食品科学

• 基础研究 • 上一篇    下一篇

红松仁清蛋白ACE抑制肽的分离纯化与结构鉴定

苗欣宇,王祖浩,王 鹏,方 丽,王 辑,闵伟红*   

  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
  • 出版日期:2017-03-15 发布日期:2017-03-28

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

MIAO Xinyu, WANG Zuhao, WANG Peng, FANG Li, WANG Ji, MIN Weihong*   

  1. National Engineering Laboratory on Wheat and Corn Further Processing, College of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China
  • Online:2017-03-15 Published:2017-03-28

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。

关键词: 红松仁清蛋白, ACE抑制肽, 分离纯化, 氨基酸序列

Abstract: 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-15 and 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 of 535.34 D. According to the amino acid sequence, an ACE inhibitory peptide was synthesized with a purity of 99.8%. The half maximal inhibitory concentration value of YLLK was 0.282 5 μmol/L.

Key words: red pine nut albumin, ACE inhibitory peptide, isolation and purification, amino acid sequence

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