Chem. J. Chinese Universities ›› 2009, Vol. 30 ›› Issue (10): 1992.

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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.

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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