI={10.1016/j.foodhyd.2005.02.019}, abstractNote={Small- and large-strain rheological methods were used to develop rheological profiles of agarose gels, including linear, non-linear, and fracture properties. Gel properties were examined under conditions of varying agarose concentration (0.5–2.5% w/w), glycerol concentration (0–60% w/w), and strain rate (0.0017–0.17 s−1). Small-strain behaviors were primarily elastic with only slight frequency dependence. Large-strain behaviors and fracture properties were dependent upon strain rate, agarose and glycerol concentration. Increasing concentrations of agarose produced an increasingly stronger, more brittle network, while increasing concentrations of glycerol produced an increasingly stronger, more deformable network. All fracture properties and non-linear behaviors increased with increasing strain rate in a similar manner, suggesting a general mechanism responsible for strain rate effects that is similar for non-linear and fracture behavior. Increasing concentrations of agarose and glycerol, respectively, increased and decreased the strain rate dependence of non-linear behavior. Phenomenological models were evaluated for describing non-linear behavior. A second-order polynomial equation was determined to describe the data more accurately than the commonly used BST equation [Blatz, P. J., Sharda, S. C., & Tschoegl, N. W. (1974). Strain energy function for rubberlike materials based on a generalized measure of strain. Transactions of the Society of Rheology, 18 (1) 145–161.], providing an estimated parameter that allowed relative non-linear behavior to be reliably quantified.}, number={2-3}, journal={FOOD HYDROCOLLOIDS}, author={Barrangou, LM and Daubert, CR and Foegeding, EA}, year={2006}, pages={184–195} }
 @article{barrangou_drake_daubert_foegeding_2006, title={Textural properties of agarose gels. II. Relationships between rheological properties and sensory texture}, volume={20}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2005.03.013}, abstractNote={Descriptive analysis was used to quantify the perceived hand texture characteristics of agarose gels, and results were compared with previously developed fundamental rheological profiles to determine if relationships could be established. Four texture attributes were used to describe the gels, including ‘hand small-strain force’, ‘hand springiness’, ‘hand fracture force’, and ‘hand fracture deformation’. Gels were differentiated similarly by sensory analysis and fracture properties (p≤0.05). Hand small-strain force and ‘hand-fracture force’ terms were capable of differentiating the gels equally as well, indicating that relative gel strength was perceived similarly with non-destructive and fracture causing deformations. Surprisingly, the hand force terms correlated more highly with fracture modulus (fractures stress/fracture strain) values (r≥0.98, p≤0.001) than fracture stress values (r=0.76–0.82, p≤0.05), suggesting sensory perception of force includes a coupling of stress and strain. The definition of the term hand fracture deformation was very similar to the commonly used sensory term ‘cohesiveness’, and was highly correlated with fracture strain values (r=0.98, p≤0.001). Linear viscoelastic properties could not distinguish gels as sensitively as fracture properties. These findings clearly demonstrate fracture properties are capable of predicting sensory texture properties.}, number={2-3}, journal={FOOD HYDROCOLLOIDS}, author={Barrangou, LM and Drake, M and Daubert, CR and Foegeding, EA}, year={2006}, pages={196–203} }
 @article{zhang_daubert_foegeding_2005, title={Characterization of polyacrylamide gels as an elastic model for food gels}, volume={44}, ISSN={["1435-1528"]}, DOI={10.1007/s00397-005-0444-5}, number={6}, journal={RHEOLOGICA ACTA}, author={Zhang, JH and Daubert, CR and Foegeding, EA}, year={2005}, month={Jul}, pages={622–630} }
 @article{mcguffey_epting_kelly_foegeding_2005, title={Denaturation and aggregation of three alpha-lactalbumin preparations at neutral pH}, volume={53}, ISSN={["1520-5118"]}, DOI={10.1021/jf048863p}, abstractNote={The denaturation and aggregation of reagent-grade (Sigmaalpha-La), ion-exchange chromatography purified (IEXalpha-La), and a commercial-grade (Calpha-La) alpha-lactalbumin were studied with differential scanning calorimetry (DSC), polyacrylamide gel electrophoresis, and turbidity measurement. All three preparations had similar thermal denaturation temperatures with an average of 63.7 degrees C. Heating pure preparations of alpha-lactalbumin produced three non-native monomer species and three distinct dimer species. This phenomenon was not observed in Calpha-La. Turbidity development at 95 degrees C (tau95 degrees C) indicated that pure preparations rapidly aggregate at pH 7.0, and evidence suggests that hydrophobic interactions drove this phenomenon. The Calpha-La required 4 times the phosphate or excess Ca2+ concentrations to develop a similar tau95 degrees C to the pure preparations and displayed a complex pH-dependent tau95 degrees C behavior. Turbidity development dramatically decreased when the heating temperature was below 95 degrees C. A mechanism is provided, and the interrelationship between specific electrostatic interactions and hydrophobic attraction, in relation to the formation of disulfide-bonded products, is discussed.}, number={8}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={McGuffey, MK and Epting, KL and Kelly, RM and Foegeding, EA}, year={2005}, month={Apr}, pages={3182–3190} }
 @article{beucler_drake_foegeding_2005, title={Design of a beverage from whey permeate}, volume={70}, DOI={10.1111/j.1365-2621.2005.tb07203.x}, abstractNote={ABSTRACT: Wheypermeate (WP) is a byproduct ofwhey protein ingredient production, and primarily contains water, lactose, and minerals, with minimal fat and protein. The majority of the WP produced in the United States is disposed of via land-spreading or is used as a component in animal feed. However, WP could be utilized in the growing beverage industry. The objectives of this study were to conduct descriptive sensory analysis of a wide selection of commercial beverages and to design a beverage utilizing WP. The descriptive sensory properties (visual, flavor, and texture/mouth-feel) of fifteen commercial beverages were determined using a trained descriptive panel (n= 11).WP with and without hydrolysis of lactose was subsequently incorporated into a basic beverage formula, substituted for 0%, 25%, 50%, 75%, or 100% of water. Consumers (n = 100) evaluated beverages withWP and commercial beverages for overall acceptability, flavor liking, and thirst-quenching ability. Drinks made with lower levels (25% and 50%) of either hydrolyzed or unhydrolyzed WP were more similar to the commercial beverages in visual and flavor properties than beverages containing higher percentages (75% and 100%) ofWP. All drinks made withWP were higher in electrolyte (Na, K, Zn, Mg, P) content compared with a commercial sports beverage (P < 0.05). Beverage incorporation represents a value-added utilization for low levels ofWP}, number={4}, journal={Journal of Food Science}, author={Beucler, J. and Drake, M. and Foegeding, E. A.}, year={2005}, pages={S277–285} }
 @article{davis_doucet_foegeding_2005, title={Foaming and interfacial properties of hydrolyzed beta-lactoglobulin}, volume={288}, ISSN={["1095-7103"]}, DOI={10.1016/j.jcis.2005.03.002}, abstractNote={beta-lactoglobulin (beta-lg) was hydrolyzed with three different proteases and subsequently evaluated for its foaming potential. Foam yield stress (tau0) was the primary variable of interest. Two heat treatments designed to inactivate the enzymes, 75 degrees C/30 min and 90 degrees C/15 min, were also investigated for their effects on foam tau0. Adsorption rates and dilatational rheological tests at a model air/water interface aided data interpretation. All unheated hydrolysates improved foam tau0 as compared to unhydrolyzed beta-lg, with those of pepsin and Alcalase 2.4L(R) being superior to trypsin. Heat inactivation negatively impacted foam tau0, although heating at 75 degrees C/30 min better preserved this parameter than heating at 90 degrees C/15 min. All hydrolysates adsorbed more rapidly at the air/water interface than unhydrolyzed beta-lg, as evidenced by their capacity to lower the interfacial tension. A previously observed relationship between interfacial dilatational elasticity (E') and tau0 was generally confirmed for these hydrolysates. Additionally, the three hydrolysates imparting the highest tau0 not only had high values of E' (approximately twice that of unhydrolyzed beta-lg), they also had very low phase angles (essentially zero). This highly elastic interfacial state is presumed to improve foam tau0 indirectly by improving foam stability and directly by imparting resistance to interfacial deformation.}, number={2}, journal={JOURNAL OF COLLOID AND INTERFACE SCIENCE}, author={Davis, JP and Doucet, D and Foegeding, EA}, year={2005}, month={Aug}, pages={412–422} }
