Abstract:

Wheat bran peptides were prepared by alkaline protease (Alcalase) hydrolysis and then purified with Sephadex G- 25 and DEAE-32 column chromatography. The cellulose acetate electrophoresis was used to determine the purity of wheat bran peptide with antioxidant activity. The surperoxide anion radical and hydroxyl radical scavenging activities of wheat bran peptide were detected through nitroblue tetrazolium (NBT) test and deoxyribose method. The erythrocatalysis extent and swelling extent of liver mitochondria were detected using spectrophotometric method. The results showed that the surperoxide anion radical and hydroxyl radical scavenging activities of purified wheat bran peptide are 53.16% and 62.39%, respectively, and the purified wheat bran antioxidant peptide can inhibit swelling of liver mitochondria and hemolysis of red blood cells, indicating that it has significant antioxidation.

Key words: wheat bran peptide, purification, antioxidation