Green Processing, Germinating and Wet Milling Brown Rice (Oryza sativa) for Beverages: Physicochemical Effects.

Plant-based beverage consumption is increasing markedly. Value-added dehulled rice (Oryza sativa) germination was investigated to improve beverage qualities. Germinating brown rice has been shown to increase health-promoting compounds. Utilizing green processing, wholesome constituents, including bran, vitamins, minerals, oils, fiber and proteins should should convey forward into germinated brown rice beverages. Rapid visco-analyzer (RVA) data and trends established that brown rice, preheated brown rice and germinated brown rice had higher pasting temperatures than white rice. As pasting temperature in similar samples may be related to gelatinization, RVA helped guide the free-flowing processing protocol using temperatures slightly above those previously reported for Rondo gelatinization. Particle size analysis and viscometric evaluations indicate that the developed sprouted brown rice beverage is on track to have properties close to commercial samples, even though the sprouted brown rice beverage developed has no additives, fortifications, added oils or salts. Phenolics and γ-aminobutyric acid increased slightly in germinated brown rice, however, increases were not maintained throughout most stages of processing. Significantly lower inorganic arsenic levels (113 ng/g) were found in germinated (sprouted) brown rice, compared to Rondo white and brown rice, which is far below the USA threshold level of 200 ng/g.

Green processing protocol for germinating and wet milling brown rice for beverage formulations: Sprouting, milling and gelatinization effects.

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. Paddy (rough) Rondo rice was dehulled using a pilot plant dehusker, sorted and cleaned into brown rice (BRR), rinsed, and germinated under various conditions (times and temperatures). Germinated brown rice (GBR) was then assessed (96.7 ± 0.8% germination and coleoptile length 2.24 ± 0.83 mm) prior to developing a method to soften, wet mill, sieve and gelatinize the matrix. Moderate macronutrient catabolism based on proximate analysis (e.g., 27.0%, 30.9% and 28.9% protein, oil and carbohydrate loss, respectively) and significantly decreased phytic acid (71.6%) from BRR â†’ GBR along with processing efficiency were used to establish a germination and processing protocol engaging the natural enzymatic hydrolysis of starch and other biochemical changes. Based on rapid visco analyzer pasting properties in heated BRR, GBR sieving results and observations of stored crude beverages, proteins and oils apparently remained soluble and were conveyed forward into an the enzyme-treated solubilized oligosaccharide matrix, which could be a natural emulsion. A method for germinating and processing brown rice, leading to a completely green process and "free-flowing" soluble matrix to deliver preliminary sprouted brown rice beverages is presented.

Simple methods to reduce major allergens Ara h 1 and Ana o 1/2 in peanut and cashew extracts.

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) p-aminobenzamidine; (2) magnetic agarose beads; and (3) extraction of a commercial peanut flour at pH 7, respectively. The first two methods were also used to reduce major allergens in cashew extracts. After treatments, samples were evaluated by SDS-PAGE. pABA-treated samples were also analyzed for IgE binding in western blot. We found that the methods resulted in peanut extracts lacking detectable Ara h 1 but containing Ara h 2/6 and cashew extract lacking Ana o 1/2, but containing Ana o 3. Consequently, reduced IgE binding was observed. We conclude that the methods are useful for producing peanut or cashew extract with little Ara h 1 or Ana o 1/2.

In vitro evaluation of digestive and endolysosomal enzymes to cleave CML-modified Ara h 1 peptides.

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. In the current study, we tested the ability of digestive and endolysosomal proteases to cleave CML-modified and unmodified Ara h 1 peptides. Mass spectrometric analyses of the digested peptides demonstrate that carboxymethylation of lysine residues renders these peptides refractory to trypsin digestion. We did not detect observable differences in the simulated gastric fluid or endolysosomal digestion between the parental and CML-modified peptides. One of the tested peptides contains a lysine residue previously shown to be CML modified laying in a previously mapped linear IgE epitope, but we did not observe a difference in IgE binding between the modified and parental peptides. Our findings suggest a molecular mechanism for the increased resistance of peanut allergens modified by thermal processing, such as Ara h 1, to digestion in intestinal fluid after heating and could help explain how food processing-induced modifications may lead to more potent food allergens by acting to protect intact IgE epitopes from digestion by proteases targeting lysine residues.

Treatment with oleic acid reduces IgE binding to peanut and cashew allergens.

Oleic acid (OA) is known to bind and change the bioactivities of proteins, such as α-lactalbumin and ß-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). After treatment, the samples were dialyzed and analyzed by SDS-PAGE and for OA content. IgE binding was evaluated by ELISA and western blot, using a pooled serum or plasma from individuals with peanut or cashew allergies. Results showed that OA at a concentration of 5mM reduced IgE binding to the allergens. Peanut sample T2 exhibited a lower IgE binding and a higher OA content (protein-bound) than T1. Cashew allergen T2 also showed a reduction in IgE binding. We conclude that OA reduces the allergenic properties of peanut extract and cashew allergen by binding to the allergens. Our findings indicate that OA in the form of sodium oleate may be potentially useful as a coating to reduce the allergenic properties of peanut and cashew allergens.

IgE binding to peanut allergens is inhibited by combined D-aspartic and D-glutamic acids.

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. Results showed that D-[Asp/Glu] (4 mg/ml) inhibited IgE binding (75%) while D-Glu, D-Asp and other D-aas had no inhibitory effect. A higher inhibition was seen with D-[Asp/Glu] than with L-[Asp/Glu]. We concluded that IgE was specific for D-[Asp/Glu], not D-Asp or D-Glu, and that D-[Asp/Glu] was more reactive than was L-[Asp/Glu] in IgE inhibition. The finding indicates that D-[Asp/Glu] may have the potential for removing IgE or reducing IgE binding to peanut allergens in vitro.

Reducing food allergy: is there promise for food applications?

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. For this reason, accidental ingestion of trace amount of allergenic proteins is common. For children with severe food allergy, this could be life-threatening. Food products with reduced allergenic proteins, if developed, could be beneficial and may raise the threshold of the amount of allergenic proteins required to trigger an allergic reaction. As a result, the number of serious allergic reactions may decrease. Moreover, such less allergenic products may be useful or replace regular products in studies such as oral tolerance induction or early exposure experiments, where children with severe peanut allergy are usually excluded due to their severe intolerance. This review focuses on recent findings and progress made in approaches to reduce allergenic proteins in foods. Modifying methods may include physical and chemical treatments as well as lifestyle changes and the use of supplements. We discuss the benefits and drawbacks these methods present for production of hypoallergenic food products and food allergy prevention.

Removing peanut allergens by tannic acid.

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. TA (0.25, 0.5, 1, and 2 mg/ml) was added to a peanut butter extract (5 mg/ml; pH 7.2), stirred, and centrifuged. The precipitates were then suspended in buffer at pH 2, centrifuged, re-suspended at pH 8, and centrifuged. Supernatants from each step were analysed by SDS-PAGE, ELISA, and Western blots. The effect of NaCl (1M) on complexes was also determined. Results showed that complexes formed at a TA concentration >0.5 mg/ml did not release major peanut allergens at pH 2 and 8, regardless of 1M NaCl being present or not. IgE binding of the extracts was reduced substantially, especially at a TA concentration of 1-2 mg/ml. Animal or clinical studies are still needed before TA can find an application in the development of low-allergen peanut products/beverages or the removal of peanut allergens due to accidental ingestion.