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Bioavailability of angiotensin I converting enzyme inhibitory peptides

Published online by Cambridge University Press:  09 March 2007

Vanessa Vermeirssen ,
John Van Camp  and
Willy Verstraete
Vanessa Vermeirssen
Affiliation:
Laboratory for Microbial Ecology and Technology and Nutrition, Ghent University, Faculty of Agriculture and Applied Biological Sciences, Ghent, Belgium Department of Food Technology and Nutrition, Ghent University, Faculty of Agriculture and Applied Biological Sciences, GhentBelgium
John Van Camp
Affiliation:
Department of Food Technology and Nutrition, Ghent University, Faculty of Agriculture and Applied Biological Sciences, GhentBelgium
Willy Verstraete*
Affiliation:
Laboratory for Microbial Ecology and Technology and Nutrition, Ghent University, Faculty of Agriculture and Applied Biological Sciences, Ghent, Belgium
*
*Corresponding author: fax + 32 92 64 62 48, Email [email protected]
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Abstract

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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.

Keywords

Bioactive peptidesHypertensionGastrointestinal digestionIntestinal transport
Type
Review article
Information
British Journal of Nutrition , Volume 92 , Issue 3 , September 2004 , pp. 357 - 366
Copyright
Copyright © The Nutrition Society 2004

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