@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{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{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{mudgal_breidt_lubkin_sandeep_2006, title={Quantifying the significance of phage attack on starter cultures: a mechanistic model for population dynamics of phage and their hosts isolated from fermenting sauerkraut}, volume={72}, ISSN={["1098-5336"]}, url={http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000238620100013&KeyUID=WOS:000238620100013}, DOI={10.1128/AEM.02429-05}, abstractNote={ABSTRACT}, number={6}, journal={APPLIED AND ENVIRONMENTAL MICROBIOLOGY}, author={Mudgal, P. and Breidt, F., Jr. and Lubkin, S. R. and Sandeep, K. P.}, year={2006}, month={Jun}, pages={3908–3915} }