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Open AccessArticle

Identification of an ACE-Inhibitory Peptide from Walnut Protein and Its Evaluation of the Inhibitory Mechanism

College of Food Science, Northeast Agricultural University, Harbin 150030, China
Department of Food Science and Engineering, Harbin Institute of Technology, Harbin 150090, China
School of Food Science and Technology, National Engineering Research Center of Seafood, Dalian Polytechnic University, Dalian 116034, China
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2018, 19(4), 1156;
Received: 11 February 2018 / Revised: 18 March 2018 / Accepted: 24 March 2018 / Published: 11 April 2018
In the present study, a novel angiotensin I-converting enzyme inhibitory (ACE inhibitory) peptide, EPNGLLLPQY, derived from walnut seed storage protein, fragment residues 80–89, was identified by ultra-high performance liquid chromatography electrospray ionization quadrupole time of flight mass spectrometry (UPLC-ESI-Q-TOF-MS/MS) from walnut protein hydrolysate. The IC50 value of the peptide was 233.178 μM, which was determined by the high performance liquid chromatography method by measuring the amount of hippuric acid (HA) generated from the ACE decomposition substrate (hippuryl-l-histidyl-l-leucine (HHL) to assess the ACE activity. Enzyme inhibitory kinetics of the peptide against ACE were also conducted, by which the inhibitory mechanism of ACE-inhibitory peptide was confirmed. Moreover, molecular docking was simulated by Discovery Studio 2017 R2 software to provide the potential mechanisms underlying the ACE-inhibitory activity of EPNGLLLPQY. View Full-Text
Keywords: walnut; protein; peptides; ACE inhibitory; molecular docking walnut; protein; peptides; ACE inhibitory; molecular docking
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MDPI and ACS Style

Wang, C.; Tu, M.; Wu, D.; Chen, H.; Chen, C.; Wang, Z.; Jiang, L. Identification of an ACE-Inhibitory Peptide from Walnut Protein and Its Evaluation of the Inhibitory Mechanism. Int. J. Mol. Sci. 2018, 19, 1156.

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