@article{shi_dean_davis_sandeep_sanders_2018, title={The effects of different dry roast parameters on peanut quality using an industrial belt-type roaster simulator}, volume={240}, ISSN={["1873-7072"]}, DOI={10.1016/j.foodchem.2017.07.130}, abstractNote={Peanuts roasted to equivalent surface colors at different temperature/time combinations can vary substantially in chemical and physical properties related to product quality. This study used a pilot plant scale roaster that simulates the configurations of one of the most common industrial roaster, a multi-zone belt roaster. Jumbo-size runner-type peanuts were systematically roasted at 5 temperatures (149-204°C) to three Hunter l-values of 53, 48.5, and 43, corresponding to light, medium, and dark roasts. Moisture and tocopherol contents were more closely correlated with roast color rather than temperature, with exceptions at 149°C. Moisture decreased with darker roast color, while the total tocopherols were greatest in peanut oils with darker colors. Yield stress of peanut pastes increased as the color darkened, indicating spreadability correspondingly decreased with darker roast colors. The overall flavor of roasted peanuts was found to be optimized at 177°C/15min with the medium roast color.}, journal={FOOD CHEMISTRY}, author={Shi, Xiaolei and Dean, Lisa O. and Davis, Jack P. and Sandeep, K. P. and Sanders, Timothy H.}, year={2018}, month={Feb}, pages={974–979} }
 @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={AbstractThe kinetics of color development during peanut roasting were investigated at roasting temperatures from 149 to 204°C which produced Hunter L color values of 25–65. Preliminary and equivalent roasting trials were conducted using a batch roaster simulating the parameters of an industrial continuous belt roaster. Hunter L and b values of the roasted peanuts were fitted well to first‐order models (mean R2 > 0.93). The activation energy calculated from the first‐order model of the L and b values ranged from 1.0 to 1.1 × 108 J/kg mol. High‐temperature roasting decreased the uniformity of color development from seed to seed and throughout of the kernel. A zc value of 37.6°C was calculated using the first‐order model of the L values. The cook values were 11.5–23.6, 24.5–31.6, and 41.5–57.5 min for light, medium, and dark roasting, respectively.}, 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{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_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} }