Abstract:Using Sinonovacula constricta as raw materials, optimum enzyme was selected from trypsin, pepsin, papain, alcalase and neutrase based on the hydroxyl free radical scavenging activity. Based on the single factor experiment, optimization of the hydrolysis conditions was conducted by the response surface methodology. The scavenging activity of hydroxyl free radical was investigated and the molecular weight of the enzymatic hydrolysates of S. constricta proteins was determined by a Sephadex G-15 gel column. The results showed that alcalase had the best hydrolytic effect and the optimum conditions for hydrolysis by alcalase were as follows:6 mg/ml substrate,3% enzyme, pH 8.0,55℃, 4 h. The scavenging activity of hydroxyl free radical of enzymatic hydrolysates was 76.60% and the IC50 was 1.89 mg/ml. The molecular weight of over 80% bioactive peptides from S. constricta was less than 1 500 Da.
