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 J. |
|
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 |
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 |
|