高等学校化学学报 ›› 2009, Vol. 30 ›› Issue (10): 1992.

• 研究论文 • 上一篇    下一篇

高活性燕麦蛋白源ACE抑制肽的制备、纯化及结构鉴定

管骁1, 刘静2, 王立3, 姚惠源3   

  1. 1. 上海理工大学医疗器械与食品学院, 上海 200093;
    2. 上海海事大学信息工程学院, 上海 200135;
    3. 江南大学食品学院, 无锡 214122
  • 收稿日期:2009-01-15 出版日期:2009-10-10 发布日期:2009-10-10
  • 通讯作者: 管骁, 男, 博士, 讲师, 从事功能性食品的应用基础研究. E-mail: gnxo790521@yahoo.com.cn
  • 基金资助:

    上海市晨光计划项目(批准号: 09CG50), 中国博士后科学基金(批准号: 20090450712)和上海市博士后科研资助计划(批准号: 09R21413300)资助.

Preparation, Purification and Structure Identification of Angiotensin Ⅰ Converting Enzyme Inhibitory Peptide with High Activity from Oat Protein

GUAN Xiao1*, LIU Jing2, WANG Li3, YAO Hui-Yuan3   

  1. 1. School of Medical Instruments and Food Engineering, University of Shanghai for Science and Technology, Shanghai 200093, China;
    2. College of Information Engineering, Shanghai Maritime University, Shanghai 200135, China;
    3. School of Food Science and Technology, Jiangnan University, Wuxi 214122, China
  • Received:2009-01-15 Online:2009-10-10 Published:2009-10-10
  • Contact: GUAN Xiao. E-mail: gnxo790521@yahoo.com.cn
  • Supported by:

    上海市晨光计划项目(批准号: 09CG50), 中国博士后科学基金(批准号: 20090450712)和上海市博士后科研资助计划(批准号: 09R21413300)资助.

摘要:

利用胰蛋白酶水解燕麦蛋白制备了高血管紧张素转化酶(Angiotensin I-Converting Enzyme, ACE)抑制活性的燕麦蛋白酶解物, 分别采用离子交换色谱、凝胶过滤色谱和反相高效液相色谱等分离手段从酶解物中分离出一种新的强活性ACE抑制肽, 其IC50值为77.3 μmol/L; 通过基质辅助激光解析电离飞行时间串联质谱对其进行结构鉴定, 其氨基酸序列为Glu-Gly-Gly-Tyr-Arg.

关键词: 燕麦蛋白; ACE抑制肽; 制备及纯化

Abstract:

Oat protein hydrolysate showing strong angiotensin I converting enzyme(ACE) inhibitory activity was prepared by enzymatic hydrolysis with trypsin. Furthermore, a novel peptide with the IC50 value of 77.3 μmol/L was isolated from the hydrolysate using consecutive chromatographic methods including ion-exchange chromatography, gel filtration chromatography, and reversed-phase high-performance liquid chromatography. The peptide was identified by matrix assisted-laser desorption/ionization time-of-flight tandem mass spectrometry as Glu-Gly-Gly-Tyr-Arg.

Key words: Oat protein; ACE inhibitory peptide; Preparation and purification

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