@article{weng_liu_white_chang_davis_hsiao_chiou_2022, title={Allergenicity reduction of the bio-elicited peanut sprout powder (BPSP) and toxicological acceptance of BPSP-supplemented diets assessed with ICR mice}, ISSN={["0975-8402"]}, DOI={10.1007/s13197-022-05537-7}, abstractNote={The allergenic and toxicological acceptances of the bio-elicited peanut sprout powder (BPSP) have not been assessed. BPSP was generated from peanut kernels germinated at 26-28 °C for 72 h (designated as 72 h-NGS). The 72 h-NGS were subsequently sliced, incubated, dried, defatted and pulverized to generate bio-elicited peanut sprout powder (BPSP). Protein solubility of BPSP increased 2.6-fold compared to 72 h-NGS. SDS-PAGE analysis revealed BPSP production triggered extensive degradation of the high-molecular weight peanut allergic proteins, mainly Ara h 1 and Ara h 3. Western blotting detected with peanut allergic patients' IgE indicated decreased in vitro reactivity. Food safety assessment of BPSP was performed with ICR mice fed with basal (control) and three doses of formulated BPSP-supplemented diets containing 0.11 g (normal), 2.5 g (high) and 25 g (super high) BPSP /kg BW. Animals appeared healthy with steady body weight gain in all groups during the entire 35-day dietary intervention. Hematological and serum biochemical analyses revealed no significant difference among groups. Histopathological examination on the tissue sections of primary organs further supported safety with no pathologies. The in vitro allergic reduction and toxicological safety in the BPSP-supplemented dietary intervention in the ICR mice study, support moving forward with BPSP-involved product development.The online version contains supplementary material available at 10.1007/s13197-022-05537-7.}, journal={JOURNAL OF FOOD SCIENCE AND TECHNOLOGY-MYSORE}, author={Weng, Brian B. -C. and Liu, Yu-Chia and White, Brittany L. and Chang, Ju-Chun and Davis, Jack P. and Hsiao, Shih-Hsuan and Chiou, Robin Y. -Y.}, year={2022}, month={Jul} }
 @article{ramesh_davis_roros_eiben_fabiani_smith_reynolds_pourdeyhimi_khan_genzer_et al._2021, title={Dual-Responsive Microgels for Structural Repair and Recovery of Nonwoven Membranes for Liquid Filtration}, volume={3}, ISSN={["2637-6105"]}, url={https://doi.org/10.1021/acsapm.0c01360}, DOI={10.1021/acsapm.0c01360}, abstractNote={This study presents dual-responsive colloidal microgels to repair nonwoven fiber mats (NWFs) and recover their native morphological and functional properties. The formulation comprises poly(N-isopr...}, number={3}, journal={ACS APPLIED POLYMER MATERIALS}, publisher={American Chemical Society (ACS)}, author={Ramesh, Srivatsan and Davis, Jack and Roros, Alexandra and Eiben, Justin and Fabiani, Thomas and Smith, Ryan and Reynolds, Lewis and Pourdeyhimi, Behnam and Khan, Saad and Genzer, Jan and et al.}, year={2021}, month={Mar}, pages={1508–1517} }
 @article{davis_agraz_kline_gottschall_nolt_whitaker_osborne_tengstrand_ostrowski_teixeira_et al._2021, title={Measurements of High Oleic Purity in Peanut Lots Using Rapid, Single Kernel Near-Infrared Reflectance Spectroscopy}, volume={98}, ISSN={["1558-9331"]}, DOI={10.1002/aocs.12487}, abstractNote={Abstract High oleic peanuts have improved shelf life vs. conventional peanuts. Purity (percentage of high oleic peanuts within a lot) is critical to ingredient performance and final lot value. Contamination can result from unintentional mix‐ups at the breeder/seed level, improper production handling, or due to physiologically immature high oleic kernels. Therefore, industry groups have established unofficial sampling plans to monitor purity. Assuming equivalent measurement performance and simple random sampling, increasing the sample size decreases variance among replicated sample test results and increases the precision of estimated lot purity. A novel instrument (QSorter Explorer by QualySense AG) using near‐infrared reflectance spectroscopy was evaluated for high speed (20 kernels per second) high oleic purity measurements. The study objectives were to assess instrument performance in: (1) measuring oleic acid (%) in runner peanuts and (2) estimating the true high oleic purity of artificially mixed peanut lots. Three grades (Jumbo, Medium, and No 1) of US Runner mini‐lots each at seven different contamination levels (0, 5, 10, 20, 30, 50, and 100%) were prepared. Oleic acid (%) of individual kernels was measured by scanning replicated samples of 10, 50, 100, and 500 kernels using the QSorter Explorer. The variance associated with each sample size and lot contamination level on returned purity values is discussed in the context of binomial sampling. Overall, the demonstrated measurement performance and capacity of the QSorter Explorer to process much larger sample sizes suggest this instrument can better identify true high oleic peanut lot purity vs. other currently available technologies.