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Enzymatic Production of Protein Hydrolysates from Steelhead (Oncorhynchus mykiss) Skin Gelatin as Inhibitors of Dipeptidyl-Peptidase IV and Angiotensin-I converting Enzyme Cheung, Imelda Wing Yan; Li-Chan, Eunice

Abstract

The objective of this study was to generate protein hydrolysates with dual in vitro inhibitory activities against dipeptidyl-peptidase IV (DPP-IV) and angiotensin-I converting enzyme (ACE), by proteolytic enzymes acting either individually or sequentially on steelhead skin gelatin. The results showed strong dual bioactivity in the low molecular weight (< 3 kDa) fractions obtained by ultrafiltration of hydrolysates produced using the enzymes pepsin, CorolaseN or papain. Alternatively, unfractionated hydrolysates exhibiting high ACE and DPP-IV inhibitory activities as well as yields could be attained by strategic selection of two enzymes for successive hydrolysis of gelatin. In particular, hydrolysates produced using 4% papain for 2 h followed either by ultrafiltration or by a second hydrolysis with 1% CorolaseN for 2 h, presented potent dual activity as ACE and DPP-IV inhibitors, and should be investigated further as potential functional food ingredients or nutraceuticals for the management of hypertension and diabetes.

Item Metadata

Title
Enzymatic Production of Protein Hydrolysates from Steelhead (Oncorhynchus mykiss) Skin Gelatin as Inhibitors of Dipeptidyl-Peptidase IV and Angiotensin-I converting Enzyme
Creator
Cheung, Imelda Wing Yan; Li-Chan, Eunice
Date Issued
2016-12-01
Description
The objective of this study was to generate protein hydrolysates with dual in vitro inhibitory activities against dipeptidyl-peptidase IV (DPP-IV) and angiotensin-I converting enzyme (ACE), by proteolytic enzymes acting either individually or sequentially on steelhead skin gelatin. The results showed strong dual bioactivity in the low molecular weight (< 3 kDa) fractions obtained by ultrafiltration of hydrolysates produced using the enzymes pepsin, CorolaseN or papain. Alternatively, unfractionated hydrolysates exhibiting high ACE and DPP-IV inhibitory activities as well as yields could be attained by strategic selection of two enzymes for successive hydrolysis of gelatin. In particular, hydrolysates produced using 4% papain for 2 h followed either by ultrafiltration or by a second hydrolysis with 1% CorolaseN for 2 h, presented potent dual activity as ACE and DPP-IV inhibitors, and should be investigated further as potential functional food ingredients or nutraceuticals for the management of hypertension and diabetes.
Subject
gelatin hydrolysate; enzymatic hydrolysis; dipeptidyl-peptidase IV inhibitory activity; angiotensin-I converting enzyme inhibitory activity; ultrafiltration
Genre
Article; Postprint
Type
Text
Language
eng
Date Available
2017-12-01
Provider
Vancouver : University of British Columbia Library
Rights
Attribution-NonCommercial-NoDerivatives 4.0 International
DOI
10.14288/1.0343428
URI
http://hdl.handle.net/2429/61083
Affiliation
Land and Food Systems, Faculty of
Citation
Cheung, I.W.Y. and Li-Chan, E.C.Y. 2017. Enzymatic production of protein hydrolysates from steelhead (Oncorhynchus mykiss) skin gelatin as inhibitors of dipeptidyl-peptidase IV and angiotensin-I converting enzyme. Journal of Functional Foods 28:254-264.
Publisher DOI
10.1016/j.jff.2016.10.030
Peer Review Status
Reviewed
Scholarly Level
Faculty
Rights URI
http://creativecommons.org/licenses/by-nc-nd/4.0/
Aggregated Source Repository
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Attribution-NonCommercial-NoDerivatives 4.0 International