PURIFICATION AND CHARACTERIZATION OF ANTIOXIDANT PEPTIDES FROM SOY PROTEIN HYDROLYSATE

Abstract

Soy protein hydrolysates (SPH) were obtained by Alcalase hydrolysis of soy protein. Antioxidant activity of SPH was measured with a lipid peroxidation inhibitory activity and lipid oxidation was evaluated by measuring the thiobarbituric acid (TBA) and peroxide value. The potent antioxidant peptide was purified using ultrafiltration and consecutive chromatographic methods including FPLC and reverse-phase high-performance liquid chromatography. The antioxidant activity having a specific activity of 108.13%/mg for TBA method was enhanced 67.6-fold compared with SPH. In the amino acid composition of the final potent antioxidant peptide, hydrophobic amino acids were the most abundant amino acids and among them phenylalanine was especially abundant.