食品工业科技2012，Vol.33Issue(5)：90-94,5.
源于鸡蛋清溶菌酶ACE抑制肽的分离纯化及结构鉴定
Isolation and identification of ACE inhibitory peptides from the gastrointestinal digests of egg white lysozyme
摘要
Abstract
The objective was to screen potent ACE inhibitory peptides,which were resistant to gastrointestinal digestion,from enzymatic hydrolysate of egg white lysozyme by gastrointestinal enzymes.Two angiotensin I-converting enzyme（ACE） inhibitory peptide KVF and WIR,were purified from the gastrointestinal digests of egg white lysozyme by centrifugal ultrafiltration,preparative reverse-phase high-performance liquid chromatography（RP-HPLC） and analytical RP-HPLC,and identified by matrix assisted laser desorption ionization time of flight tandem mass spectrometry（MALDI-TOF-TOF-MS） based on analysis of amino acids composition.After KVF and WIR was chemically synthesized,ACE inhibitory activities（IC50） of these two tripeptides were determined as 14μmol/L and 88.5μmol/L,respectively.The results suggested that the ACE inhibitory peptides from egg white lysozyme may have potential for use in the prevention and treatment of hypertension.关键词
溶菌酶/ACE抑制肽/分离纯化/质谱Key words
lysozyme/ACE inhibitory peptide/isolation/mass spectrometry分类
轻工纺织引用本文复制引用
饶胜其,刘锋锋,居涛,徐雯琪,杨严俊..源于鸡蛋清溶菌酶ACE抑制肽的分离纯化及结构鉴定[J].食品工业科技,2012,33(5):90-94,5.基金项目
国家863计划项目 （）
