Preparation and characterization of high‐quality rice bran proteins

Rice bran contains 120–200 g kg^?1 protein in addition to a large amount of fat, carbohydrate, and phytic acid. Rice bran protein (RBP) fractions were refined by a two‐step preparation to eliminate residual carbohydrate. The first step involved the sequential extraction of defatted rice bran into RBP fractions using their distinct solubility to give 37 g kg^?1 of albumin, 31 g kg^?1 of globulin, 27 g kg^?1 of glutelin, and 2 g kg^?1 of prolamin. In the second step, carried out by dissolving in respective solvent and isoelectric precipitation, the protein content of each fraction increased from 69% to 97% for albumin, from 71% to 90% for globulin, from 74% to 83% for glutelin, and from 18% to 20% for prolamin. The low protein content in the prolamin fraction might be due to its low solubility in the protein assay. Emulsifying stability index and surface hydrophobicity increased in the second‐step preparation of albumin and globulin, but not of glutelin. Emulsifying properties of RBPs were lower than that of a soybean protein isolate. Denaturation temperatures and enthalpy values of denaturation for albumin, globulin, glutelin, and prolamin were 50.1 °C/1.2 J g^?1, 79.0 °C/1.8 J g^?1, 74.5 °C/3.0 J g^?1, and 78.5 °C/8.1 J g^?1, respectively. No significant differences in the denaturation temperatures and enthalpy values of denaturation of RBP fractions were obtained with these two‐step preparations (P < 0.05). Copyright © 2007 Society of Chemical Industry