膜法制备血红蛋白血管紧张素Ⅰ转化酶抑制肽  

Preparation of ACE Ⅰ inhibitory peptides by ultrafiltration methodology

作　　者：王鹏[1] 邓晓龙[1] 卢航[1] 武龙[1] 胡建恩[1] 

机构地区：[1]大连海洋大学食品科学与工程学院,大连116023

出　　处：《食品科技》2015年第5期256-260,共5页Food Science and Technology

摘　　要：研究了猪血粉酶解及超滤法制备血管紧张素Ⅰ转化酶(ACE)抑制肽的工艺条件。首先将胃蛋白酶的猪血粉水解产物,依次通过30、10 ku和6 ku 3个截留分子质量(MWCO)的超滤膜,获得4组不同分子质量段(P-Ⅰ、P-Ⅱ、P-Ⅲ和P-Ⅳ)的血红蛋白多肽组分,质量浓度为1 mg/m L时,4个组分对ACE的抑制率分别为16.5%、21.7%、24.3%和55.6%。其次对抑制活性较低的3组分,分别用胰蛋白酶、中性蛋白酶、碱性蛋白酶和木瓜蛋白酶进行二次酶解,底物浓度均为2.0%,酶与底物质量比1.0%,根据ACE抑制率,分别确定各组分的二次酶解条件,结果显示P-Ⅰ、P-Ⅱ使用碱性蛋白酶酶解1 h时活性最强,P-Ⅲ使用中性蛋白酶酶解5 h时活性最强,得出结论血红蛋白二次酶解使水解产物的活性增强,且蛋白酶水解与膜分离的工艺适合于工业化生产。Preparation methodology of angiotensin Ⅰ-converting enzyme（ACE） inhibitory peptide from porcine powder was studied though hydrolysis and ultrafi ltration. Porcine powder was fi rstly hydrolyzed by pepsin, then the hydrolysate was fi ltrated by ultra-fi ltration membranes（MWCO 30 ku, 10 ku and 6 ku）. Four sections（P-Ⅰ, P-Ⅱ, P-Ⅲ and P-Ⅳ） were obtained and ACE inhibitory activity of each section was investigated. When mass concentration was 1 mg/m L, the ACE inhibition rates were 16.5%, 21.7%, 24.3% and 55.6%. Then the other parts except the best active part were secondary hydrolyzed by trypsin, neutrase, alcalase and papain. By analyzing ACE inhibitory rate at different time points, it showed the best protease and ensure the hydrolyze time, the results of optimum conditions were： the section P-Ⅰ, P-Ⅱwas hydrolyzed by alcalase for 1 h, the section P-Ⅲ was hydrolyzed by neutrase for 5 h. The conclusion showed that secondary hydrolysis could increased activity and membrane separation process was suitable for industrial production.

关 键 词：猪血粉 酶解 血管紧张素Ⅰ转化酶 活性肽 抑制 

分 类 号：TS201.4[轻工技术与工程—食品科学]