Rice endosperm protein was modified to enhance solubility and emulsifying properties by controlled enzymatic hydrolysis. The optimum degree of hydrolysis (DH) was determined for acid, neutral, and alkaline type proteases. Solubility and emulsifying properties of the hydrolysates were compared and correlated with DH and surface hydrophobicity. DH was positively associated with solubility of resulting protein hydrolysate regardless of the hydrolyzing enzyme, but enzyme specificity and DH interactively determined the emulsifying properties of the protein hydrolysate. The optimum DH was 6–10% for good emulsifying properties of rice protein, depending on enzyme specificity. High hydrophobic and sulfhydryl disulfide (SH‐SS) interactions contributed to protein insolubility even at high DH. The exposure of buried hydrophobic regions of protein that accompanied high‐temperature enzyme inactivation promoted aggregation and cross‐linking of partially hydrolyzed proteins, thus decreasing the solubility and emulsifying properties of the resulting hydrolysate. Due to the highly insoluble nature of rice protein, surface hydrophobicity was not a reliable indicator for predicting protein solubility and emulsifying properties. Solubility and molecular flexibility are the essential factors in achieving good emulsifying properties of rice endosperm protein isolates.
Supercritical fluid extrusion (SCFX) was used to produce shelf-stable puffed rice fortified with protein, dietary fiber, and micronutrients. Product ingredients and process parameters were evaluated for end-product nutritional and textural qualities. Supercritical carbon dioxide (SC-CO(2)) served as a viscosity-lowering plasticizer and blowing agent during the process, which has been shown to produce expanded products with good textural qualities at lower temperatures (~100 °C) than conventional steam-based extrusion (130-180 °C). The fortified puffed rice contained 8% dietary fiber, 21.5% protein, and iron, zinc, and vitamins A and C at their recommended daily values in 100 g of product. The SCFX process allowed for the complete retention of all added minerals, 55-58% retention of vitamin A, and 64-76% retention of vitamin C. All essential amino acids including lysine were retained at exceptionally high levels (98.6%), and no losses were observed due to Maillard reaction or oxidation. All of the essential amino acid contents were equal to the reference protein recommended by FAO/WHO. Soy protein fortification improved the total amount of protein in the final rice products and provided a complementary amino acid profile to that of rice; the lysine content improved from 35 to 60 mg/protein, making the end product an excellent source of complete protein. Thus, SC-CO(2)-assisted extrusion is an effective process-based approach to produce cereal grain-based, low-moisture (5-8%) expanded products fortified with protein and any cocktail of micronutrients, without compromising the end-product sensory or nutritional qualities. These products are ideally suited for consumption as breakfast cereals, snack foods, and as part of nutrition bars for school lunch programs. The balanced nutritional profile and use of staple crop byproducts such as broken rice makes these expanded crisps unique to the marketplace.
Rice proteins are nutritional, hypoallergenic, and healthy for human consumption. Efficient extraction with approved food‐grade enzymes and chemicals are essential for commercial production and application of rice protein as a functional ingredient. Rice endosperm proteins were isolated by alkali, salt, and enzymatic methods and evaluated for extractability and physicochemical properties. Alkali (RPA) and salt (RPS) methods extracted 86.9 and 87.3% of proteins with 65.9 and 58.9% yield, respectively. The enzymatic methods with Termamyl (RPET) and amylase S (RPEA) extracted 85.8 and 81.0% proteins with 85.2 and 86.2% yield, respectively. Enthalpy values of RPA (1.79 J/g), RPS (1.22 J/g), RPET (nondetectable), and RPEA (0.17 J/g), determined by differential scanning calorimetry, demonstrated that the varying level of denaturation of proteins depends on the method of extraction. Surface hydrophobicity data supported this observation. Alkali‐ and salt‐extracted proteins had higher solubility and emulsifying properties than those of enzyme‐extracted proteins. Comparatively, more favorable protein composition, lower surface hydrophobicity, higher solubility, and a lower degree of thermal denaturation of alkali‐ and salt‐extracted proteins contributed to higher emulsifying and foaming properties than those of enzyme‐extracted proteins; therefore, alkali‐ and salt‐extracted proteins can have enhanced functional use and a potential starting material for preparing tailored rice protein isolates.
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