Three Novel ACE Inhibitory Peptides Isolated From Seeds: Purification, Inhibitory Kinetic and Mechanism.

Journal: Frontiers in pharmacology
Published Date: Jan 15, 2019

Abstract

Alcalase, dispase, trypsin, and flavourzyme were used to hydrolyze the extracted seeds protein isolate (GPI). The protein hydrolyzates (GPHs) with the maximum degree of hydrolysis (DH) and ACE inhibitory activity were selected, and ultra-filtered to obtain components with different molecular weights (MW) (<1 kDa, 1-3, 3-5, and 5-10 kDa). The components with MW of <1 kDa showed better ACE inhibition (IC:0.2227 mg/mL). Purification and identification by Sephadex G-15 gel chromatography and LC-MS/MS conferred three new potential ACE inhibitory peptides [TNLDWY (non-competitive suppression mode), IC: 1.932 mM; RADFY (competitive inhibition modes), IC:1.35 mM; RVFDGAV (competitive inhibition modes), IC:1.006 mM]. Molecular docking depicting the inhibitory mechanism for ACE inhibitory peptides indicated that the peptides bound well to ACE and interacted with amino acid residues at the ACE active site.

Authors

  • Fei-Fei Ma
    School of Food Science and Engineering, Hefei University of Technology, Hefei, China.
  • Hao Wang
    Department of Cardiology, Second Medical Center, Chinese PLA General Hospital, Beijing, China.
  • Chao-Kun Wei
    School of Food Science and Engineering, Hefei University of Technology, Hefei, China.
  • Kiran Thakur
    School of Food Science and Engineering, Hefei University of Technology, Hefei, China.
  • Zhao-Jun Wei
    School of Food Science and Engineering, Hefei University of Technology, Hefei, China.
  • Li Jiang
    School of Food Science and Engineering, Hefei University of Technology, Hefei, China.

Keywords

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