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

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 trimmingderived protein...

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Published in:Food Research International
Main Authors: Harnedy, Pàdraigín A., Parthsarathy, Vadivel, McLaughlin, Chris M., O'Keeffe, Martina B., Allsopp, Philip J., McSorley, Emeir M., O'Harte, Finbarr P. M., FitzGerald, Richard J.
Format: Article in Journal/Newspaper
Language:unknown
Published: Elsevier 2018
Subjects:
Online Access:http://hdl.handle.net/10545/622900
https://doi.org/10.1016/j.foodres.2018.01.025
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spelling ftunivderby:oai:derby.openrepository.com:10545/622900 2023-05-15T15:33:05+02:00 Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: A source of antidiabetic peptides Harnedy, Pàdraigín A. Parthsarathy, Vadivel McLaughlin, Chris M. O'Keeffe, Martina B. Allsopp, Philip J. McSorley, Emeir M. O'Harte, Finbarr P. M. FitzGerald, Richard J. 2018-02-06 http://hdl.handle.net/10545/622900 https://doi.org/10.1016/j.foodres.2018.01.025 unknown Elsevier http://uir.ulster.ac.uk/39534/ Harnedy, PA, Parthsarathy, Vadivel, McLaughlin, CM, O'Keeffe, MB, Allsopp, Philip, McSorley, Emeir M, O'Harte, Finbarr and FitzGerald, RG (2018) Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: A source of antidiabetic peptides. Food Research International, 106 . pp. 598-606. 0963-9969 doi:10.1016/j.foodres.2018.01.025 http://hdl.handle.net/10545/622900 Food Research International salmon co-products gelatin muscle protein hydrolysate peptide antidiabetic trimmings Journal article 2018 ftunivderby https://doi.org/10.1016/j.foodres.2018.01.025 2020-09-04T06:43:34Z 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 trimmingderived 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 trimming-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 trimming-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. Department of Agriculture, Food and the Marine, Ireland, Department of Employment and Learning (DEL), Science Foundation Ireland Infrastructure, Higher Education Authority Article in Journal/Newspaper Atlantic salmon Salmo salar UDORA - The University of Derby Online Research Archive Food Research International 106 598 606
institution Open Polar
collection UDORA - The University of Derby Online Research Archive
op_collection_id ftunivderby
language unknown
topic salmon
co-products
gelatin
muscle
protein hydrolysate
peptide
antidiabetic
trimmings
spellingShingle salmon
co-products
gelatin
muscle
protein hydrolysate
peptide
antidiabetic
trimmings
Harnedy, Pàdraigín A.
Parthsarathy, Vadivel
McLaughlin, Chris M.
O'Keeffe, Martina B.
Allsopp, Philip J.
McSorley, Emeir M.
O'Harte, Finbarr P. M.
FitzGerald, Richard J.
Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: A source of antidiabetic peptides
topic_facet salmon
co-products
gelatin
muscle
protein hydrolysate
peptide
antidiabetic
trimmings
description 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 trimmingderived 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 trimming-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 trimming-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. Department of Agriculture, Food and the Marine, Ireland, Department of Employment and Learning (DEL), Science Foundation Ireland Infrastructure, Higher Education Authority
format Article in Journal/Newspaper
author Harnedy, Pàdraigín A.
Parthsarathy, Vadivel
McLaughlin, Chris M.
O'Keeffe, Martina B.
Allsopp, Philip J.
McSorley, Emeir M.
O'Harte, Finbarr P. M.
FitzGerald, Richard J.
author_facet Harnedy, Pàdraigín A.
Parthsarathy, Vadivel
McLaughlin, Chris M.
O'Keeffe, Martina B.
Allsopp, Philip J.
McSorley, Emeir M.
O'Harte, Finbarr P. M.
FitzGerald, Richard J.
author_sort Harnedy, Pàdraigín A.
title Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: A source of antidiabetic peptides
title_short Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: A source of antidiabetic peptides
title_full Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: A source of antidiabetic peptides
title_fullStr Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: A source of antidiabetic peptides
title_full_unstemmed Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: A source of antidiabetic peptides
title_sort atlantic salmon (salmo salar) co-product-derived protein hydrolysates: a source of antidiabetic peptides
publisher Elsevier
publishDate 2018
url http://hdl.handle.net/10545/622900
https://doi.org/10.1016/j.foodres.2018.01.025
genre Atlantic salmon
Salmo salar
genre_facet Atlantic salmon
Salmo salar
op_relation http://uir.ulster.ac.uk/39534/
Harnedy, PA, Parthsarathy, Vadivel, McLaughlin, CM, O'Keeffe, MB, Allsopp, Philip, McSorley, Emeir M, O'Harte, Finbarr and FitzGerald, RG (2018) Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: A source of antidiabetic peptides. Food Research International, 106 . pp. 598-606.
0963-9969
doi:10.1016/j.foodres.2018.01.025
http://hdl.handle.net/10545/622900
Food Research International
op_doi https://doi.org/10.1016/j.foodres.2018.01.025
container_title Food Research International
container_volume 106
container_start_page 598
op_container_end_page 606
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