Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in β-lactoglobulin

被引:195
作者
Silveira, Silvana T. [1 ]
Martinez-Maqueda, Daniel [1 ]
Recio, Isidra [1 ]
Hernandez-Ledesma, Blanca [1 ]
机构
[1] CEI UAM CSIC, CSIC UAM, CIAL, Inst Invest Ciencias Alimentac, Madrid 28049, Spain
关键词
Dipeptidyl dipeptidase IV inhibitors; Type; 2; diabetes; Whey protein concentrate; Tryptic hydrolysis; Bioactive peptide; GLUCAGON-LIKE PEPTIDE-1; ANTIDIABETIC AGENTS; 7-36; AMIDE; MILK; IDENTIFICATION; GLUCOSE; CHEESE; RATS; FAT;
D O I
10.1016/j.foodchem.2013.03.056
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Dipeptidyl peptidase-IV (DPP-IV) is a serine protease involved in the degradation and inactivation of incretin hormones that act by stimulating glucose-dependent insulin secretion after meal ingestion. DPP-IV inhibitors have emerged as new and promising oral agents for the treatment of type 2 diabetes. The purpose of this study was to investigate the potential of beta-lactoglobulin as natural source of DPP-IV inhibitory peptides. A whey protein concentrate rich in beta-lactoglobulin was hydrolysed with trypsin and fractionated using a chromatographic separation at semipreparative scale. Two of the six collected fractions showed notable DPP-IV inhibitory activity. These fractions were analysed by HPLC coupled to tandem mass spectrometry (HPLC-MS/MS) to identify peptides responsible for the observed activity. The most potent fragment (IPAVF) corresponded to beta-lactoglobulin f(78-82) which IC50 value was 44.7 mu M. The results suggest that peptides derived from beta-lactoglobulin would be beneficial ingredients of foods against type 2 diabetes. (C) 2013 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1072 / 1077
页数:6
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