}, number={6}, journal={JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY}, author={Davis, Brittany I and Agraz, Catherine B. and Kline, Mark and Gottschall, Emma and Nolt, Michael and Whitaker, Thomas B. and Osborne, Jason A. and Tengstrand, Erik and Ostrowski, Kamil and Teixeira, Rita and et al.}, year={2021}, month={Jun}, pages={621–632} }
 @article{shi_davis_xia_sandeep_sanders_dean_2017, title={Characterization of peanuts after dry roasting, oil roasting, and blister frying}, volume={75}, ISSN={["1096-1127"]}, DOI={10.1016/j.lwt.2016.09.030}, abstractNote={Peanuts were systematically deep fried, blister fried, or dry roasted at 177 °C to Hunter L-values of 53.0 ± 1.0, 48.5 ± 1.0, and 43.0 ± 1.0, corresponding to light, medium, and dark roasting, respectively. Thermal modifications of the epidermal and parenchyma cells were observed in the scanning electron microscopic images for processed peanuts, compared to raw peanuts. Peanut microstructure was most extensively damaged by blister frying, followed by deep frying, and then dry roasting. The moisture content decreased with increased surface color, due to more moisture loss with longer heat processing time. For light roasting, blister fried peanuts had significantly higher moisture contents than the deep fried and dry roasted peanuts, while for medium and dark roasting, blister fried had lower moistures than the other two. Descriptive sensory analysis was able to distinguish the flavor and texture profiles of peanuts prepared by different roasting methods. In storage testing throughout 16 weeks, peroxide value measurements indicated the blister fried peanuts had the longest shelf life, followed by the dry roasted, and then the deep fried. Descriptive sensory analysis proved that the rate of the loss of roast peanut flavor during storage was faster in dry roasted peanuts followed by blister fried and deep fried.}, journal={LWT-FOOD SCIENCE AND TECHNOLOGY}, author={Shi, Xiaolei and Davis, Jack P. and Xia, Zhoutong and Sandeep, K. P. and Sanders, Timothy H. and Dean, Lisa O.}, year={2017}, month={Jan}, pages={520–528} }
 @article{shi_sandeep_davis_sanders_dean_2017, title={Kinetics of color development of peanuts during dry roasting using a batch roaster}, volume={40}, ISSN={["1745-4530"]}, DOI={10.1111/jfpe.12498}, abstractNote={Abstract}, number={3}, journal={JOURNAL OF FOOD PROCESS ENGINEERING}, author={Shi, Xiaolei and Sandeep, K. P. and Davis, Jack P. and Sanders, Timothy H. and Dean, Lisa L.}, year={2017}, month={Jun} }
 @article{white_sanders_davis_2014, title={Potential ACE-inhibitory activity and nanoLC-MS/MS sequencing of peptides derived from aflatoxin contaminated peanut meal}, volume={56}, ISSN={["1096-1127"]}, DOI={10.1016/j.lwt.2013.11.039}, abstractNote={Our lab has developed a process for sequestering aflatoxin from contaminated peanut meal (PM) using commercial bentonite clays while protein is simultaneously extracted and hydrolyzed by a commercial protease. The objectives of this study were to sequence generated peptides and evaluate their potential ACE-inhibitory properties. Aflatoxin in the unprocessed PM was 610 μg kg−1 compared to 9.7 μg kg−1 on a dry weight basis in the 120 min hydrolysate. This hydrolysate displayed significant ACE-inhibitory activity with an IC50 of 295.1 μg mL−1. Ultrafiltration and size exclusion chromatography (SEC) improved the ACE-inhibitory properties, with the SEC fraction containing the smallest peptides having an IC50 = 44.4 μg mL−1. Additionally, 271 unique peptides were identified by nanoLC-MS/MS, of which 147 belonged to major seed storage proteins. This advanced characterization data will ultimately allow for more efficient production of hydrolysates with ACE-inhibitory activity or other bioactivities of interest from PM.}, number={2}, journal={LWT-FOOD SCIENCE AND TECHNOLOGY}, author={White, Brittany L. and Sanders, Timothy H. and Davis, Jack P.}, year={2014}, month={May}, pages={537–542} }
