ABSTRACT
Proteins from the defatted brans of representative rice cultivars were fractionated into albumins, globulins, prolamins, and acid-soluble glutelins, accounting for 34, 15, 6, and 11% of the total bran proteins, respectively. The remaining insoluble residue protein, after treatment with 0.1M sodium hydroxide, resulted in the solubilization of 95% of the residue protein, representing 32% of the total bran protein. The relative molecular mass (Mr) values determined by size-exclusion HPLC were 10–100 kDa, 10–150 kDa, 33–150 kDa, and 25–100 kDa for the fully dissociated polypeptides of albumins, globulins, prolamins, and acid-soluble glutelins, respectively. Despite a breakdown of disulfide bonds of the residue protein during sodium hydroxide solubilization, the Mr of the majority of the fully dissociated polypeptides of this fraction ranged from 45 to 150 kDa. Insolubility of residue protein was due mainly to its strong aggregation and extensive disulfide bond cross-linking. Efficient methods may be developed for solubilizing up to 98% of rice bran protein by the use of dissociating and disulfide breaking agents currently in use in the food industry.