 @article{zhang_daubert_foegeding_2005, title={Fracture analysis of alginate gels}, volume={70}, ISSN={["1750-3841"]}, DOI={10.1111/j.1365-2621.2005.tb11471.x}, abstractNote={ABSTRACT:}, number={7}, journal={JOURNAL OF FOOD SCIENCE}, author={Zhang, JH and Daubert, CR and Foegeding, EA}, year={2005}, month={Sep}, pages={E425–E431} }
 @article{doucet_foegeding_2005, title={Gel formation of peptides produced by extensive enzymatic hydrolysis of beta-lactoglobulin}, volume={6}, ISSN={["1526-4602"]}, DOI={10.1021/bm0492273}, abstractNote={The purpose of the present study was to identify which peptides were responsible for enzyme-induced gelation of extensively hydrolyzed beta-lactoglobulin with Alcalase in order to gain insight into the mechanism of gelation. Dynamic rheology, aggregation measurements, isoelectrofocusing as well as chromatography and mass spectrometry were used to understand the gel formation. A transparent gel was formed above a critical concentration of peptides while noncovalently linked aggregates appear with increasing time of hydrolysis. Extensive hydrolysis was needed for gelation to occur as indicated by the small size of the peptides. Isoelectrofocusing was successful at separating the complex mixture, and 19 main peptides were identified with molecular weight ranging from 265 to 1485 Da. Only one fragment came from a beta-sheet rich region of the beta-lactoglobulin molecule, and a high proportion of peptides had proline residues in their sequence.}, number={2}, journal={BIOMACROMOLECULES}, author={Doucet, D and Foegeding, EA}, year={2005}, pages={1140–1148} }
 @article{resch_daubert_foegeding_2005, title={The effects of acidulant type on the rheological properties of beta-lactoglobulin gels and powders derived from these gels}, volume={19}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2004.10.034}, abstractNote={Heat-induced beta-lactoglobulin (β-Lg) gels and instantly-thickening protein powders derived from these gels were rheologically characterized to identify how acid selection and pH adjustment impact whey protein gelation and derived powder properties. An established procedure for the production of an instant-thickening whey protein ingredient, consisting of protein hydration, pH adjustment to 3.35, thermal gelation at 80 °C, and drying, was applied to β-Lg. Hydrochloric, lactic, citric, and phosphoric acids were evaluated in the critical pH adjustment step. Acidulant selection clearly impacted β-Lg gelation and derived powder properties. Ion specific effects were in general agreement with classical Hofmeister series behavior. Maximum viscosity and water holding were observed in the ingredients derived from the strong, translucent gels created in systems utilizing lactic and hydrochloric acids. Use of citric acid resulted in a brittle, opaque coagulum which created an ingredient with very poor thickening functionality. Protein solutions treated with phosphoric acid were most resistant to gelation at 80 °C and led to limited thickening ability of the derived powder. Acidulant selection is an important processing parameter that may be manipulated to modify β-Lg gelation and the functional properties of derived thickening ingredients.}, number={5}, journal={FOOD HYDROCOLLOIDS}, author={Resch, JJ and Daubert, CR and Foegeding, EA}, year={2005}, month={Sep}, pages={851–860} }
 @article{resch_daubert_foegeding_2005, title={beta-lactoglobulin gelation and modification: Effect of selected acidulants and heating conditions}, volume={70}, ISSN={["1750-3841"]}, DOI={10.1111/j.1365-2621.2005.tb09025.x}, abstractNote={: The effect of acidulant selection, heating temperature, and heating rate on the properties of low-pH β-lactoglobulin (β-Lg) gels and powders derived from these gels was investigated by rheological and microscopic techniques. As isothermal gelation temperature was increased from 75 to 85 °C, gels made with hydrochloric and lactic acid showed more rapid gel formation and increased stress at gel fracture. Thickening and water-holding properties of powders derived from these gels also increased with temperature. Increases in gel strength and derivatized powder functionality appeared to plateau above 85 °C. Gels and derivatized powders prepared with phosphoric acid exhibited attributes similar to samples prepared with HCl and lactic acid at lower temperatures. The ion-specific ability of phosphate to increase denaturation temperature was responsible for the shift in properties of gels made with phosphoric acid. Microscopy revealed temperature effects on network building block size, but variations in rheological properties could not be linked to changes in gel micrographs. Alteration of heating rates from 2.0 to 0.2 °C/min during gelation affected the observed gelation temperature, but had little effect on final gel mechanical properties. Acid selection and gelation temperature offer alternatives to control β-Lg gel strength and the functional properties of instant thickening protein ingredients.}, number={1}, journal={JOURNAL OF FOOD SCIENCE}, author={Resch, JJ and Daubert, CR and Foegeding, EA}, year={2005}, pages={C79–C86} }
 @article{resch_daubert_allen foegeding_2004, title={A comparison of drying operations on the rheological properties of whey protein thickening ingredients}, volume={39}, ISSN={["1365-2621"]}, DOI={10.1111/j.1365-2621.2004.00882.x}, abstractNote={Summary}, number={10}, journal={INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY}, author={Resch, JJ and Daubert, CR and Allen Foegeding, E}, year={2004}, month={Dec}, pages={1023–1031} }
 @article{zhang_foegeding_hardin_2004, title={Effect of sulfated polysaccharides on heat-induced structural changes in beta-lactoglobulin}, volume={52}, ISSN={["1520-5118"]}, DOI={10.1021/jf035037s}, abstractNote={The mechanism that leads to a decreased aggregation of beta-lactoglobulin in the presence of dextran sulfate and lambda-carrageenan was investigated by assessing changes in the denaturation thermodynamics and protein structure. Differential scanning calorimetry results showed that the denaturation temperature (Tp) was about 4.6 degrees C higher in the presence of dextran sulfate, as compared with beta-lactoglobulin alone, whereas in the presence of lambda-carrageenan the difference in Tp was about 1.2 degrees C. Changes in protein structure studies using near-UV circular dichroism (CD) provided support for the calorimetric results. The transition midpoint (Tm) for denaturation of beta-lactoglobulin was about 5 degrees C higher in the presence of dextran sulfate than that found with beta-lactoglobulin alone and about 2 degrees C in the presence of lambda-carrageenan. Thermal modifications of the tertiary structure of beta-lactoglobulin were irreversible at temperatures above 67 degrees C; the addition of dextran sulfate reduced the extent of such modifications. Far-UV CD studies indicated that the addition of dextran sulfate or lambda-carrageenan did not affect secondary structure changes of beta-lactoglobulin upon heating. These studies indicate that dextran sulfate and lambda-carrageenan can enhance the stability of beta-lactoglobulin and thereby inhibit heat denaturation and aggregation.}, number={12}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Zhang, GY and Foegeding, EA and Hardin, CC}, year={2004}, month={Jun}, pages={3975–3981} }
 @article{davis_foegeding_hansen_2004, title={Electrostatic effects on the yield stress of whey protein isolate foams}, volume={34}, ISSN={["0927-7765"]}, DOI={10.1016/j.colsurfb.2003.10.014}, abstractNote={The mechanisms responsible for foam structure are of practical interest within the food industry. The yield stress (tau) of whey protein isolate (WPI) foams as affected by electrostatic forces was investigated by whipping 10% (w/v) protein solutions prepared over a range of pH levels and salt concentrations. Measurements of foam overrun and model WPI interfaces, i.e. adsorption kinetics as determined via dynamic surface tension and dilatational rheological characterization, aided data interpretation. Interfacial measurements were also made with the primary whey proteins, beta-lactoglobulin (beta-lg) and alpha-lactalbumin (alpha-la). Yield stress of WPI foams was dependent on pH, salt type and salt concentration. In the absence of salt, tau was highest at pH 5.0 and lowest at pH 3.0. The addition of NaCl and CaCl2 up to 400 mM significantly increased tau at pH 7.0 but not at pH 3.0. Furthermore, at pH 7.0, equivalent molar concentrations of CaCl2 as compared to NaCl increased tau to greater extents. Salts had minimal effects on tau at pH 5.0. Comparisons with interfacial rheological data suggested the protein's capacity to contribute towards tau was related to the protein's potential at forming strong, elastic interfaces throughout the structure. The dynamic surface tension data for beta-lg and alpha-la were similar to WPI, while the interfacial rheological data displayed several noticeable differences.}, number={1}, journal={COLLOIDS AND SURFACES B-BIOINTERFACES}, author={Davis, JP and Foegeding, EA and Hansen, FK}, year={2004}, month={Mar}, pages={13–23} }