 @article{white_shi_burk_kulis_burks_sanders_davis_2014, title={Strategies to Mitigate Peanut Allergy: Production, Processing, Utilization, and Immunotherapy Considerations}, volume={5}, ISSN={["1941-1421"]}, DOI={10.1146/annurev-food-030713-092443}, abstractNote={ Peanut (Arachis hypogaea L.) is an important crop grown worldwide for food and edible oil. The surge of peanut allergy in the past 25 years has profoundly impacted both affected individuals and the peanut and related food industries. In response, several strategies to mitigate peanut allergy have emerged to reduce/eliminate the allergenicity of peanuts or to better treat peanut-allergic individuals. In this review, we give an overview of peanut allergy, with a focus on peanut proteins, including the impact of thermal processing on peanut protein structure and detection in food matrices. We discuss several strategies currently being investigated to mitigate peanut allergy, including genetic engineering, novel processing strategies, and immunotherapy in terms of mechanisms, recent research, and limitations. All strategies are discussed with considerations for both peanut-allergic individuals and the numerous industries/government agencies involved throughout peanut production and utilization. }, journal={ANNUAL REVIEW OF FOOD SCIENCE AND TECHNOLOGY, VOL 5}, author={White, Brittany L. and Shi, Xiaolei and Burk, Caitlin M. and Kulis, Michael and Burks, A. Wesley and Sanders, Timothy H. and Davis, Jack P.}, year={2014}, pages={155–176} }
 @article{shi_guo_white_yancey_sanders_davis_burks_kulis_2013, title={Allergenic Properties of Enzymatically Hydrolyzed Peanut Flour Extracts}, volume={162}, ISSN={["1423-0097"]}, DOI={10.1159/000351920}, abstractNote={<b><i>Background:</i></b> Peanut flour is a high-protein, low-oil, powdered material prepared from roasted peanut seed. In addition to being a well-established food ingredient, peanut flour is also the active ingredient in peanut oral immunotherapy trials. Enzymatic hydrolysis was evaluated as a processing strategy to generate hydrolysates from peanut flour with reduced allergenicity. <b><i>Methods:</i></b> Soluble fractions of 10% (w/v) light roasted peanut flour dispersions were hydrolyzed with the following proteases: Alcalase (pH 8.0, 60°C), pepsin (pH 2.0, 37°C) or Flavourzyme (pH 7.0, 50°C) for 60 min. Western blotting, inhibition ELISA and basophil activation tests were used to examine IgE reactivity. <b><i>Results:</i></b> Western blotting experiments revealed the hydrolysates retained IgE binding reactivity and these IgE-reactive peptides were primarily Ara h 2 fragments regardless of the protease tested. Inhibition ELISA assays demonstrated that each of the hydrolysates had decreased capacity to bind peanut-specific IgE compared with nonhydrolyzed controls. Basophil activation tests revealed that all hydrolysates were comparable (p > 0.05) to nonhydrolyzed controls in IgE cross-linking capacity. <b><i>Conclusions:</i></b> These results indicate that hydrolysis of peanut flour reduced IgE binding capacity; however, IgE cross-linking capacity during hydrolysis was retained, thus suggesting such hydrolysates are not hypoallergenic.}, number={2}, journal={INTERNATIONAL ARCHIVES OF ALLERGY AND IMMUNOLOGY}, author={Shi, Xiaolei and Guo, Rishu and White, Brittany L. and Yancey, Adrienne and Sanders, Timothy H. and Davis, Jack P. and Burks, A. Wesley and Kulis, Michael}, year={2013}, pages={25–32} }
 @article{white_goekce_nepomuceno_muddiman_sanders_davis_2013, title={Comparative Proteomic Analysis and IgE Binding Properties of Peanut Seed and Testa (Skin)}, volume={61}, ISSN={["1520-5118"]}, DOI={10.1021/jf400184y}, abstractNote={To investigate the protein composition and potential allergenicity of peanut testae or skins, proteome analysis was conducted using nanoLC-MS/MS sequencing. Initial amino acid analysis suggested differences in protein compositions between the blanched seed (skins removed) and skin. Phenolic compounds hindered analysis of proteins in skins when the conventional extraction method was used; therefore, phenol extraction of proteins was necessary. A total of 123 proteins were identified in blanched seed and skins, and 83 of the proteins were common between the two structures. The skins contained all of the known peanut allergens in addition to 38 proteins not identified in the seed. Multiple defense proteins with antifungal activity were identified in the skins. Western blotting using sera from peanut-allergic patients revealed that proteins extracted from both the blanched seed and skin bound significant levels of IgE. However, when phenolic compounds were present in the skin protein extract, no IgE binding was observed. These findings indicate that peanut skins contain potentially allergenic proteins; however, the presence of phenolic compounds may attenuate this effect.}, number={16}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={White, Brittany L. and Goekce, Emine and Nepomuceno, Angelito I. and Muddiman, David C. and Sanders, Timothy H. and Davis, Jack P.}, year={2013}, month={Apr}, pages={3957–3968} }
