British Journal of Nutrition

Review article

Bioavailability of angiotensin I converting enzyme inhibitory peptides

Vanessa Vermeirssena1a2, John Van Campa2 and Willy Verstraetea1 c1

a1 Laboratory for Microbial Ecology and Technology and Nutrition, Ghent University, Faculty of Agriculture and Applied Biological Sciences, Ghent, Belgium

a2 Department of Food Technology and Nutrition, Ghent University, Faculty of Agriculture and Applied Biological Sciences, Ghent Belgium


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.

(Received January 08 2004)

(Accepted April 06 2004)


c1 *Corresponding author: fax + 32 92 64 62 48, Email