 @article{davis_foegeding_2004, title={Foaming and interfacial properties of polymerized whey protein isolate}, volume={69}, DOI={10.1111/j.1365-2621.2004.tb10706.x}, abstractNote={ABSTRACT:  Yield stresses (τ) of whipped foams prepared from various ratios of native whey protein isolate (WPI) and polymerized whey protein isolate (pWPI) were characterized by means of vane rheometry Yield stress displayed a parabolic response to increasing concentrations of pWPI, peaking at 50%. Foam air phase volume steadily decreased with increasing pWPI content, whereas equilibrium surface tension steadily increased. Dynamic surface tension measurements revealed that native WPI adsorbed much more rapidly than pWPI, presumably because of the latter's larger size. Interfacial dilatational elasticity (E') displayed a parabolic trend with increasing pWPI content, peaking at 50%. This suggested that pWPI coadsorbs with native WPI, bolstering E' of native WPI interfaces. However, too much pWPI caused a weakening of the network. A positive, curvilinear relationship between E' and τ was observed, consistent with a previous observation for WPI foams formed at various pH levels and salt concentrations, further suggesting a general link between these parameters.}, number={5}, journal={Journal of Food Science}, author={Davis, J. P. and Foegeding, E. A.}, year={2004}, pages={C404–410} }
 @article{pernell_foegeding_luck_davis_2004, title={Properties of whey and egg white protein foams (vol 204, pg 9, 2002)}, volume={238}, ISSN={["1873-4359"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-2442575970&partnerID=MN8TOARS}, DOI={10.1016/j.colsurfa.2004.03.003}, number={1-3}, journal={COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS}, author={Pernell, CW and Foegeding, EA and Luck, PJ and Davis, JP}, year={2004}, month={May}, pages={161–161} }
 @article{ravindra_genovese_foegeding_rao_2004, title={Rheology of heated mixed whey protein isolate/cross-linked waxy maize starch dispersions}, volume={18}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2003.12.004}, abstractNote={Dynamic and flow rheological characteristics of heated mixed whey protein isolate (WPI) and cross-linked waxy maize starch (CWM) dispersions: 5% solids, pH=7.0, 75 mM NaCl, were examined at starch mass fractions (smf) from 0 (pure WPI) to 1 (pure CWM). The heated mixed dispersions had lower values of G′ than the pure WPI dispersion, primarily due to the disruptive effect of CWM granules on the WPI network. The point of phase inversion (minimum G′ value) was at about smf=0.65. Based on frequency sweep data, the mixed dispersions were classified as ‘structured liquids’. Shear stress–shear rate data on the blends showed three different behaviors: WPI dispersion-like, CWM dispersion-like, or intermediate between the two depending on the composition. Apparent viscosity–shear rate curves followed the power law model with flow behavior index (n) values of 0.09≤n≤0.16 at smf≤0.2, and 0.47≤n≤0.53 at smf≥0.4.}, number={5}, journal={FOOD HYDROCOLLOIDS}, author={Ravindra, P and Genovese, DB and Foegeding, EA and Rao, MA}, year={2004}, month={Sep}, pages={775–781} }
 @article{gwartney_larick_foegeding_2004, title={Sensory texture and mechanical properties of stranded and particulate whey protein emulsion gels}, volume={69}, DOI={10.1111/j.1365-2621.2004.tb09945.x}, abstractNote={ABSTRACT:  The influence of gel structure type and amount of lipid on texture of whey protein isolate (WPI) gels was evaluated by descriptive sensory analysis and determination of fracture and water‐holding properties. A series of 16 gels of varying structure (particulate or stranded) and lipid composition (0% to 20%) were developed at a constant protein concentration (12% w/v). Stranded gels had higher values for fracture strain, strain hardening, and held‐water. Particulate and stranded gels were similar in fracture stress. Eighteen sensory texture attributes were used to evaluate gels throughout the mastication process that was separated by the following phases: prefracture, 1st bite, chew‐down, and preswallowing. The 1st bite property of firmness and preswallowing properties of number of chews and time to swallow were the only sensory properties associated with lipid content. Fracture stress was correlated with these properties. The remaining 15 texture terms were primarily determined by gel structure type. It appears that gel structure type determines the primary texture properties of WPI emulsion gels. An increase in lipid content increases gel firmness and amount of chews required; however, it did not change the primary texture sensation.}, number={9}, journal={Journal of Food Science}, author={Gwartney, E. A. and Larick, D. K. and Foegeding, E. A.}, year={2004}, pages={S333–339} }
 @article{lee_buwalda_euston_foegeding_mckenna_2003, title={Changes in the rheology and microstructure of processed cheese during cooking}, volume={36}, ISSN={["0023-6438"]}, DOI={10.1016/s0023-6438(03)00012-4}, abstractNote={The ‘creaming reaction’ of a processed cheese can be traced by the change in its viscosity profile. The viscosity profile can be measured by shearing the processed cheese at a low but constant shear rate using a rheometer. We showed that this change in the viscosity profile during cooking occurred in processed cheese made from a typical formulation as well as from a fat-free model system. This indicated that the ‘creaming reaction’ is primarily a protein-based interaction, which takes places with or without the presence of fat. The observed viscosity profile can be explained in terms of changes in the protein structure of the molten processed cheese during processing. A model is proposed.}, number={3}, journal={LEBENSMITTEL-WISSENSCHAFT UND-TECHNOLOGIE-FOOD SCIENCE AND TECHNOLOGY}, author={Lee, SK and Buwalda, RJ and Euston, SR and Foegeding, EA and McKenna, AB}, year={2003}, pages={339–345} }
 @article{steiner_foegeding_drake_2003, title={Descriptive analysis of caramel texture}, volume={18}, ISSN={["0887-8250"]}, DOI={10.1111/j.1745-459X.2003.tb00390.x}, abstractNote={ABSTRACT}, number={4}, journal={JOURNAL OF SENSORY STUDIES}, author={Steiner, AE and Foegeding, EA and Drake, M}, year={2003}, month={Aug}, pages={277–289} }
 @article{doucet_gauthier_otter_foegeding_2003, title={Enzyme-induced gelation of extensively hydrolyzed whey proteins by Alcalase: Comparison with the plastein reaction and characterization of interactions}, volume={51}, ISSN={["1520-5118"]}, DOI={10.1021/jf026041r}, abstractNote={Extensive hydrolysis of whey protein isolate by Alcalase 2.4L produces a gel. The objectives of this study were to compare enzyme-induced gelation with the plastein reaction by determining the types of interactions involved in gelation. The average chain length of the peptides did not increase during hydrolysis and reached a plateau after 30 min to be approximately 4 residues, suggesting that the gel was formed by small molecular weight peptides held together by non-covalent interactions. The enzyme-induced gel network was stable over a wide range of pH and ionic strength and, therefore, showed some similarities with the plastein reaction. Disulfide bonds were not involved in the gel network. The gelation seems to be caused by physical aggregation, mainly via hydrophobic interactions with hydrogen bonding and electrostatic interactions playing a minor role.}, number={20}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Doucet, D and Gauthier, SF and Otter, DE and Foegeding, EA}, year={2003}, month={Sep}, pages={6036–6042} }