 @article{white_oakes_shi_price_lamb_sobolev_sanders_davis_2013, title={Development of a pilot-scale process to sequester aflatoxin and release bioactive peptides from highly contaminated peanut meal}, volume={51}, ISSN={["1096-1127"]}, DOI={10.1016/j.lwt.2012.10.022}, abstractNote={Peanut meal (PM) is the high protein by-product remaining after commercial extraction of peanut oil. PM applications are limited because of typical high concentrations of aflatoxin. For the first time, pilot-scale extraction of protein and sequestration of aflatoxin from PM were evaluated. Aqueous PM dispersions were mixed with two commercial bentonite clays and Alcalase in a jacketed mixer, hydrolysed for 1 h, heated to inactivate protease, and solids and liquids were separated using a decanter. Liquid hydrolysates derived from this process had >90% reduction in aflatoxin when clay was present. ACE-inhibitory activities of these hydrolysates suggest a potential benefit for blood pressure regulation. The insoluble fractions from the dispersions were dried and used in a separate turkey poult feeding study. These results indicate that scale-up of this novel process is feasible and offers a means for adding value to this underutilized protein source.}, number={2}, journal={LWT-FOOD SCIENCE AND TECHNOLOGY}, author={White, Brittany L. and Oakes, Aaron J. and Shi, Xiaolei and Price, Kristin M. and Lamb, Marshall C. and Sobolev, Victor S. and Sanders, Timothy H. and Davis, Jack P.}, year={2013}, month={May}, pages={492–499} }
 @article{oakes_white_lamb_sobolev_sanders_davis_2013, title={Process development for spray drying a value-added extract from aflatoxin-contaminated peanut meal}, volume={48}, ISSN={["1365-2621"]}, DOI={10.1111/j.1365-2621.2012.03158.x}, abstractNote={Summary}, number={1}, journal={INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY}, author={Oakes, Aaron J. and White, Brittany L. and Lamb, Marshall and Sobolev, Victor and Sanders, Timothy H. and Davis, Jack P.}, year={2013}, month={Jan}, pages={58–66} }
 @article{athalye_sharma-shivappa_peretti_kolar_davis_2013, title={Producing biodiesel from cottonseed oil using Rhizopus oryzae ATCC #34612 whole cell biocatalysts: Culture media and cultivation period optimization}, volume={17}, ISSN={0973-0826}, url={http://dx.doi.org/10.1016/J.ESD.2013.03.009}, DOI={10.1016/j.esd.2013.03.009}, abstractNote={The effect of culture medium composition and cultivation time on biodiesel production by Rhizopus oryzae ATCC #34612 whole cell catalysts, immobilized on novel rigid polyethylene biomass supports, was investigated. Supplementation of the medium with carbon sources led to higher lipase activity and increased the biomass immobilized on the BSPs. Statistical analysis indicates that a cultivation period of 72 h in a basal medium supplemented with both cottonseed oil and glucose is optimal for biodiesel production by R. oryzae, resulting in a fatty acid methyl ester (FAME) yield of 27.9 wt.% (228.2 g/L).}, number={4}, journal={Energy for Sustainable Development}, publisher={Elsevier BV}, author={Athalye, Sneha and Sharma-Shivappa, Ratna and Peretti, Steven and Kolar, Praveen and Davis, Jack P.}, year={2013}, month={Aug}, pages={331–336} }
 @article{davis_sweigart_price_dean_sanders_2013, title={Refractive Index and Density Measurements of Peanut Oil for Determining Oleic and Linoleic Acid Contents}, volume={90}, ISSN={["1558-9331"]}, DOI={10.1007/s11746-012-2153-4}, abstractNote={Abstract}, number={2}, journal={JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY}, author={Davis, Jack P. and Sweigart, Daniel S. and Price, Kristin M. and Dean, Lisa L. and Sanders, Timothy H.}, year={2013}, month={Feb}, pages={199–206} }
