Publications by authors named "Shawndrika Reed"

Plant-based beverage consumption is increasing markedly. Value-added dehulled rice () germination was investigated to improve beverage qualities. Germinating brown rice has been shown to increase health-promoting compounds.

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Rice-derived beverages offer a non-soy, lactose-free, cholesterol and gluten-free food source, which may offer well-balanced nutrition. Brown rice is nutritionally superior to white rice but oil oxidation and rancidity can be problematic regarding organoleptics during processing and storage. Using green technologies, which do not rely upon stabilization, brown rice was sprouted and processed with enzymes to produce preliminary value-added rice beverages.

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Whole peanut or cashew extracts are usually used in immunotherapy. Reducing major allergen(s) in the extracts may lessen their side effects. Three methods were evaluated to reduce major allergens in peanut extracts: (1) -aminobenzamidine; (2) magnetic agarose beads; and (3) extraction of a commercial peanut flour at pH 7, respectively.

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Ara h 1 is a major peanut allergen. Processing-induced modifications may modulate the allergenic potency of Ara h 1. Carboxymethyl lysine (CML) modifications are a commonly described nonenzymatic modification on food proteins.

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Oleic acid (OA) is known to bind and change the bioactivities of proteins, such as α-lactalbumin and β-lactoglobulin in vitro. The objective of this study was to determine if OA binds to allergens from a peanut extract or cashew allergen and changes their allergenic properties. Peanut extract or cashew allergen (Ana o 2) was treated with or without 5mM sodium oleate at 70°C for 60 min (T1) or under the same conditions with an additional overnight incubation at 37°C (T2).

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The objective of this study was to determine if D-amino acids (D-aas) bind and inhibit immunoglobulin E (IgE) binding to peanut allergens. D-aas such as D-Asp (aspartic acid), D-Glu (glutamic acid), combined D-[Asp/Glu] and others were each prepared in a cocktail of 9 other D-aas, along with L-amino acids (L-aas) and controls. Each sample was mixed with a pooled plasma from peanut-allergic donors, and tested by ELISA (enzyme-linked immunosorbent assay) and Western blots for IgE binding to peanut allergens.

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Food allergy is on the rise and has become a growing food safety concern. The main treatment is strictly avoiding allergens in the diet. However, this is difficult to do because foods are sometimes contaminated with allergens due to processing of different foods with the same machinery.

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Tannic acid (TA) forms insoluble complexes with proteins. The aims here were to remove major peanut allergens as insoluble TA complexes and determine if they would dissociate and release the allergens at pH 2 and 8 (gut pH). Release of the allergens in the gut could lead to absorption and consequently an allergic reaction.

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