UBC Faculty Research and Publications

Do whey protein-derived peptides have dual dipeptidyl-peptidase IV and angiotensin I-converting enzyme inhibitory activities? Lacroix, Isabelle Marie Estelle; Meng, Guangtao; Cheung, Imelda Wing Yan; Li-Chan, Eunice

Abstract

Inhibition of dipeptidyl-peptidase IV (DPP-IV) and angiotensin I-converting enzyme (ACE) are useful strategies for managing, respectively, diabetes and hypertension, two conditions often occurring together. In this study, debittered and nondebittered whey protein hydrolysates (WPHs) were assessed for their in vitro inhibitory activity against ACE and DPP-IV and characterized for their constituent peptides. All WPHs and several fractions obtained from them had ACE and DPP-IV inhibitory activities, with ACE being generally more strongly inhibited than DPP-IV. Among the identified peptides tested, GYGGVSLPEW derived from α-lactalbumin and LKPTPEGDLE from β-lactoglobulin were, respectively, the most effective at inhibiting ACE (IC⁵⁰ = 2 μM) and DPP-IV (IC50 = 42 μM). Although some identified peptides were able to inhibit both enzymes, the majority did not show a dual inhibitory effect. This research provides new insight on the active peptides responsible for the ACE and DPP-IV inhibitory activities of whey protein hydrolysates.

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Attribution-NonCommercial-NoDerivatives 4.0 International

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