 @article{doucet_otter_gauthier_foegeding_2003, title={Enzyme-induced gelation of extensively hydrolyzed whey proteins by Alcalase: Peptide identification and determination of enzyme specificity}, volume={51}, ISSN={["1520-5118"]}, DOI={10.1021/jf026242v}, abstractNote={Extensive hydrolysis of whey protein isolate by Alcalase was shown to induce gelation mainly via hydrophobic interactions. The aim of this work was to characterize the peptides released in order to better understand this phenomenon. The apparent molecular mass distribution indicated that aggregates were formed by small molecular mass peptides (<2000 Da). One hundred and thirty peptides with various lengths were identified by reversed-phase high-performance liquid chromatography coupled with electrospray ionization mass spectrometry. Alcalase was observed to have a high specificity for aromatic (Phe, Trp, and Tyr), acidic (Glu), sulfur-containing (Met), aliphatic (Leu and Ala), hydroxyl (Ser), and basic (Lys) residues. Most peptides had an average hydrophobicity of 1-1.5 kcal/residue and a net charge of 0 at the pH at which gelation occurred (6.0). Therefore, an intermolecular attractive force such as hydrophobic interaction suggests the formation of aggregates that further leads to the formation of a gel.}, number={21}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Doucet, D and Otter, DE and Gauthier, SF and Foegeding, EA}, year={2003}, month={Oct}, pages={6300–6308} }
 @article{zhang_foegeding_2003, title={Heat-induced phase behavior of beta-lactoglobulin/polysaccharide mixtures}, volume={17}, ISSN={["0268-005X"]}, DOI={10.1016/S0268-005X(03)00099-7}, abstractNote={The influence of polysaccharides on the thermal stability of β-lactoglobulin at pH 6.8 was investigated regarding polysaccharide type, concentration and size. Two kinds of polysaccharides, sulfate-containing polysaccharides (carrageenans and dextran sulfate with different molecular mass) and neutral polysaccharides (dextran with different molecular mass), were investigated. At low ratios of sulfate-containing polysaccharide to β-lactoglobulin, heat-induced aggregation was decreased as shown by lower turbidity. Increasing the ratio induced a significant increase in turbidity, leading to segregative phase separation. Phase diagrams were established by centrifugation, chemical assays and visual observation for β-lactoglobulin/kappa-carrageenan and β-lactoglobulin/dextran sulfates. Significant phases (stable, separated and gel) were found, indicating the varieties of phase behavior and a strong competition between phase separation and gelation caused by thermal treatment. Moreover, gelation was reversible in β-lactoglobulin/dextran sulfate systems depending on the polysaccharide concentration.}, number={6}, journal={FOOD HYDROCOLLOIDS}, author={Zhang, GY and Foegeding, EA}, year={2003}, month={Nov}, pages={785–792} }
 @article{brown_foegeding_daubert_drake_gumpertz_2003, title={Relationships among rheological and sensorial properties of young cheeses}, volume={86}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(03)73905-8}, abstractNote={This study investigated the sensory and rheological properties of young cheeses in order to better understand perceived cheese texture. Mozzarella and Monterey Jacks were tested at 4, 10, 17, and 38 d of age; process cheese was tested at 4 d. Rheological methods were used to determine the linear and nonlinear viscoelastic and fracture properties. A trained sensory panel developed a descriptive language and reference scales to evaluate cheese texture. All methods differentiated the cheeses by variety. Principal component analysis of sensory texture revealed that three principal components explained 96.1% of the total variation in the cheeses. The perception of firmness decreased as the cheeses aged, whereas the perception of springiness increased. Principal component analysis of the rheological parameters (three principal components: 87.9% of the variance) showed that the cheeses' solid-like response (storage modulus and fracture modulus) decreased during aging, while phase angle, maximum compliance, and retardation time increased. Analysis of the instrumental and sensory parameters (three principal components: 82.1% of the variance) revealed groupings of parameters according to cheese rigidity, resiliency, and chewdown texture. Rheological properties were highly associated with rigidity and resiliency, but less so with chewdown texture.}, number={10}, journal={JOURNAL OF DAIRY SCIENCE}, author={Brown, JA and Foegeding, EA and Daubert, CR and Drake, MA and Gumpertz, M}, year={2003}, month={Oct}, pages={3054–3067} }
 @article{lowe_foegeding_daubert_2003, title={Rheological properties of fine-stranded whey protein isolate gels}, volume={17}, ISSN={["0268-005X"]}, DOI={10.1016/S0268-005X(03)00014-6}, abstractNote={The rheological and fracture properties of fine stranded WPI gels were determined over a range of shear strain rates (0.014–0.69 s−1). All gels had the highest fracture strain when deformed at a strain rate of 0.014 s−1. Fracture stress was relatively constant over all strain rates. These effects were observed at all protein concentrations and suggest a link with molecular or network relaxations. The apparent modulus (stress/strain at any level of strain) exhibited decreasing or linear behavior at low to moderate strains, followed by non-linear strain-hardening behavior at higher strains. As strain rate increased, the gels displayed increased non-linear behavior. The strain where the modulus switched from linear to non-linear behavior decreased as protein concentration or strain rate was increased. Therefore, both strain rate and protein concentration affect the large-strain viscoelastic behavior of WPI gels during deformation and fracture. This observation suggests a link with the molecular relaxation processes occurring in the gel network.}, number={4}, journal={FOOD HYDROCOLLOIDS}, author={Lowe, LL and Foegeding, EA and Daubert, CR}, year={2003}, month={Jul}, pages={515–522} }
 @article{foegeding_brown_drake_daubert_2003, title={Sensory and mechanical aspects of cheese texture}, volume={13}, ISSN={["0958-6946"]}, DOI={10.1016/S0958-6946(03)00094-3}, abstractNote={Producing high quality dairy products requires precise control over factors determining product appearance, flavor and texture. Food texture is analyzed by descriptive sensory analysis. This method uses terms that depict the textural sensations perceived from first bite through mastication and swallowing. One component of sensory texture is mechanical properties, which are determined by empirical or fundamental methods. However, if one wants to understand the molecular basis of texture, then fundamental tests are required. Fundamental rheological properties are linked to network models, such as those for rubber elasticity or filled gels. These models predict how network interactions will alter rheological properties, providing a link from molecular interactions to sensory texture. In general, sensory and rheological terms that relate to the overall firmness and resiliency of cheese are highly correlated. However, sensory terms that describe the breakdown pattern, adhesiveness and cohesiveness of cheese, are weakly, if at all, correlated with rheological properties.}, number={8}, journal={INTERNATIONAL DAIRY JOURNAL}, author={Foegeding, EA and Brown, J and Drake, M and Daubert, CR}, year={2003}, pages={585–591} }
 @article{foegeding_davis_doucet_mcguffey_2002, title={Advances in modifying and understanding whey protein functionality}, volume={13}, ISSN={["1879-3053"]}, DOI={10.1016/S0924-2244(02)00111-5}, abstractNote={Whey protein ingredients are used for a variety of functional applications in the food industry. Each application requires one or several functional properties such as gelation, thermal stability, foam formation or emulsification. Whey protein ingredients can be designed for enhanced functional properties by altering the protein and non-protein composition, and/or modifying the proteins. Modifications of whey proteins based on enzymatic hydrolysis or heat-induced polymerization have a broad potential for designing functionality for specific applications. The effects of these modifications are demonstrated by discussing how they alter gelation and interfacial properties.}, number={5}, journal={TRENDS IN FOOD SCIENCE & TECHNOLOGY}, author={Foegeding, EA and Davis, JP and Doucet, D and McGuffey, MK}, year={2002}, month={May}, pages={151–159} }
 @article{luck_bray_foegeding_2002, title={Factors determining yield stress and overrun of whey protein foams}, volume={67}, ISSN={["0022-1147"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-0036324489&partnerID=MN8TOARS}, DOI={10.1111/j.1365-2621.2002.tb08704.x}, abstractNote={ABSTRACT:  Foams were formed by whipping whey protein solutions (15% w/v protein) containing NaCl, CaCl2, lactose, or glycine. Foam overrun and yield stress were determined. Foams made from whey protein ingredients have greater overrun and yield stress if the concentration of β‐lactoglobulin is high relative to a‐lactalbumin. The presence of 0.4 M CaCl2 in the foaming solution increases overrun and yield stress for β‐lactoglobulin and a‐lactalbumin. The high yield stress of β‐lactoglobulin and a‐lactalbumin foams made from solutions containing CaCl2 suggests that CaCl2 is altering rheological properties of the interfacial protein film and/or contributing to protein aggregation or network formation in the lamellae.}, number={5}, journal={JOURNAL OF FOOD SCIENCE}, author={Luck, PJ and Bray, N and Foegeding, EA}, year={2002}, pages={1677–1681} }
