Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: a source of antidiabetic peptides
peer-reviewed 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...
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Online Access: | http://hdl.handle.net/10344/6582 https://doi.org/10.1016/j.foodres.2018.01.025 |
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ftunivlimerick:oai:ulir.ul.ie:10344/6582 2023-05-15T15:32:59+02:00 Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: a source of antidiabetic peptides Harnedy, Pádraigín A. Parthsarathy, Vadivel McLaughlin, Chris M. O'Keeffe, Martina B. Allsopp, Philip J. McSorley, Emeir M. O'Harte, Finbarr P.M. Fitzgerald, Richard J. Harnedy-Rothwell, Pádraigín A. Department of Agriculture, Food and the Marine SFI Programme for Research in Third Level Institutions (cycle 4) 2019-01-16 http://hdl.handle.net/10344/6582 https://doi.org/10.1016/j.foodres.2018.01.025 eng eng Elsevier Food Research International;106, pp. 598-605 https://doi.org/10.1016/j.foodres.2018.01.025 11/F/063 11/F/064 13/F/467 13/F/536 14/F/873 http://hdl.handle.net/10344/6582 doi:10.1016/j.foodres.2018.01.025 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 info:eu-repo/semantics/openAccess salmon skin co-products gelatin muscle protein hydrolysate peptide antidiabetic trimmings info:eu-repo/semantics/article all_ul_research ul_published_reviewed 2019 ftunivlimerick https://doi.org/10.1016/j.foodres.2018.01.025 2022-05-23T15:13:56Z peer-reviewed 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. ... Article in Journal/Newspaper Atlantic salmon Salmo salar University of Limerick: Institutional Repository (ULIR) Food Research International 106 598 606 |
institution |
Open Polar |
collection |
University of Limerick: Institutional Repository (ULIR) |
op_collection_id |
ftunivlimerick |
language |
English |
topic |
salmon skin co-products gelatin muscle protein hydrolysate peptide antidiabetic trimmings |
spellingShingle |
salmon skin co-products gelatin muscle protein hydrolysate peptide antidiabetic trimmings Harnedy, Pádraigín 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 skin co-products gelatin muscle protein hydrolysate peptide antidiabetic trimmings |
description |
peer-reviewed 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. ... |
author2 |
Harnedy-Rothwell, Pádraigín A. Department of Agriculture, Food and the Marine SFI Programme for Research in Third Level Institutions (cycle 4) |
format |
Article in Journal/Newspaper |
author |
Harnedy, Pádraigín 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, Pádraigín 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, Pádraigín 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 |
2019 |
url |
http://hdl.handle.net/10344/6582 https://doi.org/10.1016/j.foodres.2018.01.025 |
genre |
Atlantic salmon Salmo salar |
genre_facet |
Atlantic salmon Salmo salar |
op_relation |
Food Research International;106, pp. 598-605 https://doi.org/10.1016/j.foodres.2018.01.025 11/F/063 11/F/064 13/F/467 13/F/536 14/F/873 http://hdl.handle.net/10344/6582 doi:10.1016/j.foodres.2018.01.025 |
op_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 info:eu-repo/semantics/openAccess |
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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1766363455226380288 |