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作 者:吴秉宇 左琦[1] 钱炳俊[1] 姚晓敏[1] 张建华[1]
机构地区:[1]上海交通大学农业与生物学院,上海200240
出 处:《上海交通大学学报(农业科学版)》2015年第5期54-59,共6页Journal of Shanghai Jiaotong University(Agricultural Science)
基 金:海洋公益性行业科研专项经费项目(201205031-05)
摘 要:为了获得血管紧张素转化酶(ACE)抑制肽,使用α-胰凝乳蛋白酶对虾副产物进行预酶解,再选择羧肽酶A/B进行酶解,通过透析和凝胶层析纯化后,测定分离肽的ACE抑制活性。通过检测水解度,确定α-胰凝乳蛋白酶的最优水解时间为4h,羧肽酶A/B最优水解时间为6h。两步酶解产物的ACE半抑制浓度(IC50)值为6.39mg/mL。通过透析,得到〈500Da和500~1 000Da 2个抑制活性更高的组分,IC50分别为1.69和2.87mg/mL。进一步通过Sephadex G-15凝胶层析分离,得到4个IC50值小于0.2mg/mL的组分,其中组分F8最低,为0.134mg/mL,显示了较高的ACE抑制活性。该结果验证了羧肽酶A/B酶解可制备出高活性ACE抑制肽。To prepare angiotensin I-converting enzyme(ACE)inhibitory peptides,shrimp byproducts were successively hydrolyzed by α-chymotrypsin and carboxypeptidase A/B.The hydrolysates were then separated and purified by dialysis and gel-filtration chromatography.Based on the hydrolysis degree,the optimal hydrolysis time was 4hforα-chymotrypsin and 6hfor carboxypeptidase A/B.The IC50 value of the final hydrolysate was 6.39mg/mL.Fractions of molecular weight〈500Da(IC50=1.69mg/mL)and 500-1000Da(IC50=2.87mg/mL)were obtained by dialysis.These two fractions were further separated into 8fractions by sephadex G-15gel-filtration chromatography,four of them had IC50 values lower than 0.2mg/mL,and that of the lowest one(F8)was 0.134 mg/mL.The result proved that the enzymolysis of carboxypeptidase A/B could produce peptides with high ACE inhibitory activity.
分 类 号:TS254.1[轻工技术与工程—水产品加工及贮藏工程]
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