多棘海盘车多肽的制备及其抑制ACE活性研究

Polypeptide of Asterias amurensis of Preparation and Research of its Inhibitory Activity on ACE

采用酶解法制备多棘海盘车多肽,选取胃蛋白酶、木瓜蛋白酶和碱性蛋白酶分别酶解多棘海盘车的水溶性蛋白,获得多肽样品PE-P、PA-P和AP-P。选取胰蛋白酶水解多棘海盘车的水溶性蛋白后再用质量分数为30%,50%,80%的硫酸铵溶液分别沉淀出不同分子量范围的多肽样品P-1,P-2和P-3。然后采用HPLC法分别测定上述多肽的血管紧张素转换酶(ACE)抑制活性。结果表明,PE-P,PA-P和AP-P均具有一定的抑制ACE活性,其中AP-P的抑制活性最好,PA-P次之,PE-P最差,它们的IC50值分别为0.6827,0.5526,0.3328 mg/mL。通过对P-1,P-2和P-3分析结果可知,分子量越小的多肽对ACE的抑制活性越显著。

Polypeptide of Asterias amurensis was prepared by enzymolysis method.Pepsin,papain and alkaline protease were selected to enzymolysis the water-soluble protein,and PE-P,PA-P and AP-P were obtained.Polypeptide samples of P-1,P-2 and P-3 with different molecular weight range were precipitated with 30%,50%and 80%ammonium sulfate.Then the ACE inhibitory activities of the peptides were determined by HPLC.The results showed that PE-P,PA-P and AP-P were all had certain inhibitory activity,among which AP-P had the best inhibitory activity,PA-P was the second,PE-P was the worst,and their IC50 values were 0.6827,0.5526,0.3328 mg/mL,respectively.The results of p-1,P-2 and P-3 showed that the peptides with smaller molecular weight had more significant inhibitory activity on ACE.