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 trimmings-derived prote...
Main Authors: | , , , , , , , |
---|---|
Format: | Other Non-Article Part of Journal/Newspaper |
Language: | unknown |
Published: |
2018
|
Subjects: | |
Online Access: | https://figshare.com/articles/journal_contribution/Atlantic_salmon_Salmo_salar_co-product-derived_protein_hydrolysates_a_source_of_antidiabetic_peptides/19821091 |
id |
ftunivlimericfig:oai:figshare.com:article/19821091 |
---|---|
record_format |
openpolar |
spelling |
ftunivlimericfig:oai:figshare.com:article/19821091 2023-05-15T15:32:54+02:00 Atlantic salmon (Salmo salar) co-product-derived protein hydrolysates: a source of antidiabetic peptides Pádraigín A. Harnedy Vadivel Parthsarathy Chris M. McLaughlin Martina B. O'Keeffe Philip J. Allsopp Emeir M. McSorley Finbarr P.M. O'Harte Richard J. Fitzgerald 2018-01-01T00:00:00Z https://figshare.com/articles/journal_contribution/Atlantic_salmon_Salmo_salar_co-product-derived_protein_hydrolysates_a_source_of_antidiabetic_peptides/19821091 unknown 10344/6582 https://figshare.com/articles/journal_contribution/Atlantic_salmon_Salmo_salar_co-product-derived_protein_hydrolysates_a_source_of_antidiabetic_peptides/19821091 CC BY-NC-SA 1.0 CC-BY-NC-SA salmon skin co-products gelatin muscle protein hydrolysate peptide antidiabetic trimmings Text Journal contribution 2018 ftunivlimericfig 2022-12-28T08:49:01Z 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 ... Other Non-Article Part of Journal/Newspaper Atlantic salmon Salmo salar Research from University of Limerick |
institution |
Open Polar |
collection |
Research from University of Limerick |
op_collection_id |
ftunivlimericfig |
language |
unknown |
topic |
salmon skin co-products gelatin muscle protein hydrolysate peptide antidiabetic trimmings |
spellingShingle |
salmon skin co-products gelatin muscle protein hydrolysate peptide antidiabetic trimmings Pádraigín A. Harnedy Vadivel Parthsarathy Chris M. McLaughlin Martina B. O'Keeffe Philip J. Allsopp Emeir M. McSorley Finbarr P.M. O'Harte Richard J. Fitzgerald 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 |
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 ... |
format |
Other Non-Article Part of Journal/Newspaper |
author |
Pádraigín A. Harnedy Vadivel Parthsarathy Chris M. McLaughlin Martina B. O'Keeffe Philip J. Allsopp Emeir M. McSorley Finbarr P.M. O'Harte Richard J. Fitzgerald |
author_facet |
Pádraigín A. Harnedy Vadivel Parthsarathy Chris M. McLaughlin Martina B. O'Keeffe Philip J. Allsopp Emeir M. McSorley Finbarr P.M. O'Harte Richard J. Fitzgerald |
author_sort |
Pádraigín A. Harnedy |
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 |
publishDate |
2018 |
url |
https://figshare.com/articles/journal_contribution/Atlantic_salmon_Salmo_salar_co-product-derived_protein_hydrolysates_a_source_of_antidiabetic_peptides/19821091 |
genre |
Atlantic salmon Salmo salar |
genre_facet |
Atlantic salmon Salmo salar |
op_relation |
10344/6582 https://figshare.com/articles/journal_contribution/Atlantic_salmon_Salmo_salar_co-product-derived_protein_hydrolysates_a_source_of_antidiabetic_peptides/19821091 |
op_rights |
CC BY-NC-SA 1.0 |
op_rightsnorm |
CC-BY-NC-SA |
_version_ |
1766363374822621184 |