@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={Abstract}, 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{salaheen_white_bequette_biswas_2014, title={Peanut fractions boost the growth of Lactobacillus casei that alters the interactions between Campylobacter jejuni and host epithelial cells}, volume={62}, ISSN={["1873-7145"]}, DOI={10.1016/j.foodres.2014.05.061}, abstractNote={Since gut microbiota elicit host responses that impact human health and affect the nutritional value of animal products, the modulation of gut flora with a combination of natural prebiotics and probiotics, known as synbiotic, is an area of significant research interest. In this study, we evaluated the role of peanut fractions on the growth of Lactobacillus casei and Campylobacter jejuni, a probiotic and pathogenic bacteria, respectively. Moreover, in a co-culture system, we investigated whether there are synergistic effects between the bacterium in the presence of the peanut fraction. We observed that water-soluble (5 g/L) and alcalase-treated peanut fraction significantly stimulated L. casei growth by more than 1.5 logs at 24 h. However, the peanut fraction had no direct effect on C. jejuni growth. Analysis of the fatty acids profile suggested that the higher percentage of oleic acid present in peanuts might be responsible for stimulation of L. casei growth. The initial pH of medium ranging from 6 to 8 did not alter the growth of C. jejuni. In a co-culture system in the presence of the water soluble peanut fraction, the growth of C. jejuni was inhibited in a time dependent manner, reaching the highest level of inhibition (~ 2 logs) at 72 h, while no growth difference was observed in absence of peanut fractions or even in presence of alcalase-treated peanut fraction. In addition, L. casei competitively reduced the colonization of C. jejuni on human intestinal epithelial (INT407) cells. Our data suggest that peanut fraction induced the growth of L. casei, which in turn led to a reduction in the growth of C. jejuni as well as its colonization. Therefore, we hypothesize that regular consumption of peanuts may positively impact on the composition of human gut microbiota and decrease the burden of gastrointestinal infections by enteric bacterial pathogens.}, journal={FOOD RESEARCH INTERNATIONAL}, author={Salaheen, Serajus and White, Brittany and Bequette, Brian J. and Biswas, Debabrata}, year={2014}, month={Aug}, pages={1141–1146} }
 @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{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} }