Bioavailability of angiotensin I converting enzyme inhibitory peptides

Vermeirssen, Vanessa, Van Camp, John and Verstraete, Willy (2004) Bioavailability of angiotensin I converting enzyme inhibitory peptides. The British Journal of Nutrition, 92 3: 357-366. doi:10.1079/BJN20041189

Author Vermeirssen, Vanessa
Van Camp, John
Verstraete, Willy
Title Bioavailability of angiotensin I converting enzyme inhibitory peptides
Journal name The British Journal of Nutrition   Check publisher's open access policy
ISSN 0007-1145
Publication date 2004-09
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1079/BJN20041189
Volume 92
Issue 3
Start page 357
End page 366
Total pages 10
Place of publication Cambridge
Publisher Cambridge University Press
Language eng
Subject 030406 Proteins and Peptides
Abstract Hypertension or high blood pressure is a significant health problem worldwide. Bioactive peptides that inhibit angiotensin I converting enzyme (ACE) in the cardiovascular system can contribute to the prevention and treatment of hypertension. These ACE inhibitory peptides are derived from many food proteins, especially milk proteins. An ACE inhibitory activity in vitro does not always imply an antihypertensive effect in vivo. Even if it does, it is very difficult to establish a direct relationship between in vitro and in vivo activity. This is mainly due to the bioavailability of the ACE inhibitory peptides after oral administration and the fact that peptides may influence blood pressure by mechanisms other than ACE inhibition. To exert an antihypertensive effect after oral ingestion, ACE inhibitory peptides have to reach the cardiovascular system in an active form. Therefore, they need to remain active during digestion by human proteases and be transported through the intestinal wall into the blood. The bioavailability of some ACE inhibitory peptides has been studied. It is also known that (hydroxy)proline-containing peptides are generally resistant to degradation by digestive enzymes. Peptides can be absorbed intact through the intestine by paracellular and transcellular routes, but the potency of the bioactivity after absorption is inversely correlated to chain length. In addition, some strategies are proposed to increase the bioavailability of ACE inhibitory peptides. Further research into the bioavailability of ACE inhibitory peptides will lead to the development of more effective ACE inhibitory peptides and foods. [PUBLICATION ABSTRACT]
Keyword Bioactive peptides
Gastrointestinal digestion
Intestinal transport
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: Excellence in Research Australia (ERA) - Collection
Advanced Water Management Centre Publications
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Created: Fri, 13 Feb 2009, 15:23:23 EST by Joanne Mellor on behalf of Advanced Water Management Centre