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Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: a source of antidiabetic peptides

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dc.contributor.author Harnedy, Pádraigín A.
dc.contributor.author Parthsarathy, Vadivel
dc.contributor.author McLaughlin, Chris M.
dc.contributor.author O'Keeffe, Martina B.
dc.contributor.author Allsopp, Philip J.
dc.contributor.author McSorley, Emeir M.
dc.contributor.author O'Harte, Finbarr P.M.
dc.contributor.author Fitzgerald, Richard J.
dc.date.accessioned 2018-02-20T15:11:53Z
dc.date.issued 2018
dc.identifier.uri http://hdl.handle.net/10344/6582
dc.description peer-reviewed en_US
dc.description.abstract Large quantities of low-value protein rich co-products, such as salmon skin and trimmings, are generated annually. These co-products can be upgraded to high-value functional ingredients. The aim of this study was to assess the antidiabetic potential of salmon skin gelatin and trimmings-derived protein hydrolysates in vitro. The gelatin hydrolysate generated with Alcalase 2.4L and Flavourzyme 500L exhibited significantly higher (p < 0.001) insulin and GLP-1 secretory activity from pancreatic BRIN-BD11 and enteroendocrine GLUTag cells, respectively, when tested at 2.5 mg/mL compared to hydrolysates generated with Alcalase 2.4L or Promod 144MG. The gelatin hydrolysate generated with Alcalase 2.4L and Flavourzyme 500L showed significantly more potent (p < 0.01) DPP-IV inhibitory activity than those generated with Alcalase 2.4L or Promod 144MG. No significant difference was observed in the insulinotropic activity mediated by any of the trimmings-derived hydrolysates when tested at 2.5 mg/mL. However, the trimmings hydrolysate generated with Alcalase 2.4L and Flavourzyme 500L exhibited significantly higher DPP-IV inhibitory (p < 0.05:Alcalase 2.4L and p < 0.01:Promod 144MG) and GLP-1 (p < 0.001, 2.5 mg/mL) secretory activity than those generated with Alcalase 2.4L or Promod 144MG. The salmon trimmings hydrolysate generated with Alcalase 2.4L and Flavourzyme 500L when subjected to simulated gastrointestinal digestion (SGID) was shown to retain its GLP-1 secretory and DPP-IV inhibitory activities, in addition to improving its insulin secretory activity. However, the gelatin hydrolysate generated with Alcalase 2.4L and Flavourzyme 500L was shown to lose GLP-1 secretory activity following SGID. A significant increase in membrane potential (p < 0.001) and intracellular calcium (p < 0.001) by both co-product hydrolysates generated with Alcalase 2.4L and Flavourzyme 500L suggest that both hydrolysates mediate their insulinotropic activity through the KATP channel-dependent pathway. Additionally, by stimulating a significant increase in intracellular cAMP release (p < 0.05) it is likely that the trimmings-derived hydrolysate may also mediate insulin secretion through the protein kinase A pathway. The results presented herein demonstrate that salmon co-product hydrolysates exhibit promising in vitro antidiabetic activity. en_US
dc.language.iso eng en_US
dc.publisher Elsevier en_US
dc.relation.ispartofseries Food Research International;106, pp. 598-605
dc.relation.uri https://doi.org/10.1016/j.foodres.2018.01.025
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, 2018, 106, 598-605, https://doi.org/10.1016/j.foodres.2018.01.025 en_US
dc.subject salmon skin en_US
dc.subject co-products en_US
dc.subject gelatin en_US
dc.subject muscle en_US
dc.subject protein hydrolysate en_US
dc.subject peptide en_US
dc.subject antidiabetic en_US
dc.subject trimmings en_US
dc.title Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: a source of antidiabetic 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.identifier.doi 10.1016/j.foodres.2018.01.025
dc.contributor.sponsor Department of Agriculture, Food and the Marine en_US
dc.contributor.sponsor SFI en_US
dc.contributor.sponsor Programme for Research in Third Level Institutions (cycle 4) 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 2019-01-16
dc.embargo.terms 2019-01-16 en_US
dc.rights.accessrights info:eu-repo/semantics/openAccess en_US
dc.internal.rssid 2868793


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