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.

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.