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Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates

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dc.contributor.author Nongonierma, Alice B.
dc.contributor.author Fitzgerald, Richard J.
dc.date.accessioned 2017-04-13T10:47:21Z
dc.date.available 2017-04-13T10:47:21Z
dc.date.issued 2013
dc.identifier.citation Nongonierma, AB,FitzGerald, RJ (2013) 'Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates'. Peptides, 39 :157-163. en_US
dc.identifier.uri http://hdl.handle.net/10344/5710
dc.description peer-reviewed en_US
dc.description.abstract Selected synthetic dipeptides and milk protein hydrolysates were evaluated for their dipeptidyl peptidase IV (DPP-IV) inhibitory properties, and their superoxide (SO) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activities. DPP-IV inhibition was seen with eight out of the twelve dipeptides and 5 of the twelve hydrolysates studied. Trp-Val inhibited DPP-IV, however, inhibition was not observed with the reverse peptide Val-Trp. The most potent hydrolysate inhibitors were generated from casein (CasH2) and lactoferrin (LFH1). Two Trp containing dipeptides, Trp-Val and Val-Trp, and three lactoferrin hydrolysates scavenged DPPH. The dipeptides had higher SO EC50 values compared to the milk protein hydrolysates (arising from three lactoferrin and one whey protein hydrolysates). Higher molecular mass fractions of the milk protein hydrolysates were associated with the SO scavenging activity. Trp-Val and one lactoferrin hydrolysate (LFH1) were multifunctional displaying both DPP-IV inhibitory and antioxidant (SO and DPPH scavenging) activities. These compounds may have potential as dietary ingredients in the management of type 2 diabetes by virtue of their ability to scavenge reactive oxygen species and to extend the half-life of incretin molecules. (C) 2012 Elsevier Inc. All rights reserved. en_US
dc.language.iso eng en_US
dc.publisher Elsevier en_US
dc.relation.ispartofseries Peptides;39, pp. 157-163
dc.relation.uri http://dx.doi.org/10.1016/j.peptides.2012.11.016
dc.rights This is the author’s version of a work that was accepted for publication in Peptides. 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 Peptides, 39, pp. 157-163, http://dx.doi.org/10.1016/j.peptides.2012.11.016 en_US
dc.subject dipeptidyl peptidase IV inhibitors en_US
dc.subject 2,2-diphenyl-1-picrylhydrazyl (DPPH) en_US
dc.subject superoxide en_US
dc.subject antioxidant en_US
dc.subject tryptophan en_US
dc.title Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates 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 2017-04-10T18:23:20Z
dc.description.version ACCEPTED
dc.identifier.doi 10.1016/j.peptides.2012.11.016
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 1436621
dc.internal.copyrightchecked Yes
dc.identifier.journaltitle Peptides
dc.description.status peer-reviewed


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