贻贝盐溶蛋白特性分析及其ACE抑制肽的酶法制备  

Characterization of Salt-Soluble Protein from Mytilus edulis and Enzymatic Preparation of ACE Inhibitory Peptides

作　　者：乔美玲 刘汉雄 樊凤娇 涂茂林 于翠平 杜明 QIAO Meiling;LIU Hanxiong;FAN Fengjiao;TU Maolin;YU Cuiping;DU Ming(National Engineering Research Center of Seafood,School of Food Science and Technology,Dalian Polytechnic University, Dalian 116034,China;School of Chemistry and Chemical Engineering,Harbin Institute of Technology,Harbin 150001,China)

机构地区：[1]大连工业大学食品学院,国家海洋食品工程技术研究中心,辽宁大连116034 [2]哈尔滨工业大学化工与化学学院,黑龙江哈尔滨150001

出　　处：《食品科学》2018年第22期51-56,共6页Food Science

基　　金：“十三五”国家重点研发计划重点专项(2017YFD0400201)。

摘　　要：以贻贝为原料提取盐溶性蛋白,首先研究盐溶性蛋白的分子质量分布、粒度分布和变性温度等性质,然后比较其3种蛋白酶(胰蛋白酶、中性蛋白酶和胰酶)酶解产物的血管紧张素转化酶(angiotensin converting enzyme,ACE)抑制活性,筛选出ACE抑制活性较高的胰蛋白酶酶解物,其IC_(50)值为215.96 μg/mL。利用质谱对胰蛋白酶酶解物中的多肽氨基酸序列进行鉴定,利用多肽序列与ACE的对接分数初步筛选出11个分值大于180分的多肽序列,通过氨基酸组成结合情况和两者间氢键等相互作用,进一步筛选活性肽并阐述抑制活性机理,最终推测出LYDIDVAK和WIAEEADK是活性较高的抑制肽。The molecular mass distribution,particle size distribution and degeneration temperature of the salt-soluble protein from Mytilus edulis muscle were studied.The tryptic hydrolysate of M.edulis muscle was found to have higher angiotensin converting enzyme(ACE)inhibitory activity than the hydrolysates produced with neutral protease and pancreatin,with a half maximal inhibitory concentration(IC50)of 215.96μg/mL.The amino acid sequences of peptides from the tryptic hydrolysate were identified by mass spectrometry.Eleven peptides bound to ACE with scores greater than 180 were selected.The interaction and hydrogen bonds between amino acid binding sites were analyzed to screen active peptides and the mechanism of antihypertensive activity was elucidated.Finally,LYDIDVAK and WIAEEADK were predicted as peptides with high ACE inhibitory activity.

关 键 词：贻贝 盐溶性蛋白 超高效液相色谱-四极杆-飞行时间串联质谱 血管紧张素转化酶抑制肽 分子对接 

分 类 号：TS254[轻工技术与工程—水产品加工及贮藏工程]