 @article{mcdaniel_white_dean_sanders_davis_2012, title={Compositional and Mechanical Properties of Peanuts Roasted to Equivalent Colors using Different Time/Temperature Combinations}, volume={77}, ISSN={["0022-1147"]}, DOI={10.1111/j.1750-3841.2012.02979.x}, abstractNote={Abstract:  Peanuts in North America and Europe are primarily consumed after dry roasting. Standard industry practice is to roast peanuts to a specific surface color (Hunter L‐value) for a given application; however, equivalent surface colors can be attained using different roast temperature/time combinations, which could affect product quality. To investigate this potential, runner peanuts from a single lot were systematically roasted using 5 roast temperatures (147, 157, 167, 177, and 187 °C) and to Hunter L‐values of 53 ± 1, 48.5 ± 1, and 43 ± 1, corresponding to light, medium, and dark roasts, respectively. Moisture contents (MC) ranged from 0.41% to 1.70% after roasting. At equivalent roast temperatures, MC decreased as peanuts became darker; however, for a given color, MC decreased with decreasing roast temperature due to longer roast times required for specified color formation. Initial total tocopherol contents of expressed oils ranged from 164 to 559 μg/g oil. Peanuts roasted at lower temperatures and darker colors had higher tocopherol contents. Glucose content was roast color and temperature dependent, while fructose was only temperature dependent. Soluble protein was lower at darker roast colors, and when averaged across temperatures, was highest when samples were roasted at 187 °C. Lysine content decreased with increasing roast color but was not dependent on temperature. MC strongly correlated with several components including tocopherols (R2 = 0.67), soluble protein (R2 = 0.80), and peak force upon compression (R2 = 0.64). The variation in characteristics related to roast conditions is sufficient to suggest influences on final product shelf life and consumer acceptability.}, number={12}, journal={JOURNAL OF FOOD SCIENCE}, author={McDaniel, Kristin A. and White, Brittany L. and Dean, Lisa L. and Sanders, Timothy H. and Davis, Jack P.}, year={2012}, month={Dec}, pages={C1292–C1298} }
 @article{jairam_kolar_sharma-shivappa_osborne_davis_2012, title={KI-impregnated oyster shell as a solid catalyst for soybean oil transesterification}, volume={104}, ISSN={["1873-2976"]}, DOI={10.1016/j.biortech.2011.10.039}, abstractNote={Research on inexpensive and green catalysts is needed for economical production of biodiesel. The goal of the research was to test KI-impregnated calcined oyster shell as a solid catalyst for transesterification of soybean oil. Specific objectives were to characterize KI-impregnated oyster shell, determine the effect of reaction variables and reaction kinetics. The catalyst was synthesized by impregnating KI on calcined oyster shells. X-ray diffraction analysis indicated the presence of portlandite and potassium iodide on the surface and a 31-fold increase in surface as a result of calcination and KI impregnation. Under the conditions tested, ideal reaction variables were 1 mmol g−1 for catalyst loading, 50 °C for temperature, 10:1 for methanol/oil, and 4 h for reaction time. The transesterification followed a first-order reaction (k = 0.4385 h−1). The option of using oyster shell for the production of transesterification catalysts could have economic benefits to the aquaculture industry in the US.}, journal={BIORESOURCE TECHNOLOGY}, author={Jairam, Suguna and Kolar, Praveen and Sharma-Shivappa, Ratna and Osborne, Jason A. and Davis, Jack P.}, year={2012}, month={Jan}, pages={329–335} }
 @article{kane_davis_oakes_dean_sanders_2012, title={VALUE-ADDED PROCESSING OF PEANUT MEAL: ENZYMATIC HYDROLYSIS TO IMPROVE FUNCTIONAL AND NUTRITIONAL PROPERTIES OF WATER SOLUBLE EXTRACTS}, volume={36}, ISSN={["1745-4514"]}, DOI={10.1111/j.1745-4514.2011.00566.x}, abstractNote={Value-added applications are needed for peanut meal, which is the high-protein by-product of commercial peanut oil production. Peanut meal dispersions were hydrolyzed with alcalase, flavourzyme and pepsin in an effort to improve functional and nutritional properties of the resulting water soluble extracts. Degree of hydrolysis (DH) ranged from 20 to 60% for alcalase, 10 to 20% for pepsin and 10 to 70% for flavourzyme from 3 to 240 min. Low molecular weight peptides (<14 kDa) and unique banding patterns reflected the different proteolytic activities of each enzyme as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Total soluble solids and soluble nitrogen increased a minimum of 30 and 110%, respectively, for all hydrolysates after 4-h hydrolysis. Differences in air/water adsorption responses of hydrolysates were a function of protease specificity. Antioxidant capacities of all hydrolysates were greater than unhydrolyzed controls and correlated linearly (R2 = 0.87) with DH, whereas antioxidant capacities of hydrolysates were minimally dependent on bicinchoninic acid protein solubility or relative amino acid distribution. 