 @article{pernell_luck_foegeding_daubert_2002, title={Heat-induced changes in angel food cakes containing egg-white protein or whey protein isolate}, volume={67}, ISSN={["0022-1147"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-0036812822&partnerID=MN8TOARS}, DOI={10.1111/j.1365-2621.2002.tb08843.x}, abstractNote={ABSTRACT:  Angel food cakes made from egg white or whey protein foams were compared. Cakes were evaluated based on final volume, dynamic volume change, and rheological transitions during baking. Cake expansion during baking was a function of protein concentration regardless of protein type. Cakes containing whey proteins had a lower ability to prevent collapse once starch gelatinization started during baking. Heat‐treating whey proteins or adding xanthan gum increases cake volume, but not to the extent of egg‐white proteins. Cakes containing egg‐white proteins became more elastic at 60 to 85 °C than those containing whey proteins, indicating physical differences in the heat‐set protein foam network associated with protein type.}, number={8}, journal={JOURNAL OF FOOD SCIENCE}, author={Pernell, CW and Luck, PJ and Foegeding, EA and Daubert, CR}, year={2002}, month={Oct}, pages={2945–2951} }
 @article{pernell_foegeding_luck_davis_2002, title={Properties of whey and egg white protein foams}, volume={204}, ISSN={["0927-7757"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-0037161616&partnerID=MN8TOARS}, DOI={10.1016/S0927-7757(01)01061-5}, abstractNote={Foams made of varying concentrations (2–20% w/v protein) of egg white and whey protein isolate were compared by measuring rheological and microstructural properties. Egg white proteins formed foams with higher yield stress (τ) at lower protein concentrations and less whipping time than whey protein isolate foams. The model of Princen and Kiss [J. Coll. Interf. Sci. 128 (1989) 176] predicts a relationship among τ, surface tension (σ), phase volume (φ), and bubble size (R32). This was supported by τ increasing with φ, and the relationship between τ and φ1/3 becoming more linear as protein concentration increased. However, egg white foams had yield stress values as much as 100 Pa greater than whey protein foams, despite having similar phase volumes, bubble size, and lower surface tensions. The experimentally determined factors, Y(φ), for egg white and whey protein isolate foams were within the range determined by Princen and Kiss [J. Coll. Interf. Sci. 128 (1989) 176] for concentrated emulsions. Egg white foams were different in that the values for Y(φ) increased at lower phase volumes than for whey protein isolate foams or concentrated emulsions. These results suggest that specific proteins contribute to foam τ by some means in addition to altering surface properties.}, number={1-3}, journal={COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS}, author={Pernell, CW and Foegeding, EA and Luck, PJ and Davis, JP}, year={2002}, month={May}, pages={9–21} }
 @article{gwartney_foegeding_larick_2002, title={The texture of commercial full-fat and reduced-fat cheese}, volume={67}, ISSN={["0022-1147"]}, DOI={10.1111/j.1365-2621.2002.tb10682.x}, abstractNote={ABSTRACT:  The effect of fat reduction on sensory texture and physical properties of commercially available natural and processed cheeses was investigated. The texture of 5 cheeses in full‐ and reduced‐fat versions was characterized by modified descriptive analysis and torsional fracture methods. Reduced‐fat cheeses were perceived to be more waxy, fracturable, chewy, hard, and springy and less sticky, cohesive, meltable, and smooth than full‐fat cheese. Full‐fat cheese had lower fracture stress values than the equivalent reduced‐fat products. Fracture strain values did not distinguish cheeses based on fat content. These results demonstrate general textural differences between the full‐fat and reduced fat versions of select cheeses.}, number={2}, journal={JOURNAL OF FOOD SCIENCE}, author={Gwartney, E and Foegeding, EA and Larick, DK}, year={2002}, month={Mar}, pages={812–816} }
 @article{mcguffey_foegeding_2001, title={Electrostatic effects on physical properties of particulate whey protein isolate gels}, volume={32}, ISSN={["1745-4603"]}, DOI={10.1111/j.1745-4603.2001.tb01049.x}, abstractNote={Physical properties of particulate whey protein isolate gels formed under varying electrostatic conditions were investigated using large strain rheological and microstructural techniques. The two treatment ranges evaluated were adjusting pH (5.2‐5.8) with no added NaCl and adjusting the NaCl (0.2‐0.6 M) at pH 7. Gels (10% protein w/v) were formed by heating at 80C for 30 min. The large strain properties of fracture strain (γf), fracture stress (σf), and a measure of strain hardening (R0.3) were determined using a torsion method. Gel microstructure was evaluated using scanning electron microscopy (SEM) and gel permeability (Bgel). Overlaying σf and γf curves for pH and NaCl treatments demonstrated an overlap where gels of equal σf and γf could be formed by adjusting pH or NaCl concentration. The high fracture stress (σf∼ 23 kPa and γf∼ 1.86) pair conditions were pH 5.47 and 0.25 M NaCl, pH 7.0. The low fracture stress (σf∼ 13 kPa and γf∼ 1.90) pair conditions were pH 5.68 and 0.6 M NaCl, pH 7.0. The 0.25 M NaCl, pH 7 treatment demonstrated higher R0.3 values than the pH 5.47 treatment. When the sulfhydryl blocker n‐ethylmaleimide was added at 2 mM to the 0.25 M NaCl, pH 7 gel treatment, its rheological behavior was NSD (p>0.05) to the pH 5.47 gel treatment, indicating disulfide bond formation regulated strain hardening. Altering surface charge or counterions, and disulfide bonding, was required to produce gels with similar large strain rheological properties. An increase in gel permeability coincided with an increase in pore size as observed by SEM, independent of rheological properties. This demonstrated that at the length scales investigated, microstructure was not linked to changes in large strain rheological properties.}, number={4}, journal={JOURNAL OF TEXTURE STUDIES}, author={McGuffey, MK and Foegeding, EA}, year={2001}, month={Nov}, pages={285–305} }
 @article{vardhanabhuti_foegeding_mcguffey_daubert_swaisgood_2001, title={Gelation properties of dispersions containing polymerized and native whey protein isolate}, volume={15}, ISSN={["1873-7137"]}, DOI={10.1016/S0268-005X(00)00062-X}, abstractNote={Whey protein polymers (WP-polymers) were prepared by heating whey protein isolate below the critical concentration for gelation at neutral pH and low salt conditions. The effects of WP-polymers and salt types (CaCl2 or NaCl) on rheological properties (large-strain and small-strain analysis), water holding properties, turbidity and microstructure of heat-induced whey protein isolate gels were investigated. Replacement of native whey protein isolate with WP-polymers increased fracture stress, fracture modulus, held water, and the translucency of gels. With both salt types, the addition of WP-polymers changed the gel structure from particulate to fine-stranded. However, the effect of WP-polymers on rheological properties was salt specific. Addition of 20–100% WP-polymers in the presence of 10 mM CaCl2 caused a continued increase in fracture stress. In contrast, protein dispersions containing 30 mM NaCl did not form self-supporting gels when ≥60% WP-polymers were added. Dispersions containing 200 mM NaCl formed self supporting gels at all levels of WP-polymer addition but fracture stresses for gels containing 20–100% WP were similar. Dispersions containing 80% WP-polymers and 200 mM NaCl had lower gel points (time and temperature) than dispersions with 80% WP-polymers and 10 mM CaCl2. It appeared that CaCl2 was more effective in increasing gel fracture stress while NaCl was more effective in decreasing gelation time. Different gel properties may be prepared by altering the amount of WP-polymers and salt types.}, number={2}, journal={FOOD HYDROCOLLOIDS}, author={Vardhanabhuti, B and Foegeding, EA and McGuffey, MK and Daubert, CR and Swaisgood, HE}, year={2001}, month={Mar}, pages={165–175} }
 @article{mleko_foegeding_2001, title={Incorporation of polymerized whey proteins into processed cheese analogs}, volume={56}, number={11}, journal={Milchwissenschaft [Milk Science International]}, author={Mleko, S. and Foegeding, E. A.}, year={2001}, pages={612–615} }
