酶法水解珠蛋白制备血管紧张素Ⅰ转换酶抑制肽  

THE PRODUCING OF ANGIOTENSIN-I-CONVERTING ENZYME INHIBITORY PEPTIDE BY HYDROLYZING GLOBIN WITH PROTEASE

作　　者：余奕珂[1] 胡建恩[1] 白雪芳[1] 杜昱光[1] 林炳承[1] 

机构地区：[1]中国科学院大连化学物理研究所

出　　处：《河南工业大学学报（自然科学版）》2006年第5期59-61,共3页Journal of Henan University of Technology：Natural Science Edition

基　　金：辽宁省自然科学基金项目(20052162)

摘　　要：分别用3种不同的蛋白酶对珠蛋白进行水解,测定不同水解时间所得产物对血管紧张素I转换酶(ACE)的抑制活性,并对抑制活性最高的水解液进行分离.结果表明:胃蛋白酶水解珠蛋白所得的水解液对ACE的抑制率最高,其半抑制浓度(IC50)为1.19 mg/mL,用SephadexLH20对其进行分离,所得的第5组分的IC50为0.10 mg/mL,活性比水解液提高了12倍.Three trade-proteases were chosen to hydrolyze globin, the angiotensin-I- converting enzyme （ACE） inhibitory activities of the hydrolysates were investigated. The results showed that the ACE inhibitory activity of peptic globin hydrolysate was the highest, with the IC5o value of 1.19 mg/mL. The peptic globin hydrolysate was separated on Sephadex LH-20 gel filtration column and five majorfractions （Ⅰ , Ⅱ ,Ⅲ ,Ⅳ, Ⅴ ） were obtained. Fraction V had an ICso value of 0.10 mg/mL, and was purified 12-fold from hydrolysate.

关 键 词：血管紧张素I转换酶 SEPHADEX LH-20 珠蛋白 水解 

分 类 号：TS201.2[轻工技术与工程—食品科学]