Peptides inhibiting angiotensin-I-converting enzyme: Isolation from flavourzyme hydrolysate of Protaetia brevitarsis larva protein and identification

Abstract

Many angiotensin-I-converting enzyme (ACE) inhibitory peptides are used to prevent and manage hypertension. In this study, ACE inhibitory peptides were isolated from an insect protein that is attracting attention for it potential antihypertensive activity. Protaetia brevitarsis larva protein was enzymatically hydrolyzed by Flavourzyme®, and the hydrolysate was shown to inhibit ACE. Subsequent fractionation, using ultrafiltration and gel permeation chromatography followed by liquid chromatography-tandem mass spectrometry analysis, identified four previously unknown peptides with significant ACE inhibition characteristics (Ser-Tyr, Pro-Phe, Tyr-Pro-Tyr, and Trp-Ile). The highest inhibition activity observed for Trp-Ile. These peptides stimulated production of NO in human umbilical vein endothelial cells and, based on molecular docking analysis, exerted their inhibitory effects via hydrogen bonding with the ACE receptor active site. Thus, the identified peptides can be considered as promising candidates for ACE inhibition and have potential to be used as functional food ingredients.

Keywords: Angiotensin-I-converting enzyme; Antihypertensive peptide; Edible insect (Protaetia brevitarsis); Inhibition; Molecular docking; Nitric oxide.