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

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• 作者：Silvana T. Silveira¹ ; Daniel Martí ; nez-Maqueda ; Isidra Recio ; Blanca Herná ; ndez-Ledesma ; ^{b.hernandez@csic.es}
• 关键词：Dipeptidyl dipeptidase IV inhibitors ; Type 2 diabetes ; Whey protein concentrate ; Tryptic hydrolysis ; Bioactive peptide
• 刊名：Food Chemistry
• 出版年：2013
• 出版时间：15 November, 2013
• 年：2013
• 卷：141
• 期：2
• 页码：1072-1077
• 全文大小：382 K

文摘

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 ¦Â-lactoglobulin as natural source of DPP-IV inhibitory peptides. A whey protein concentrate rich in ¦Â-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 ¦Â-lactoglobulin f(78-82) which IC₅₀ value was 44.7 ¦ÌM. The results suggest that peptides derived from ¦Â-lactoglobulin would be beneficial ingredients of foods against type 2 diabetes.