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Milk protein isolate (MPI) as a source of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides

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dc.contributor.author Nongonierma, Alice B.
dc.contributor.author Lalmahomed, Mehdeeyah
dc.contributor.author Paolella, Sara
dc.contributor.author Fitzgerald, Richard J.
dc.date.accessioned 2017-04-18T13:11:54Z
dc.date.issued 2017
dc.identifier.uri http://hdl.handle.net/10344/5717
dc.description peer-reviewed en_US
dc.description.abstract A multifactorial [temperature (40, 50 and 60 °C), hydrolysis time (60, 150 and 240 min) and enzyme to substrate ratio (E:S; 1.0, 1.5 and 2.0%)] design of experiments (DOE) was used to optimise the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides during hydrolysis of bovine milk protein isolate (MPI) with Neutrase 0.8L™, yielding 15 hydrolysates (H1-H15). Variation in temperature and time had a significant effect on DPP-IV inhibitory properties (p < 0.05) in contrast with E:S (p > 0.05). The DPP-IV half maximal inhibitory concentration (IC50) of H4, a potent sample, was maintained following simulated gastrointestinal digestion (SGID, DPP-IV IC50 = 0.60 ± 0.06 vs. 0.58 ± 0.09 mg ml−1, p > 0.05). Several peptides with DPP-IV inhibitory features or known activity were identified by liquid chromatography-tandem mass spectrometry (LC–MS/MS) within the hydrolysates. MPI hydrolysates may have potential for use as dietary ingredients with serum glucose lowering activity in humans. en_US
dc.language.iso eng en_US
dc.publisher Elsevier en_US
dc.relation.ispartofseries Food Chemistry;231, pp. 202-211
dc.relation.uri http://dx.doi.org/10.1016/j.foodchem.2017.03.123
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, 231, pp. 202-211, http://dx.doi.org/10.1016/j.foodchem.2017.03.123 en_US
dc.subject dipeptidyl peptidase IV inhibition en_US
dc.subject milk protein isolate en_US
dc.subject bioactive peptides en_US
dc.subject response surface methodology en_US
dc.title Milk protein isolate (MPI) as a source of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides 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 2017-04-11T11:07:43Z
dc.description.version ACCEPTED
dc.identifier.doi 10.1016/j.foodchem.2017.03.123
dc.contributor.sponsor EI en_US
dc.contributor.sponsor SFI en_US
dc.relation.projectid TC2013-0001 en_US
dc.date.embargoEndDate 2018-03-23
dc.embargo.terms 2018-03-23 en_US
dc.rights.accessrights info:eu-repo/semantics/openAccess en_US
dc.internal.rssid 2714881
dc.internal.copyrightchecked Yes
dc.identifier.journaltitle Food Chemistry
dc.description.status peer-reviewed


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