 
 
 
PRACTICAL APPLICATIONS 
 
Peanut meal is the high-protein by-product of commercial peanut oil production. While an excellent source of protein, aflatoxin contamination currently limits applications of peanut meal to feed markets. Recently described efforts to sequester aflatoxin from peanut meal during processing have proven successful, potentially allowing for processing of this material into value-added components including aflatoxin-free protein/peptide concentrates. Accordingly, the current manuscript focuses on the potential for enzymatic hydrolysis (three different proteases are compared) to improve functional and nutritional properties of peanut meal during processing. Enzymatic hydrolysis substantially increases solubility and antioxidant capacities of peanut meal hydrolysates. A potential mechanism for increased antioxidant capacity with increasing hydrolysis is discussed. These and other chemical/functional data within the manuscript directly apply to strategies for value-added processing of peanut meal.}, number={5}, journal={JOURNAL OF FOOD BIOCHEMISTRY}, author={Kane, Lauren E. and Davis, Jack P. and Oakes, Aaron J. and Dean, Lisa L. and Sanders, Timothy H.}, year={2012}, month={Oct}, pages={520–531} }
 @inproceedings{mcdaniel_mifsud_lechat_schneider_sanders_davis_2011, title={Kinetics of dry roasting as related to peanut quality}, volume={1362}, booktitle={Olfaction and electronic nose: proceedings of the 14th international symposium on olfaction and electronic nose}, author={McDaniel, K. A. and Mifsud, J. C. and Lechat, H. and Schneider, C. and Sanders, T. H. and Davis, J. P.}, year={2011}, pages={81–83} }
 @article{stephens_dean_davis_osborne_sanders_2010, title={Peanuts, Peanut Oil, and Fat Free Peanut Flour Reduced Cardiovascular Disease Risk Factors and the Development of Atherosclerosis in Syrian Golden Hamsters}, volume={75}, ISSN={["1750-3841"]}, DOI={10.1111/j.1750-3841.2010.01569.x}, abstractNote={ABSTRACT:  Human clinical trials have demonstrated the cardiovascular protective properties of peanuts and peanut oil in decreasing total and low density lipoprotein cholesterol (LDL‐C) without reducing high density lipoprotein cholesterol (HDL‐C). The cardiovascular effects of the nonlipid portion of peanuts has not been evaluated even though that fraction contains arginine, flavonoids, folates, and other compounds that have been linked to cardiovascular health. The objective of this study was to evaluate the effects of fat free peanut flour (FFPF), peanuts, and peanut oil on cardiovascular disease (CVD) risk factors and the development of atherosclerosis in male Syrian golden hamsters. Each experimental diet group was fed a high fat, high cholesterol diet with various peanut components (FFPF, peanut oil, or peanuts) substituted for similar metabolic components in the control diet. Tissues were collected at week 0, 12, 18, and 24. Total plasma cholesterol (TPC), LDL‐C, and HDL‐C distributions were determined by high‐performance gel filtration chromatography, while aortic total cholesterol (TC) and cholesteryl ester (CE) were determined by gas liquid chromatography. Peanuts, peanut oil, and FFPF diet groups had significantly (P < 0.05) lower TPC, non‐HDL‐C than the control group beginning at about 12 wk and continuing through the 24‐wk study. HDL‐C was not significantly different among the diet groups. Peanut and peanut component diets retarded an increase in TC and CE. Because CE is an indicator of the development of atherosclerosis this study demonstrated that peanuts, peanut oil, and FFPF retarded the development of atherosclerosis in animals consuming an atherosclerosis inducing diet.}, number={4}, journal={JOURNAL OF FOOD SCIENCE}, author={Stephens, Amanda M. and Dean, Lisa L. and Davis, Jack P. and Osborne, Jason A. and Sanders, Timothy H.}, year={2010}, month={May}, pages={H116–H122} }
