仿刺参ACE抑制肽的纯化及其分子量的测定  

Purification and Molecular Weight Assay of ACE Inhibition Peptides in Apostichopus japonicus

作　　者：张悦容[1] 徐茂琴[2] 刘文[1] 智姝婕 苏秀榕[1] 

机构地区：[1]宁波大学海洋学院,浙江宁波315211 [2]宁波城市职业技术学院,浙江宁波315100

出　　处：《核农学报》2014年第7期1240-1245,共6页Journal of Nuclear Agricultural Sciences

基　　金：国家农业科技成果转化资金资助项目(2007GB2C220359);浙江省重大科技专项(2008C02009)

摘　　要：利用仿刺参体壁制备具有抑制血管紧张素转移酶(ACE)活性的多肽,为进一步研究ACE抑制肽提供理论基础。本研究采用动物蛋白水解酶酶解仿刺参体壁,得到具有ACE抑制活性的酶解液;将酶解液粗品通过截留分子量5KDa的超滤系统,将活性部分继续用Sephadex G15分离纯化,采用HPLC法测定各组分的ACE抑制活性,同时利用RP-HPLC测定其相对分子质量分布。结果可知:仿刺参活性较高的ACE抑制肽主要由二肽到五肽组成,且分子量越小,抑制活性越高,得到了具有较高ACE抑制活性且组成比较单一的组分d,其IC50为439μg·mL-1。The body wall of Apostichopus japonicus was enzymatic degraded to prepare peptide which could inhibit Angiotensin-converting enzyme I（ ACE）,this work is to provide a theoretical basis for further investigating ACE inhibition peptide. Enzymatic hydrolysate with ACE inhibitory activity were obtained from Apostichopus japonicus by animal protein hydrolases. First,the crude hydrolysate was dialysed with ultra filtration system cut-off 5KDa,the fractions which were found to be active segment with ACE inhibitory activity were separated and purified by Sephadex G15. The ACE inhibitory activity and molecular weight of each component were measured by HPLC and RP-HPLC,respectively. ACE inhibition peptides of Apostichopus japonicas with high activity were mainly composed of dipeptide to pentapeptide and the lower molecular weight,the greater the inhibitory activity. The d was affirmed to be high ACE inhibitory and relatively simple peptide,whose IC50value was 439μg·mL- 1.

关 键 词：仿刺参 ACE抑制肽 降血压 分子量 

分 类 号：S968.9[农业科学—水产养殖]