 @article{ikeda_nishinari_foegeding_2001, title={Mechanical characterization of network formation during heat-induced gelation of whey protein dispersions}, volume={56}, ISSN={["0006-3525"]}, DOI={10.1002/1097-0282(2000)56:2<109::aid-bip1056>3.0.co;2-u}, abstractNote={The formation of gel network structures during isothermal heating of whey protein aqueous dispersions was probed by mechanical spectroscopy. It was anticipated that the pathway of the sol-to-gel transition of whey protein dispersions is quite different from that of ordinary cross-linking polymers (e.g., percolation-type transition), since aqueous solutions of native whey proteins have been shown to be highly structured even before gelation, in our previous study. At 20 degrees C, aqueous dispersions of beta-lactoglobulin, the major whey protein, and those of whey protein isolate (WPI), a mixture of whey proteins, exhibited solid-like mechanical spectra, i.e., the predominant storage modulus G' over the loss modulus G", in a certain range of the frequency omega (1-100 rad/s), regardless of the presence or absence of added NaCl. The existence of the added salt was, however, a critical factor for determining transitions in mechanical spectra during gelation at 70 degrees C. beta-Lactoglobulin dispersions in 0.1 mol/dm(3) NaCl maintained the solid-like nature during the entire gelation process and, after passing through the gelation point, satisfied parallel power laws (G' approximately G" approximately omega(n)) that have been proposed for a critical gel (i.e., the gel at the gelation point) that possesses a self-similar or fractal network structure. In contrast, beta-lactoglobulin dispersions without added salt exhibited a transition from solid-like [G'(omega) > G"(omega)] to liquid-like [G'(omega) < G"(omega)] mechanical spectra before gelation, but no parallel power law behavior was recognized at the gelation point. During extended heating time (aging), beta-lactoglobulin gels with 0.1 mol/dm(3) NaCl showed deviations from the parallel power laws, while spectra of gels without added NaCl approached the parallel power laws, suggesting that post-gelation reactions also significantly affect gel network structures. A percolation-type sol-to-gel transition was found only for WPI dispersions without added salt.}, number={2}, journal={BIOPOLYMERS}, author={Ikeda, S and Nishinari, K and Foegeding, EA}, year={2001}, pages={109–118} }
 @article{doucet_gauthier_foegeding_2001, title={Rheological characterization of a gel formed during extensive enzymatic hydrolysis}, volume={66}, ISSN={["1750-3841"]}, DOI={10.1111/j.1365-2621.2001.tb04626.x}, abstractNote={ABSTRACT Extensive hydrolysis of whey protein isolate (WPI) by Alcalase 2.4L® caused a dramatic increase in turbidity and viscosity. A gel was formed after the degree of hydrolysis was ≥ 18%, coinciding with < 16%β‐lactoglobulin and < 4%α‐lactalbumin remaining unhydrolyzed. Heat‐induced and enzyme‐induced WPI gels were compared. Frequency and strain dependence indicated that both gels could be considered as strong, physical gels.}, number={5}, journal={JOURNAL OF FOOD SCIENCE}, author={Doucet, D and Gauthier, SF and Foegeding, EA}, year={2001}, pages={711–715} }
 @article{bowland_foegeding_2001, title={Small strain oscillatory shear and microstructural analyses of a model processed cheese}, volume={84}, ISSN={["0022-0302"]}, DOI={10.3168/jds.S0022-0302(01)74686-3}, abstractNote={The rheological and microstructural properties of a model processed cheese were investigated. The cheese contained 20% protein (rennet casein), 27% anhydrous milk fat, 1.5% NaCl and 1 to 3% Na2HPO4 (DSP). Processing time (10, 20, or 30 min), DSP (1, 2, or 3%) and pH of the DSP-NaCl solution (5.4, 5.6, or 5.8) were adjusted to alter rheological properties. Small-strain oscillatory shear rheological parameters that correlated with transitions previously observed by large-strain (fracture) properties were moduli at 8 degrees C and changes in moduli with cooling from 80 to 25 degrees C. Mechanical spectra at 80 degrees C indicated cheeses containing less than 2.0% DSP were entangled macromolecular dispersions, and those containing more than 2.0% DSP were gels. A compilation of small strain results suggested samples could be divided into three basic rheological states. A model describing the gel network is proposed based on the results of this investigation and large-strain (fracture) rheological properties. The model was based on increased breakdown of para-casein aggregates into amphiphilic molecules and rheological properties being related to the combination of para-casein aggregates and amphiphilic molecules.}, number={11}, journal={JOURNAL OF DAIRY SCIENCE}, author={Bowland, EL and Foegeding, EA}, year={2001}, month={Nov}, pages={2372–2380} }
 @misc{hudson_daubert_foegeding_2001, title={Thermal and PH stable protein thickening agent and method of making the same}, volume={6,261,624}, number={2001 July 17}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Hudson, H. M. and Daubert, C. R. and Foegeding, E. A.}, year={2001} }
 @article{rich_foegeding_2000, title={Effects of sugars on whey protein isolate gelation}, volume={48}, ISSN={["0021-8561"]}, DOI={10.1021/jf000272l}, abstractNote={Whey protein isolate (WPI) gels were prepared from solutions containing ribose or lactose at pH values ranging from 6 to 9. The gels with added lactose had no color development, whereas the gels with added ribose were orange/brown. Lactose stabilized the WPI to denaturation, which increased the time and temperature required for gelation, thus decreasing the fracture modulus of the gel compared to the gels with added ribose and the gels with no sugar added. Ribose, however, favored the Maillard reaction and covalent cross-linking of proteins, which increased gel fracture modulus. The decreased pH caused by the Maillard reaction in the gels containing ribose occurred after protein denaturation and gelation, thus having little if any effect on the gelation process.}, number={10}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Rich, LM and Foegeding, EA}, year={2000}, month={Oct}, pages={5046–5052} }
 @article{pernell_foegeding_daubert_2000, title={Measurement of the yield stress of protein foams by vane rheometry}, volume={65}, ISSN={["0022-1147"]}, DOI={10.1111/j.1365-2621.2000.tb15964.x}, abstractNote={ABSTRACT:}, number={1}, journal={JOURNAL OF FOOD SCIENCE}, author={Pernell, CW and Foegeding, EA and Daubert, CR}, year={2000}, pages={110–114} }
 @misc{foegeding_mleko_2000, title={Method of forming whey protein products}, volume={6,451,371}, number={2000 Sep 25}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Foegeding, E. A. and Mleko, S. W.}, year={2000} }
 @article{ikeda_foegeding_hardin_2000, title={Phospholipid/fatty acid-induced secondary structural change in beta-lactoglobulin during heat-induced gelation}, volume={48}, ISSN={["0021-8561"]}, DOI={10.1021/jf990434h}, abstractNote={Effects of phosphatidylcholine (PC) and the predominant fatty acids (FAs) in milk, butyrate, oleate, and palmitate, on secondary structural changes in beta-lactoglobulin (beta-LG) during heat-induced gelation were analyzed on the basis of circular dichroism (CD) spectra. Small-strain oscillatory measurements were carried out to characterize viscoelastic properties of the heat-induced gels. In the absence of added salt, PC and FAs induced helix formation of beta-LG on heating to 80 degrees C and increased the storage moduli (G') of heat-induced gels. In the presence of 500 mM NaCl, PC did not change the CD spectrum of beta-LG but decreased G'. In contrast, butyrate substantially unfolded beta-LG in 500 mM NaCl on heating, forming very elastic gels with increased G' values. Palmitate and oleate induced beta-LG gel formation at 25 degrees C without heating; heating to 80 degrees C almost completely unfolded beta-LG in 500 mM NaCl.}, number={3}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Ikeda, S and Foegeding, EA and Hardin, CC}, year={2000}, month={Mar}, pages={605–610} }
 @article{mleko_foegeding_2000, title={Physical properties of rennet casein gels and processed cheese analogs containing whey proteins}, volume={55}, number={9}, journal={Milchwissenschaft [Milk Science International]}, author={Mleko, S. and Foegeding, E. A.}, year={2000}, pages={513–516} }
