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Susceptibility of milk protein-derived peptides to dipeptidyl peptidase IV (DPP-IV) hydrolysis

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dc.contributor.author Nongonierma, Alice B.
dc.contributor.author Fitzgerald, Richard J.
dc.date.accessioned 2017-04-21T10:58:37Z
dc.date.available 2017-04-21T10:58:37Z
dc.date.issued 2014
dc.identifier.uri http://hdl.handle.net/10344/5727
dc.description peer-reviewed en_US
dc.description.abstract In silico digestion of milk protein-derived peptides with gastrointestinal enzyme activities was used to predict the release of peptides with a Pro residue at position 2 from the N terminus. These peptides are known to act as preferred dipeptidyl peptidase IV (DPP-IV) substrates. Five casein-derived synthetic peptides (Ile-Pro-Ile-Gin-Tyr, Leu-Pro-Leu-Pro-Leu, Tyr-Pro-Tyr-Tyr, Leu-Pro-Tyr-Pro-Tyr and Ile-Pro-Ile) and a casein (CasH), whey (WPH) and lactoferrin hydrolysate (LFH) generated with gastrointestinal enzymes were incubated with DPP-IV at 37 degrees C for 18 or 24 h. Peptide breakdown was evident following incubation with DPP-IV. Different modes of DPP-IV inhibition were observed depending on the test compound. Ile-Pro-Ile-Gln-Tyr, Tyr-Pro-Tyr-Tyr and Leu-Pro-Tyr-Pro-Tyr were substrate-, Leu-Pro-Leu-Pro-Leu and CasH were prodrug- while WPH and LFH were true DPP-IV inhibitors. These results are relevant for the bioactivity and bioavailability of functional foods targeting DPP-IV inhibition with potential blood glucose regulatory properties in humans. (C) 2013 Elsevier Ltd. All rights reserved. en_US
dc.language.iso eng en_US
dc.publisher Elsevier en_US
dc.relation.ispartofseries Food Chemistry;145, pp. 845-852
dc.relation.uri http://dx.doi.org/10.1016/j.foodchem.2013.08.097
dc.rights This is the author’s version of a work that was accepted for publication in Food Chemistry. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Food Chemistry, 145, pp. 845-852, http://dx.doi.org/10.1016/j.foodchem.2013.08.097 en_US
dc.subject dipeptidyl peptidase IV inhibitors en_US
dc.subject substrate-type inhibition en_US
dc.subject prodrug-type inhibition en_US
dc.subject antioxidant en_US
dc.title Susceptibility of milk protein-derived peptides to dipeptidyl peptidase IV (DPP-IV) hydrolysis en_US
dc.type info:eu-repo/semantics/article en_US
dc.type.supercollection all_ul_research en_US
dc.type.supercollection ul_published_reviewed en_US
dc.date.updated 2017-04-10T18:21:45Z
dc.description.version ACCEPTED
dc.identifier.doi 10.1016/j.foodchem.2013.08.097
dc.contributor.sponsor EI en_US
dc.relation.projectid CC20080001 en_US
dc.rights.accessrights info:eu-repo/semantics/openAccess en_US
dc.internal.rssid 1556023
dc.internal.copyrightchecked Yes
dc.identifier.journaltitle Food Chemistry
dc.description.status peer-reviewed


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