红松仁清蛋白ACE抑制肽的分离纯化与结构鉴定  

Isolation, Purification and Structural Analysis of ACE Inhibitory Peptides Derived from Red Pine(Pinus koraiensis Sieb. et Zucc.) Nuts Albumin

作　　者：苗欣宇[1] 王祖浩[1] 王鹏[1] 方丽[1] 王辑[1] 闵伟红[1] MIAO Xinyu;WANG Zuhao;WANG Peng;FANG Li;WANG Ji;MIN Weihong(National Engineering Laboratory on Wheat and Corn Further Processing, College of Food Science and Engineering,Jilin Agricultural University, Changchun 130118, China)

机构地区：[1]吉林农业大学食品科学与工程学院,小麦和玉米深加工国家工程实验室,吉林长春130118

出　　处：《食品科学》2017年第5期129-133,共5页Food Science

基　　金：国家高技术研究发展计划(863计划)项目(2013AA102206)

摘　　要：为研究酶解红松仁清蛋白中具有血管紧张素转换酶(angiotensin converting enzyme,ACE)抑制活性短肽的组分及其序列,采用超滤、Sephadex G-25、Sephadex G-15及反相高效液相色谱对松仁清蛋白酶解液进行分离纯化,对纯化后样品(组分D2)进行质谱结构鉴定。质谱结果进行从头测序,筛选得到ACE抑制肽Tyr-Leu-Leu-Lys(YLLK),分子质量为535.34 D。该肽经固相合成纯度为99.80%,其半数抑制浓度测定值为0.282 5 μmol/L。In this study,the composition and structural characteristics of angiotensin converting enzyme(ACE)inhibitory peptides derived from albumin extracted from red pine nuts were evaluated.The hydrolysate of albumin was separated by ultrafiltration,Sephadex G-25,Sephadex G-15and reversed-phase high-performance liquid chromatography(RPHPLC).The structural characteristics of the purified fraction(D2)were identified by electrospray ionization tandem mass spectrometry(ESI-MS/MS),and one ACE inhibitory peptide was obtained with amino acid sequence of Tyr-Leu-Leu-Lys(YLLK)and molecular mass of535.34D.According to the amino acid sequence,an ACE inhibitory peptide was synthesized with a purity of99.8%.The half maximal inhibitory concentration value of YLLK was0.2825μmol/L.

关 键 词：红松仁清蛋白 ACE抑制肽 分离纯化 氨基酸序列 

分 类 号：TS255.6[轻工技术与工程—农产品加工及贮藏工程]