 @article{hudson_daubert_foegeding_2000, title={Rheological and physical properties of derivitized whey protein isolate powders}, volume={48}, ISSN={["0021-8561"]}, DOI={10.1021/jf990906s}, abstractNote={Pregelatinized starch is employed in many food applications due to the instantaneous nature of thickening and stability imparted by modification. Proteins, however, have been excluded as a viscosifying agent due to requisite thermal treatments required to create structure. Whey protein isolate gels were produced while manipulating heating time, pH, and mineral type/content, producing a variety of gel types/networks. Gels were frozen, freeze-dried, and ground into a powder. Once reconstituted in deionized water, gel powders were evaluated based on solubility studies, rotational viscometry, and electrophoresis. The protein powder exhibiting the largest apparent viscosity, highest degree of hydrolysis, and greatest solubility was selected for pH and temperature stability analyses and small amplitude oscillatory rheology. This processing technique manipulates WPI into a product capable of forming cold-set weak gel structures suitable for thickening over a wide range of temperature and pH food systems.}, number={8}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Hudson, HM and Daubert, CR and Foegeding, EA}, year={2000}, month={Aug}, pages={3112–3119} }
 @misc{foegeding_mleko_2000, title={Whey protein products}, volume={6,383,551}, number={2000 Sep 25}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Foegeding, E. A. and Mleko, S. W.}, year={2000} }
 @article{mleko_foegeding_2000, title={pH induced aggregation and weak gel formation of whey protein polymers}, volume={65}, ISSN={["1750-3841"]}, DOI={10.1111/j.1365-2621.2000.tb15969.x}, abstractNote={ABSTRACT:}, number={1}, journal={JOURNAL OF FOOD SCIENCE}, author={Mleko, S and Foegeding, EA}, year={2000}, pages={139–143} }
 @article{ikeda_foegeding_1999, title={Dynamic viscoelastic properties of thermally induced whey protein isolate gels with added lecithin}, volume={13}, ISSN={["1873-7137"]}, DOI={10.1016/S0268-005X(99)00006-5}, abstractNote={The effect of crude egg yolk lecithin on the formation of heat-induced whey protein isolate (WPI) gels was investigated using dynamic small-strain rheometry. Three different types of gel networks, fine-stranded, mixed, and particulate network, were formed by varying NaCl concentration. In all conditions, storage modulus (G′) increased during holding at 80°C, development of which was well-described by first-order reaction kinetics. There was an additional increase in G′ during cooling to 25°C. The final values of G′ and the fracture modulus showed similar trends in the effect of lecithin addition: a substantial reinforcing effect on fine-stranded and mixed gels and slightly negative effect on particulate gels. For fine-stranded and mixed networks, lecithin addition decreased the gelation time and increased the gelation rate constant at 80°C. In contrast, lecithin addition to particulate gels did not affect these rate parameters. The positive effect of lecithin on rheological properties of WPI gels with fine-stranded or mixed networks was not only due to the acceleration of gelation rates during the heating process but also due to the enhancement of the elastic nature of the networks during cooling.}, number={3}, journal={FOOD HYDROCOLLOIDS}, author={Ikeda, S and Foegeding, EA}, year={1999}, month={May}, pages={245–254} }
 @article{foegeding_lowe_boland_hill_1999, title={Effect of genetic polymorphism on the gelation of beta-lactoglobulin}, volume={140}, ISSN={["1022-1360"]}, DOI={10.1002/masy.19991400115}, abstractNote={Abstract}, journal={MACROMOLECULAR SYMPOSIA}, author={Foegeding, EA and Lowe, R and Boland, MJ and Hill, JP}, year={1999}, month={May}, pages={137–143} }
 @article{ikeda_foegeding_1999, title={Effects of lecithin on thermally induced whey protein isolate gels}, volume={13}, ISSN={["1873-7137"]}, DOI={10.1016/S0268-005X(99)00005-3}, abstractNote={The effect of lecithin on fundamental fracture properties (true shear stress and true shear strain at fracture) and water holding capacity of heat-induced whey protein isolate (WPI) gels were investigated. Adding egg yolk lecithin to WPI gels substantially increased the fracture stress of gels containing ≤50 mmol/dm3 NaCl but slightly decreased the fracture modulus at concentrations >100 mmol/dm3. The fracture strain and water holding capacity were decreased by lecithin addition across the NaCl concentration range examined (30–500 mmol/dm3). These results suggest that the gel network type and/or the dispersed state of lecithin changing with NaCl concentration in the system is responsible for the mechanism of lecithin–whey protein interactions. Lecithin can play a beneficial role in promoting gel strength but there is an optimal level which is strongly related to the amount of NaCl in the system.}, number={3}, journal={FOOD HYDROCOLLOIDS}, author={Ikeda, S and Foegeding, EA}, year={1999}, month={May}, pages={239–244} }
 @article{bowland_foegeding_1999, title={Factors determining large-strain (fracture) rheological properties of model processed cheese}, volume={82}, ISSN={["1525-3198"]}, DOI={10.3168/jds.S0022-0302(99)75418-4}, abstractNote={Abstract Torsional fracture was used to map changes in large-strain rheological properties of a model processed cheese that contained 20% protein (rennet casein), 27% anhydrous milk fat, 1.5% NaCl, and 1 to 3% Na 2 HPO 4 . Processing time (10, 20, or 30min), Na 2 HPO 4 (1, 2 or 3%), and pH of the Na 2 HPO 4 -NaCl solution (5.4, 5.6, or 5.8) were adjusted to alter the extent of casein micelle solubilization and heat-induced protein-protein interactions. A Box-Behnken experimental design was employed, and results were analyzed using response surface regression and ridge analysis techniques. Further investigation employed a single factorial design in which Na 2 HPO 4 increased from 1 to 4%. Model processed cheeses had fracture stress, fracture strain, and fracture modulus (fracture stress/fracture strain) values ranging from 25.1 to 79.7 kPa, 0.66 to 1.88 kPa, and 15.2 to 96.0 kPa, respectively. The properties of fracture modulus and fracture strain formed a master curve, independent of the processing variable. Conditions favoring increased protein solubilization and heat-induced protein-protein interactions increase fracture modulus and decreased fracture strain. This finding coincided with an increase in slope ratio (fracture modulus/modulus at 30% of the fracture strain), indicating a change in fracture mechanism from strain weakening to elastic fracture. These results suggested that large-strain (fracture) rheological properties could be used to characterize the effects of processing variables important to processed cheese quality.}, number={9}, journal={JOURNAL OF DAIRY SCIENCE}, author={Bowland, EL and Foegeding, EA}, year={1999}, month={Sep}, pages={1851–1859} }
 @article{mleko_foegeding_1999, title={Formation of whey protein polymers: Effects of a two-step heating process on rheological properties}, volume={30}, ISSN={["1745-4603"]}, DOI={10.1111/j.1745-4603.1999.tb00207.x}, abstractNote={ABSTRACT}, number={2}, journal={JOURNAL OF TEXTURE STUDIES}, author={Mleko, S and Foegeding, EA}, year={1999}, month={Jul}, pages={137–149} }
 @article{li_errington_foegeding_1999, title={Isostrength comparison of large-strain (fracture) rheological properties of egg white and whey protein gels}, volume={64}, ISSN={["0022-1147"]}, DOI={10.1111/j.1365-2621.1999.tb15935.x}, abstractNote={ABSTRACT:}, number={5}, journal={JOURNAL OF FOOD SCIENCE}, author={Li, H and Errington, AD and Foegeding, EA}, year={1999}, pages={893–898} }
 @article{vardhanabhuti_foegeding_1999, title={Rheological properties and characterization of polymerized whey protein isolates}, volume={47}, ISSN={["0021-8561"]}, DOI={10.1021/jf981376n}, abstractNote={Whey protein polymers were formed by heating whey protein isolate solutions at 80 degrees C. Flow behaviors of whey protein polymers produced from different protein concentrations and heating times were comparable to various flow behaviors of hydrocolloids. Polymer formation was found to be a two-phase process. The initial protein concentration was a significant factor that determines the size and/or shape of the primary polymer in the first phase as shown by intrinsic viscosity. Heating time was a factor in determining the aggregation in the second phase as shown by apparent viscosity. Intrinsic viscosity of whey protein polymers was as high as 141.7 +/- 7.30 mL/g, compared to 5.04 +/- 0.20 mL/g for native whey proteins. The intrinsic viscosity and gel electrophoresis data suggested that disulfide bonds played an important role in whey polymer formation.}, number={9}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Vardhanabhuti, B and Foegeding, EA}, year={1999}, month={Sep}, pages={3649–3655} }
