The hydrolyzing technologies of oysterCrassostrea gigas antioxidation peptides

The hydrolysis process and antioxidation measured in scavenging activities of hydroxyl radicals in the hydrolysates were optimized for peptides of Pacific oyster Crassostrea gigas by papain and neutral protease in orthogonal experiments.The maximal activity of scavenging hydroxyl radicals was found in the papain hydrolysate under the follow conditions of hydrolytic period of 150 min,6% of the enzyme supplementation,at 45 ℃ and pH 7.0.The maximal activity of scavenging hydroxyl radicals was observed in the neutral protease hydrolysate under the follow conditions of hydrolytic period of 110 min,3% of the enzyme supplementation,at 65 ℃ and pH 6.0.The sephadex G-15 analysis revealed that there were considerable variations in the scavenging hydroxyl radical activity of different peptide fractions.The peptide hydrolyzed by the papain had molecular weight of about 1191 Dalton and 826 Dalton,with the maximal hydroxyl radical scavenging activity,while the peptide hydrolyzed by the neutral protease had molecular weight of about 1074 Dalton and 735 Dalton,with the maximal hydroxyl radical scavenging activity.