Abstract

Angiotensin-I-converting enzyme (ACE) has been classically associated with the renin-angiotensin system which regulates peripheral blood pressure. Peptides derived from the major whey proteins, i.e. alpha-lactalbumin (alpha-la) and beta-lactoglobulin (beta-lg) in addition to bovine serum albumin (BSA), inhibit ACE. Some of these inhibitory peptides, i.e. alpha-lactorphin (alpha-la f(50-53)), beta-lactorphin (beta-lg f(102-105)), beta-lactotensin (beta-lg f(146-149) and albutensin A (BSA f(208-216)), have other bioactivities. The most potent lactokinin reported to date, (beta-lg f(142-148)), has an ACE IC50 of 42.6 mumol/l. While they do not have the inhibitory potency of synthetic drugs commonly used in the treatment of hypertension, these naturally occurring peptides may represent nutraceutical/functional food ingredients for the prevention/treatment of high blood pressure. Studies with gastric and pancreatic proteinase digests of whey proteins indicate that enzyme specificity rather than extent of hydrolysis dictates the ACE inhibitory potency of whey hydrolysates.