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Título: | Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in β-lactoglobulin |
Autor: | Silveira, Silvana T.; Martínez-Maqueda, D. CSIC ORCID; Recio, Isidra CSIC ORCID ; Hernández-Ledesma, Blanca CSIC ORCID | Palabras clave: | Type 2 diabetes Whey protein concentrate Tryptic hydrolysis Bioactive peptides Dipeptidyl dipeptidase IV inhibitors |
Fecha de publicación: | 2013 | Editor: | Elsevier | Citación: | Food Chemistry 141(2): 1072-1077 (2013) | Resumen: | 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 β-lactoglobulin as natural source of DPP-IV inhibitory peptides. A whey protein concentrate rich in β-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 β-lactoglobulin f(78-82) which IC 50 value was 44.7 u.M. The results suggest that peptides derived from β-lactoglobulin would be beneficial ingredients of foods against type 2 diabetes. © 2013 Elsevier Ltd. All rights reserved. | URI: | http://hdl.handle.net/10261/99916 | DOI: | 10.1016/j.foodchem.2013.03.056 | Identificadores: | doi: 10.1016/j.foodchem.2013.03.056 issn: 0308-8146 |
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