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Identification and characterisation of peptides from a boarfish (Capros aper) protein hydrolysate displaying in vitro dipeptidyl peptidase-IV (DPP-IV) inhibitory and insulinotropic activity

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dc.contributor.author Harnedy-Rothwell, Pádraigín A.
dc.contributor.author McLaughlin, Chris M.
dc.contributor.author O'Keeffe, Martina B.
dc.contributor.author Le Gouic, Aurélien V.
dc.contributor.author Allsopp, Philip J.
dc.contributor.author McSorley, Emeir M.
dc.contributor.author Sharkey, Shaun
dc.contributor.author Whooley, Jason
dc.contributor.author McGovern, Brian
dc.contributor.author O'Harte, Finbarr P.M.
dc.contributor.author Fitzgerald, Richard J.
dc.date.accessioned 2020-04-01T15:25:47Z
dc.date.issued 2020
dc.identifier.issn 0963-9969
dc.identifier.uri http://hdl.handle.net/10344/8680
dc.description peer-reviewed en_US
dc.description The full text of this article will not be available in ULIR until the embargo expires on the 21/01/2021
dc.description.abstract Twenty-two novel dipeptidyl peptidase-IV (DPP-IV) inhibitory peptides (with IC50 values <200 µM) and fifteen novel insulinotropic peptides were identified in a boarfish protein hydrolysate generated at semi-pilot scale using Alcalase 2.4L and Flavourzyme 500L. This was achieved by bioassay-driven semi preparative reverse phase-high performance liquid chromatography fractionation, liquid chromatography-mass spectrometry and confirmatory studies with synthetic peptides. The most potent DPP-IV inhibitory peptide (IPVDM) had a DPP-IV half maximal inhibitory concentration (IC50) values of 21.72 ± 1.08 µM in a conventional in vitro and 44.26 ± 0.65 µM in an in situ cell-based (Caco 2) DPP-IV inhibition assay. Furthermore, this peptide stimulated potent insulin secretory activity (1.6 fold increase compared to control) from pancreatic BRIN-BD11 cells grown in culture. The tripeptide IPV exhibited potent DPP-IV inhibitory activity (IC50: 5.61 ± 0.20 µM) comparable to that reported for the known DPP-IV inhibitor IPI (IC50: 5.61 µM). Boarfish proteins contain peptide sequences with potential to play a role in glycaemic management in vivo. en_US
dc.language.iso eng en_US
dc.publisher Elsevier en_US
dc.relation.ispartofseries Food Research International;131, 108989
dc.rights This is the author’s version of a work that was accepted for publication in Food Research International. 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 Research International, 2020, 131, 108989, https://doi.org/10.1016/j.foodres.2020.108989 en_US
dc.subject Bioactive peptide en_US
dc.subject Boarfish en_US
dc.subject Dipeptidyl peptidase-IV en_US
dc.subject Insulinotropic en_US
dc.subject Type 2 diabetes en_US
dc.title Identification and characterisation of peptides from a boarfish (Capros aper) protein hydrolysate displaying in vitro dipeptidyl peptidase-IV (DPP-IV) inhibitory and insulinotropic activity 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 2020-04-01T15:16:39Z
dc.identifier.doi 10.1016/j.foodres.2020.108989
dc.contributor.sponsor Department of Agriculture, Food and the Marine, IRE en_US
dc.relation.projectid 11/F/063 en_US
dc.relation.projectid 11/F/064 en_US
dc.relation.projectid 13/F/467 en_US
dc.relation.projectid 13/F/536 en_US
dc.relation.projectid 14/F/873 en_US
dc.date.embargoEndDate 2021-01-21
dc.embargo.terms 2021-01-21 en_US
dc.rights.accessrights info:eu-repo/semantics/embargoedAccess en_US
dc.internal.rssid 2942593
dc.internal.copyrightchecked Yes
dc.identifier.journaltitle Food Research International
dc.description.status peer-reviewed


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