Effects of bioactive peptides encrypted in whey-, soy- and rice protein on local and systemic angiotensin-converting enzyme activity

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

Abstract

The renin-angiotensin system (RAS) is one of the main control systems of arterial blood pressure. Here, key player is the angiotensin converting enzyme (ACE). Inhibition of ACE is a standard therapy to lower elevated blood pressure. This study aimed to determine the ACE-inhibitory activity of tryptophan- and tyrosine-containing peptide mixes, based on hydrolysates of whey-, soy- and rice-protein. Effects on circulating and tissue ACE were investigated. IC50 values range from 16.60 ± 2.59 mg/l to 282.04 ± 18.51 mg/l, depending on the peptide mix and the ACE-system. Strongest ACE-inhibition is generally obtained with whey peptide mix characterized by a high fraction of isoleucine-tryptophan. Good inhibitory potential was obtained for plasma and tissue ACE. Thus, the use of whey peptide mix and isoleucine-tryptophan, respectively, appears to deserve further studies as innovative food additives with the potential to delay or even prevent RAS-related hypertension and subsequent deterioration of vessel structure and function.

Details

Original languageEnglish
Pages (from-to)299-305
Number of pages7
JournalJournal of Functional Foods
Volume28
Publication statusPublished - 1 Jan 2017
Peer-reviewedYes

External IDs

Scopus 85003875034
ORCID /0000-0002-3564-0193/work/158765837

Keywords

Keywords

  • Angiotensin-converting enzyme, Arterial hypertension, Bioactive peptides, Rice protein, Soy protein, Whey protein