 @article{davis_dean_price_sanders_2010, title={Roast effects on the hydrophilic and lipophilic antioxidant capacities of peanut flours, blanched peanut seed and peanut skins}, volume={119}, ISSN={["0308-8146"]}, DOI={10.1016/j.foodchem.2009.06.057}, abstractNote={Hydrophilic and lipophilic oxygen radical antioxidant capacity (H&L-ORAC) of peanut flours, blanched peanut seed, and peanut skins were characterised across a range of roast intensities. H-ORAC ranged from 5910 to 7990, 3040 to 3700 and 152,290 to 209,710 μmoles Trolox/100 g for the flours, seed, and skins, respectively. H-ORAC increased linearly with darker seed colour after roasting at 166 °C from 0 to 77 min, whereas skin H-ORAC peaked after roasting for 7 min. Linear correlations with H-ORAC and total phenolic content were observed. Additionally, completely defatted peanut seed were solubilised (5% w/w) in water and H-ORAC measured. For these samples, H-ORAC decreased with roast intensity which correlated with soluble protein. L-ORAC ranged from 620 to 1120, 150 to 730 and 2150 to 6320 μmoles Trolox/100 g for peanut flours, seed, and skins, respectively. L-ORAC increased linearly with both darker seed colour and skin colour across the 77 min range. L-ORACs of roasted peanuts and ingredients are discussed in terms of tocopherol contents and Maillard reaction products.}, number={2}, journal={FOOD CHEMISTRY}, author={Davis, J. P. and Dean, L. L. and Price, K. M. and Sanders, T. H.}, year={2010}, month={Mar}, pages={539–547} }
 @article{seifert_davis_dorner_jaynes_zartman_sanders_2010, title={Value-Added Processing of Peanut Meal: Aflatoxin Sequestration during Protein Extraction}, volume={58}, ISSN={["1520-5118"]}, DOI={10.1021/jf9045304}, abstractNote={The efficacy of a bentonite clay, Astra-Ben 20A (AB20A), to sequester aflatoxin from contaminated (approximately 110 ppb) peanut meal during protein extraction was studied. Aqueous peanut meal dispersions (10% w/w) were prepared by varying the pH, temperature, enzymatic hydrolysis conditions, and concentrations of AB20A. After extraction, dispersions were centrifuged and filtered to separate both the water-soluble and the water-insoluble fractions for subsequent testing. Inclusion of AB20A at 0.2 and 2% reduced (p < 0.05) aflatoxin concentrations below 20 ppb in both fractions; however, the higher concentration of AB20A also reduced (p < 0.05) the water-soluble protein content. Inclusion of 0.2% AB20A did not affect protein solubility, total soluble solids, or degree of hydrolysis. Peanut meal adsorption isotherms measured the AB20A capacity to sequester aflatoxin. These results are discussed in the context of a process designed to sequester aflatoxin from contaminated peanut meal, which could enable derivatives of this high protein material to be utilized in enhanced feed and/or food applications.}, number={9}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Seifert, Lauren E. and Davis, Jack P. and Dorner, Joe W. and Jaynes, William F. and Zartman, Richard E. and Sanders, Timothy H.}, year={2010}, month={May}, pages={5625–5632} }
 @article{karakoti_monteiro-riviere_aggarwal_davis_narayan_self_mcginnis_seal_2008, title={Nanoceria as antioxidant: Synthesis and biomedical applications}, volume={60}, ISSN={["1543-1851"]}, url={http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000253852900008&KeyUID=WOS:000253852900008}, DOI={10.1007/s11837-008-0029-8}, abstractNote={The therapeutic application of nanomaterials has been a focus of numerous studies in the past decade. Due to its unique redox properties, cerium oxide (ceria) is finding widespread use in the treatment of medical disorders caused by the reactive oxygen intermediates (ROI). The radical-scavenging role of ceria nanoparticles (nanoceria) have been established, as well as the autocatalytic ability of nanoceria to regenerate under various environmental conditions. The synthesis of nanoceria in biocompatible media has also been reported along with cell viability in order to determine the potential use of nanoceria in biomedical applications.}, number={3}, journal={JOM}, author={Karakoti, A. S. and Monteiro-Riviere, N. A. and Aggarwal, R. and Davis, J. P. and Narayan, R. J. and Self, W. T. and McGinnis, J. and Seal, S.}, year={2008}, month={Mar}, pages={33–37} }
 @article{davis_dean_faircloth_sanders_2008, title={Physical and chemical characterizations of normal and high-oleic oils from nine commercial cultivars of peanut}, volume={85}, ISSN={["0003-021X"]}, DOI={10.1007/s11746-007-1190-x}, abstractNote={Abstract}, number={3}, journal={JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY}, author={Davis, J. P. and Dean, L. O. and Faircloth, W. H. and Sanders, T. H.}, year={2008}, month={Mar}, pages={235–243} }
