富硒螺旋藻多肽对血管紧张素转化酶的抑制作用  

Angiotensin Convert Enzyme Inhibition of Peptides Derived from Water Soluble Total Protein of Selenium-enriched Spirulina platensis

作　　者：高冬芳[1] 张逸波[1] 凌钦婕[1] 邹颖[1] 黄峙[1] 

机构地区：[1]暨南大学生命科学技术学院,广东广州510632

出　　处：《食品科学》2011年第7期7-10,共4页Food Science

基　　金：国家自然科学基金项目(20975045;20675045);暨南大学大学生创新工程项目(cx10088)

摘　　要：从富硒螺旋藻(SeSP)中提取总蛋白(SeSP-TP),用不同蛋白酶水解SeSP-TP制备富硒螺旋藻多肽(SeSP-Ps),体外测定SeSP-Ps对血管紧张素转化酶(ACE)的抑制作用。结果表明:5种常见蛋白酶在最适条件下对SeSP-TP水解度明显不同,其中胃蛋白酶-胰蛋白酶-胰凝乳蛋白酶联合使用时的酶水解度最高;虽然不同蛋白酶水解制备的SeSP-Ps均对ACE具有较强的抑制作用,但不同酶水解的SeSP-Ps对ACE的50%抑制浓度(IC50)存在明显差异,其中胃蛋白酶-胰蛋白酶-胰凝乳蛋白酶联合酶解制备的SeSP-Ps对ACE的IC50值最低,为74.6μg/mL。结果提示:SeSP在体内经胃肠蛋白酶消化产生的多肽,对ACE具有较强的抑制活性,且SeSP-Ps对ACE的抑制作用呈现显著的剂量-效应依赖性。The water soluble total protein（TP） of selenium-enriched Spirulina platensis（SeSP）,named as SeSP-TP,was extracted by phosphate buffer and then hydrolyzed by 5 different proteases to produce SeSP peptides（SeSP-Ps）.The angiotensin convert enzyme（ACE） inhibition of SeSP-Ps was measured in vitro.The results showed that treatments with different proteases caused obvious difference of hydrolysis degree（HD） to SeSP-TP,and the combined use of pepsin,trypsin and chimotrypsin led to the highest H.Furthermore,we found that all SeSP-Ps produced by various proteases could inhibit ACE.The 50% ACE inhibition concentration（IC50） of SeSP-Ps derived from the combination of pepsin,trypsin and chimotrypsin was 74.6μg/mL,which was the lowest in comparison with SeSP-Ps obtained with each of the three enzymes or papain.The present results implied that the excellent functional food SeSP contains highly active dose-dependent ACE inhibition peptides.

关 键 词：血管紧张素转化酶(ACE) 螺旋藻 硒 多肽 

分 类 号：TS201.6[轻工技术与工程—食品科学]