摘要
Abstract
ACE inhibitory peptides were prepared from casein by sequential hydrolysis with pepsin and trypsin.Casein hydrolysate was preliminarily separated with 6 ku MWCO ultrafiltration membrane and further purified by Sephadex G-15 column chromatography.The ACE inhibitory activity（IC50） of the separated fractions was determined by an in vitro assay,and their peptide profiles and molecular weights were measured by capillary electrophoresis（CE） and Q-TOF LC/MS,respectively.The results showed that IC50 values of casein hydrolysate,filtrate,and three fractions obtained by Sephadex G-15 column chromatography,factions Ⅰ,Ⅱ and Ⅲ were 560,250,123.41,66.67μg/mL and 64.29μg/mL,respectively.FactionsⅠ,Ⅱ and Ⅲ were composed of 19,14 and 5 peptides,respectively and their molecular weights ranged from 400 to 800 u.关键词
酪蛋白/酪蛋白水解物/ACE抑制肽/胃蛋白酶/胰蛋白酶Key words
casein/casein hydrolysate/ACE inhibitory peptide/pepsin/trypsin分类
轻工纺织
