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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
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Creator | |
Date Issued |
2016-12-01
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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.
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Subject | |
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Type | |
Language |
eng
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Date Available |
2017-12-01
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Provider |
Vancouver : University of British Columbia Library
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Rights |
Attribution-NonCommercial-NoDerivatives 4.0 International
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DOI |
10.14288/1.0343428
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URI | |
Affiliation | |
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.
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Publisher DOI |
10.1016/j.jff.2016.10.030
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Peer Review Status |
Reviewed
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Scholarly Level |
Faculty
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Rights URI | |
Aggregated Source Repository |
DSpace
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Item Citations and Data
Rights
Attribution-NonCommercial-NoDerivatives 4.0 International