STRUCTURAL-ANALYSIS OF ANTIOXIDATIVE PEPTIDES FROM SOYBEAN BETA-CONGLYCININ

Protease hydrolyses of a soybean protein, beta-conglycinin (7S protein ), yielded antioxidative activity against the peroxidation of linoleic acid in an aqueous system at pH 7.0. Six antioxidative peptides were isolated from the hydrolysate prepared with protease S by size exclusi on chromatography and reversed-phase HPLC. The amino acid sequences of the peptides were determined using a gas-phase protein sequencer and electron spray mass spectrometry. The peptides were composed of 5-16 a mino acid residues, including hydrophobic amino acids, valine or leuci ne, at the N-terminal positions, and proline, histidine, or tyrosine i n the sequences.