 @article{ikeda_foegeding_hagiwara_1999, title={Rheological study on the fractal nature of the protein gel structure}, volume={15}, ISSN={["0743-7463"]}, DOI={10.1021/la9817415}, abstractNote={The effects of ionic strength on fractal structures in heat-induced gels prepared from globular proteins were investigated in the framework of a fractal aggregation of colloidal particles. All gels formed at 90 °C exhibited power law relationships between the storage shear modulus (G‘) and protein concentration. At 25 mM NaCl, the fractal dimension, d (∼2.2), calculated based on the value of the power law exponent agreed with those for reaction-limited cluster−cluster aggregation. Further addition of NaCl (50, 80, 500, 1000 mM) decreased the values of d (∼1.8), which agreed with d for diffusion-limited cluster−cluster aggregation. These results suggest that the predominant effect of an increase in ionic strength on globular protein gelation is ascribed to shielding charges on the surface of the proteins, thereby increasing the reaction probability of protein aggregation. The effective structure-determining rheological properties of heat-induced protein gels are characterized by fractal dimensions deduced ...}, number={25}, journal={LANGMUIR}, author={Ikeda, S and Foegeding, EA and Hagiwara, T}, year={1999}, month={Dec}, pages={8584–8589} }
 @article{errington_foegeding_1998, title={Factors determining fracture stress and strain of fine-stranded whey protein gels}, volume={46}, ISSN={["1520-5118"]}, DOI={10.1021/jf980112y}, abstractNote={Whey proteins form translucent heat-induced gels at low and high pH that differ in fracture properties. Gels formed at pH 7.0 and 6.5 were strong (fracture stress of 59−92 kPa) and rubbery (fracture strain of 1.7−1.2). Gels formed at pH 3.0 and 2.5 were weak (fracture stress of 17−19 kPa) and brittle (fracture strain of 0.33−0.39). Altering disulfide bond formation changed gel texture. Addition of a disulfide reducing agent (dithiothreitol) at concentrations ≥ 25 mM, at pH 7.0, caused the gel to weaken (>46% reduction in fracture stress) and become brittle (fracture strain of 0.30−0.32). Increasing the number of disulfide bonds in gels formed at pH values ≤3.5 increased fracture strain to 2.0 while causing a minor increase in fracture stress. Formation of disulfide bonds appears to be essential to the deformability of heat-induced whey protein gels. Keywords: Gelation; fracture properties; disulfide bonding; whey proteins}, number={8}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Errington, AD and Foegeding, EA}, year={1998}, month={Aug}, pages={2963–2967} }
 @inbook{foegeding_gwartney_errington_1998, title={Functional properties of whey proteins in forming networks}, DOI={10.1021/bk-1998-0708.ch009}, abstractNote={Gel formation is one of the most important functionalities of whey proteins. The network structures formed in protein gelation contribute to the appearance, texture, water-holding and flavor delivery of the gel. Gel networks are classified as fine-stranded, particulate or mixed structures. In general, fine-stranded gels are transparent or translucent and have high water-holding properties, whereas particulate gels are opaque and have lower water-holding properties. Fine-stranded gels are formed when aggregation produces network strands with diameters representing one to several molecular diameters. Particulate gels are formed when there is aggregation prior to denaturation, or the aggregation of denatured molecules produces dispersed protein clusters with diameters 100-1000 times molecular diameters. Particulate gel networks appear to be formed from secondary aggregation of these clusters. The type of gel network formed is determined by pH, solutes and kinetics of gelation.}, booktitle={Functional properties of proteins and lipids}, publisher={Washington, DC: American Chemical Society}, author={Foegeding, E. A. and Gwartney, E. A. and Errington, A. D.}, year={1998}, pages={145–157} }
 @misc{berry_foegeding_1997, title={Cold temperature adaptation and growth of microorganisms}, volume={60}, ISSN={["1944-9097"]}, DOI={10.4315/0362-028X-60.12.1583}, abstractNote={Most microorganisms must accommodate a variety of changing conditions and stresses in their environment in order to survive and multiply. Because of the impact of temperature on all reactions of the cell, adaptations to fluctuations in temperature are possibly the most common. Widespread in the environment and well-equipped for cold temperature growth, psychrophilic and psychrotrophic microorganisms may yet make numerous adjustments when faced with temperatures lower than optimum. Phospholipid and fatty acid alterations resulting in increased membrane fluidity at lower temperatures have been described for many cold tolerant microorganisms while others may make no similar adjustment. While the enzymes of cold growing bacteria have been less extensively studied than those of thermophilic bacteria, it appears that function at low temperature requires enzymes with flexible conformational structure, in order to compensate for lower reaction rates. In many organisms, including psychrophilic and psychrotrophic bacteria, specific sets of cold shock proteins are induced upon abrupt shifts to colder temperatures. While this cold shock response has not been fully delineated, it appears to be adaptive, and may function to promote the expression of genes involved in translation when cells are displaced to lower temperatures. The cold shock response of Escherichia coli has been extensively studied, and the major cold shock protein CspA appears to be involved in the regulation of the response. Upon cold shock, the induction of CspA and its counterparts in most microorganisms studied is prominent, but transient; studies of this response in some psychrotrophic bacteria have reported constitutive synthesis and continued synthesis during cold temperature growth of CspA homologues, and it will be interesting to learn if these are common mechanisms of among cold tolerant organisms. Psychrotrophic microorganisms continue to be a spoilage and safety problem in refrigerated foods, and a greater understanding of the physiological mechanisms and implications of cold temperature adaptation and growth should enhance our ability to design more effective methods of preservation.}, number={12}, journal={JOURNAL OF FOOD PROTECTION}, author={Berry, ED and Foegeding, PM}, year={1997}, month={Dec}, pages={1583–1594} }
 @article{sherwin_foegeding_1997, title={The effects of CaCi2 on aggregation of whey proteins}, volume={52}, number={2}, journal={Milchwissenschaft [Milk Science International]}, author={Sherwin, C. P. and Foegeding, E. A.}, year={1997}, pages={93–96} }
 @inproceedings{foegeding_lowe_hill_1997, title={The properties of heat-induced whey protein concentrate gels produced from lactic whey containing only beta-lactoglobulin A, only beta-lactoglobulin B, or a mixture of beta-lactoglobulin A and B}, number={1997}, booktitle={Milk protein polymorphism: Proceedings of the IDF seminar held in Palmerston North, New Zealand, February 1997}, publisher={Brussels: International Dairy Federation}, author={Foegeding, E. A. and Lowe, R. and Hill, J. P.}, year={1997}, pages={146–157} }
 @article{foegeding_gonzalez_hamann_case_1994, title={POLYACRYLAMIDE GELS AS ELASTIC MODELS FOR FOOD GELS}, volume={8}, ISSN={["0268-005X"]}, DOI={10.1016/S0268-005X(09)80038-6}, abstractNote={The physical properties of Polyacrylamide gels (10% w/v) were evaluated by dynamic oscillatory testing, stress relaxation and torsional fracture analysis. Gels had a linear relationship between shear stress and strain when deformed to fracture; thus small strain (storage modulus, G′) and large strain (fracture modulus, Gf) moduli were equivalent. Non-fracture and fracture tests showed that gels maintained an entropy (rubber) elastic response over all testing temperatures (10–80°C). Shear stress at fracture was independent of temperature, whereas shear strain at fracture decreased as temperature increased. This was associated with increased thermal motion strains decreasing the amount of mechanically induced strain required for fracture. Our results have shown that Polyacrylamide gels are a suitable elastic model for understanding the molecular mechanisms of food texture.}, number={2}, journal={FOOD HYDROCOLLOIDS}, author={FOEGEDING, EA and GONZALEZ, C and HAMANN, DD and CASE, S}, year={1994}, month={May}, pages={125–134} }
 @article{foegeding_kuhn_hardin_1992, title={SPECIFIC DIVALENT CATION-INDUCED CHANGES DURING GELATION OF BETA-LACTOGLOBULIN}, volume={40}, ISSN={["0021-8561"]}, DOI={10.1021/jf00023a011}, abstractNote={Thermally induced gelation of β-lactoglobulin sols that contained NaCl and/or CaCl 2 at pH 7.0 and the rheological properties of the resulting gels were investigated. Gels confining 20 mM CaCl 2 were more deformable than gels confining 100 mM NaCl since a greater shear strain was required to achieve fracture. Investigating the gelation process by small-strain dynamic rheology showed that β-lactoglobulin sols confining 20 mM CaCl 2 gelled more rapidly and had lower gel points than similar sols confining 100 mM NaCl}, number={11}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={FOEGEDING, EA and KUHN, PR and HARDIN, CC}, year={1992}, month={Nov}, pages={2092–2097} }