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乳清分离蛋白(MPI)作为二肽基肽酶IV(DPP-IV)抑制肽的来源。

Milk protein isolate (MPI) as a source of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides.

作者信息

Nongonierma Alice B, Lalmahomed Mehdeeyah, Paolella Sara, FitzGerald Richard J

机构信息

Department of Biological Sciences, University of Limerick, Limerick, Ireland; Food for Health Ireland (FHI), University of Limerick, Limerick, Ireland.

Department of Biological Sciences, University of Limerick, Limerick, Ireland.

出版信息

Food Chem. 2017 Sep 15;231:202-211. doi: 10.1016/j.foodchem.2017.03.123. Epub 2017 Mar 23.

DOI:10.1016/j.foodchem.2017.03.123
PMID:28449998
Abstract

A multifactorial [temperature (40, 50 and 60°C), hydrolysis time (60, 150 and 240min) and enzyme to substrate ratio (E:S; 1.0, 1.5 and 2.0%)] design of experiments (DOE) was used to optimise the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides during hydrolysis of bovine milk protein isolate (MPI) with Neutrase 0.8L™, yielding 15 hydrolysates (H1-H15). Variation in temperature and time had a significant effect on DPP-IV inhibitory properties (p<0.05) in contrast with E:S (p>0.05). The DPP-IV half maximal inhibitory concentration (IC) of H4, a potent sample, was maintained following simulated gastrointestinal digestion (SGID, DPP-IV IC=0.60±0.06vs. 0.58±0.09mgml, p>0.05). Several peptides with DPP-IV inhibitory features or known activity were identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS) within the hydrolysates. MPI hydrolysates may have potential for use as dietary ingredients with serum glucose lowering activity in humans.

摘要

采用多因素[温度(40、50和60°C)、水解时间(60、150和240分钟)以及酶与底物比例(E:S;1.0%、1.5%和2.0%)]实验设计(DOE),以优化用Neutrase 0.8L™水解乳清分离蛋白(MPI)过程中二肽基肽酶IV(DPP-IV)抑制肽的释放,得到15种水解产物(H1-H15)。与酶与底物比例(p>0.05)相比,温度和时间的变化对DPP-IV抑制特性有显著影响(p<0.05)。经过模拟胃肠道消化(SGID)后,有效样品H4的DPP-IV半数最大抑制浓度(IC)保持不变(DPP-IV IC=0.60±0.06对0.58±0.09mg/ml,p>0.05)。通过液相色谱-串联质谱(LC-MS/MS)在水解产物中鉴定出几种具有DPP-IV抑制特性或已知活性的肽。MPI水解产物可能有潜力用作具有降低人体血清葡萄糖活性的膳食成分。

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