Do whey protein-derived peptides have dual dipeptidyl-peptidase IV and angiotensin I-converting enzyme inhibitory activities?

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.

Item Metadata

Title	Do whey protein-derived peptides have dual dipeptidyl-peptidase IV and angiotensin I-converting enzyme inhibitory activities?
Creator	Lacroix, Isabelle Marie Estelle; Meng, Guangtao; Cheung, Imelda Wing Yan; Li-Chan, Eunice
Date Issued	2015-12-11
Description	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.
Subject	Angiotensin I-converting enzyme; dipeptidyl-peptidase IV; whey protein hydrolysates; bioactive peptides; dual inhibitors
Genre	Article; Postprint
Type	Text
Language	eng
Date Available	2017-04-11
Provider	Vancouver : University of British Columbia Library
Rights	Attribution-NonCommercial-NoDerivatives 4.0 International
DOI	10.14288/1.0343557
URI	http://hdl.handle.net/2429/61180
Affiliation	Land and Food Systems, Faculty of
Citation	Lacroix, I.M.E., Meng, G., Cheung, I.W.Y., and Li-Chan, E.C.Y. 2016. Do whey protein-derived peptides have dual dipeptidyl-peptidase IV and angiotensin I-converting enzyme inhibitory activities? Journal of Functional Foods 21: 87-96.
Publisher DOI	10.1016/j.jff.2015.11.038
Peer Review Status	Reviewed
Scholarly Level	Faculty; Postdoctoral
Rights URI	http://creativecommons.org/licenses/by-nc-nd/4.0/
Aggregated Source Repository	DSpace

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