Properties of Whole and Unidigested Fraction of Protein Bodies of Milled Rice

Abstract

Protein bodies (PB) were prepared from IR480-5-9 (10.5% protein) milled rice by destar-ching the cooked rice flour with crystalline bacterial α-amylase. Corresponding PB from raw rice prepared by treatment with analytical grade glucoamylase were more susceptible to pepsin digestion than PB from cooked rice. The undigested residue from pepsin digestion of both cooked and raw rice PB and preparations of fecal protein particles from man and rat on an IR480-5-9 cooked milled rice diet represented the core of PB. The core protein was poorer in lysine and had lower mol. wt. subunits than whole PB protein. The pepsin-digested PB preparations had higher fat content than whole PB preparation.