Structure characterization and antihypertensive effect of an antioxidant peptide purified from alcalase hydrolysate of velvet antler

Seung Tae Im1, Seung-Hong Lee1,2,*
Author Information & Copyright
1Department of Medical Science, Soonchunhyang University, Asan 31538, Korea.
2Department of Pharmaceutical Engineering, Soonchunhyang University, Asan 31538, Korea.
*Corresponding Author: Seung-Hong Lee, Department of Pharmaceutical Engineering, Soonchunhyang University, Asan 31538, Korea. E-mail:

© Copyright 2022 Korean Society for Food Science of Animal Resources. This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License ( which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Received: Sep 21, 2022 ; Revised: Nov 08, 2022 ; Accepted: Nov 21, 2022

Published Online: Nov 24, 2022


Recently, interest in food-derived bioactive peptides as promising ingredients for the prevention and improvement of hypertension is increasing. The purpose of this study was to determine the structure and antihypertensive effect of an antioxidant peptide purified from velvet antler in a previous study and evaluate its potential as a various bioactive peptide. Molecular weight (MW) and amino acid sequences of the purified peptide were determined by Q-TOF ESI mass spectroscopy. The angiotensin I-converting enzyme (ACE) inhibition activity of the purified peptide was assessed by enzyme reaction methods and in silico molecular docking analysis to determine the interaction between the purified peptide and ACE. Also, antihypertensive effect of the purified peptide in spontaneously hypertensive rats (SHRs) was investigated. The purified antioxidant peptide was identified to be a pentapeptide Asp-Asn-Arg-Tyr-Tyr (DNRYY) with a MW of 730.31 Da. This pentapeptide showed potent inhibition activity against ACE (IC50 value, 3.72 μM). Molecular docking studies revealed a good and stable binding affinity between purified peptide and ACE and indicated that the purified peptide could interact with HOH2570, ARG522, ARG124, GLU143, HIS387, TRP357, and GLU403 residues of ACE. Furthermore, oral administration of the pentapeptide significantly reduced blood pressure in SHRs. The pentapeptide derived from enzymatic hydrolysate of velvet antler is an excellent ACE inhibitor. It might be effectively applied as an animal-based functional food ingredient.

Keywords: velvet antler; purified peptide; angiotensin I-converting enzyme; antihypertensive effect; animal-based functional food ingredients