酪蛋白非磷肽中一种ACE活性抑制肽的分离和鉴定  

Isolation and Identification of Inhibitory Peptides for Angiotensin Converting Enzyme in Casein Non-phosphopeptides

作　　者：赵一明[1] 王璋[1] 许时婴[1] 张文斌[1] 

机构地区：[1]江南大学食品学院

出　　处：《食品与发酵工业》2008年第4期21-24,共4页Food and Fermentation Industries

基　　金：苏州市科技攻关项目(SNG0722)

摘　　要：酪蛋白经碱性蛋白酶Alcalase水解后,加入乙醇提取出的酪蛋白非磷肽(CNPPs)对血管紧张素转化酶(ACE)的活性有很强的抑制作用。采用凝胶过滤色谱Sephadex G-15和反相高效液相色谱(RP—HPLC)对CNPPs进行分离纯化,通过高效液相色谱/电喷雾电离质谱联用分析和氨基酸组成分析鉴定出一种抑制ACE活性肽,其氨基酸序列为Ser-Trp,ACE半抑制浓度为92.8μmol/L。Casein non-phosphopeptides （CNPPs） which showed significant inhibitory activity against the angiotensin converting enzyme （ACE） could be obtained from casein by enzymatic hydrolysis and extracting with ethanol. CNPPs was first isolated by size exclusion chromatography （SEC） Sephadex G-15, and was further purified by reversed-phase HPLC. The pure peptide with ACE inhibitory activity was obtained, the amino acid sequence of which was identified as Ser-Trp by LC/ESI-MS and amino acid composition analysis. And the inhibitory concentration 50% （IC50） was 92.8 μmol/L.

关 键 词：酪蛋白非磷肽 血管紧张素转化酶抑制肽 氨基酸序列 高效液相色谱 电喷雾电离质谱 

分 类 号：TQ464.7[化学工程—制药化工]