Enzymatic production of protein hydrolysates from steelhead (Oncorhynchus mykiss) skin gelatin as inhibitors of dipeptidyl-peptidase IV and angiotensin-I converting enzyme

被引:43
作者
Cheung, Imelda W. Y. [1 ]
Li-Chan, Eunice C. Y. [1 ]
机构
[1] Univ British Columbia, Fac Land & Food Syst, Food Nutr & Hlth Program, 2205 East Mall, Vancouver, BC V6T 1Z4, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
Gelatin hydrolysate; Enzymatic hydrolysis; Dipeptidyl-peptidase IV inhibitory activity; Angiotensin-I converting enzyme inhibitory activity; Ultrafiltration; FUNCTIONAL-PROPERTIES; HYPERTENSION; FISH; ANTIOXIDANT; MANAGEMENT; OXIDATION; DATABASE;
D O I
10.1016/j.jff.2016.10.030
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
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. (C) 2016 Elsevier Ltd. All rights reserved.
引用
收藏
页码:254 / 264
页数:11
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