 @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{davis_sanders_2007, title={Liquid to semisolid rheological transitions of normal and high-oleic peanut oils upon cooling to refrigeration temperatures}, volume={84}, ISSN={["1558-9331"]}, DOI={10.1007/s11746-007-1133-6}, abstractNote={Abstract}, number={11}, journal={JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY}, author={Davis, J. P. and Sanders, T. H.}, year={2007}, month={Nov}, pages={979–987} }
 @article{davis_gharst_sanders_2007, title={Some rheological properties of aqueous peanut flour dispersions}, volume={38}, ISSN={["0022-4901"]}, DOI={10.1111/j.1745-4603.2007.00097.x}, abstractNote={ABSTRACT The rheological behaviors of aqueous peanut flour dispersions were characterized across a range of conditions, including controlled heating and cooling rates under both large‐ and small‐strain deformations. Fat content of the dry flours influenced rheological changes, as dispersions of higher‐fat flours were less viscous than lower‐fat flours on an equal weight basis. A roast effect was also apparent, especially for dispersions of the higher‐fat flours in which light roast flours were more viscous than dark roast flours. Dispersions of toasted soy flour were more viscous at lower temperatures (<75C), but at higher temperatures, low‐fat peanut flour dispersions were more viscous than soy. Centrifugal separation revealed that the insoluble material of all dispersions primarily contributed to the observed rheological responses. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis  was used to characterize the soluble and insoluble proteins making up the various dispersions, and these results are discussed in terms of observed rheological phenomena.}, number={2}, journal={JOURNAL OF TEXTURE STUDIES}, author={Davis, J. P. and Gharst, G. and Sanders, T. H.}, year={2007}, month={Apr}, pages={253–272} }
 @article{gharst_clare_davis_sanders_2007, title={The effect of transglutaminase crosslinking on the rheological characteristics of heated peanut flour dispersions}, volume={72}, ISSN={["0022-1147"]}, DOI={10.1111/j.1750-3841.2007.00442.x}, abstractNote={ABSTRACT:  Peanut flour (PF) is a high‐protein ingredient prepared after the partial extraction of oil from roasted peanut seed. Microbial transglutaminase (TGase) catalyzes protein crosslinking via acyl‐transfer reactions, resulting in the modification of functional properties such as viscosity, gelation, solubility, and water holding capacity. This work was conducted to observe changes in rheological properties of PF dispersions in the presence and the absence of TGase and amidated pectin (AP). Dispersions were characterized across a range of conditions, including controlled heating and cooling rates under both large‐ and small‐strain deformations. Gelation occurred at temperatures above 78 °C using PF dispersions treated with TGase compared to untreated dispersions devoid of the enzyme (about 68 °C). The addition of AP (0.5%) resulted in a general increase in viscoelasticity for all dispersions. AP addition also minimized the shift in gel point temperature caused by TGase polymerization reactions. High‐molecular‐weight polymers were formed in TGase‐treated PF dispersions in both the presence and the absence of AP; however, polymer formation was more rapid in PF dispersions without AP. Ortho‐phthaldialdehyde assays indicated about 40% protein coupling in PF dispersions treated with TGase compared to about 20% in those containing both AP and TGase. Collectively, these data suggest potential applications of TGase‐treated PF dispersions, both in the presence and the absence of AP, for use in peanut‐base food products, including protein bars, shakes, and value‐added baked goods.}, number={7}, journal={JOURNAL OF FOOD SCIENCE}, author={Gharst, G. and Clare, D. A. and Davis, J. P. and Sanders, T. H.}, year={2007}, month={Sep}, pages={C369–C375} }
 @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} }
 @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{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{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{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} }