Dipeptidyl peptidase IV (DPP-IV) inhibitory properties of camel milk protein hydrolysates generated with trypsin

被引：85

作者：

Nongonierma, Alice B. ^{[1
,2
]}

Paolella, Sara ^{[1
,2
]}

Mudgil, Priti ^{[3
]}

Maqsood, Sajid ^{[3
]}

FitzGerald, Richard R. ^{[1
,2
]}

机构：

[1] Univ Limerick, Dept Biol Sci, Limerick, Ireland

[2] Univ Limerick, FHI, Limerick, Ireland

[3] United Arab Emirates Univ, Dept Food Sci, Coll Food & Agr, Al Ain 15551, U Arab Emirates

来源：

JOURNAL OF FUNCTIONAL FOODS | 2017年 / 34卷

基金：

爱尔兰科学基金会;

关键词：

Dipeptidyl peptidase IV inhibition; Camel milk proteins; Bioactive peptides; Trypsin; Response surface methodology (RSM); In silico analysis; ANGIOTENSIN-CONVERTING ENZYME; IN-VITRO; GASTROINTESTINAL DIGESTION; ANTIOXIDANT ACTIVITIES; BIOACTIVE PROPERTIES; BETA-LACTOGLOBULIN; DIETARY PROTEINS; BOVINE-MILK; CASEIN; IDENTIFICATION;

D O I：

10.1016/j.jff.2017.04.016

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Dipeptidyl peptidase IV (DPP-IV) inhibitory peptides were identified in silico within camel milk proteins. Camel milk was hydrolysed with trypsin using a design of experiments (DOE, temperature (40-60 degrees C), enzyme to substrate (E:S) ratio (0.50-2.00% (w/w)) and time (60-240 min)). Fifteen hydrolysates (H1-H15) having DPP-IV half maximal inhibitory concentration (IC50) values between 0.52 +/- 0.06 (H9) and 1.26 +/- 0.13 (H1) mg mL(-1) were produced. Camel and bovine milk proteins hydrolysed at 40 degrees C, 1.8% E:S and 218 min had DPP-IV IC50 values of 0.68 +/- 0.08 and 0.85 +/- 0.10 mg mL(-1) (p < 0.05), respectively. Potent and unique DPP-IV inhibitory peptides (Leu-Pro-Val-Pro-Gln and Trp-Lys) were identified in camel milk protein hydrolysates, which were not present in bovine milk protein hydrolysates. The DPP-IV inhibitory properties of camel milk peptides were reported for the first time in this study. Camel milk is an interesting substrate to further investigate for its antidiabetic potential. (C) 2017 Elsevier Ltd. All rights reserved.

引用

页码：49 / 58

页数：10

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