Identification of ACE I-inhibitory peptides released by the hydrolysis of tub gurnard (Chelidonichthys lucerna) skin proteins and the impact of their in silico gastrointestinal digestion

This article belongs to the Special Issue Sustainable Valorization of Seafood By-Products through Recovery of Valuable Bioactive Compounds.

Detalhes bibliográficos
Autores: Bougatef, Hajer, Vega-Fernández, Cristina de la, Sila, Assaâd, Bougatef, Ali, Martínez Álvarez, Óscar
Tipo de documento: artigo
Estado:Versão publicada
Data de publicação:2023
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositório:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/334611
Acesso em linha:http://hdl.handle.net/10261/334611
Access Level:Acceso aberto
Palavra-chave:By-catch
Protein hydrolysates
Angiotensin converting enzyme
Bioactive peptides
Upgrading
Fish skin
Tub gurnard
Functional ingredient
Chelidonichthys lucerna
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oai_identifier_str oai:digital.csic.es:10261/334611
network_acronym_str ES
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repository_id_str
spelling Identification of ACE I-inhibitory peptides released by the hydrolysis of tub gurnard (Chelidonichthys lucerna) skin proteins and the impact of their in silico gastrointestinal digestionBougatef, HajerVega-Fernández, Cristina de laSila, AssaâdBougatef, AliMartínez Álvarez, ÓscarBy-catchProtein hydrolysatesAngiotensin converting enzymeBioactive peptidesUpgradingFish skinTub gurnardFunctional ingredientChelidonichthys lucernaThis article belongs to the Special Issue Sustainable Valorization of Seafood By-Products through Recovery of Valuable Bioactive Compounds.Tub gurnard is a highly abundant fishery species caught as a discard in the Mediterranean Sea. This work proposes its valorisation through the release of potential antihypertensive peptides and glycosaminoglycans (GAGs) through the controlled hydrolysis of tub gurnard skin proteins. Four proteases (Esperase, Alcalase, Trypsin and Pronase E) were used to obtain potent angiotensin converting enzyme I (ACE)-inhibitory hydrolysates. Peptides and GAGs were separated and evaluated for their antihypertensive potential by fluorometry. The peptide-rich fractions derived from the Esperase and Alcalase hydrolysates showed very low IC50 values (47 and 68 μg/mL, respectively). Only the GAGs from the Trypsin and Esperase hydrolysates were relevant ACE inhibitors (63 and 52% at 1 mg/mL, respectively). The peptide composition of the most potent ACE-inhibitory fractions derived from the Esperase and Alcalase hydrolysates (IC50 values of 33 and 29 μg/mL, respectively) was analysed by RP-LC-ESI-MS/MS. The analysis suggests that the ACE-inhibitory activity is related to the peptide hydrophobicity, as well as to the presence of specific residues at any of the last four C-terminal positions. The in silico gastrointestinal digestion of these fractions yielded small peptides with antihypertensive potential.This work was funded by MCIN/AEI/10.13039/501100011033 (grant ref. PID2020-116142RB-I00), and by the Spanish National Research Council (CSIC) under the i-COOP+ programme (ref. COOPA20192). The proteomic analysis was performed in the Proteomics Unit of the Complutense University of Madrid, a member of ProteoRed and is supported by grant PT17/0019, of the Strategic Plan I+D+i 2013-2016, funded by ISCIII and ERDF A way of making Europe.Peer reviewedMultidisciplinary Digital Publishing InstituteMinisterio de Ciencia, Innovación y Universidades (España)Agencia Estatal de Investigación (España)European CommissionUniversidad Complutense de MadridConsejo Superior de Investigaciones Científicas (España)Instituto de Salud Carlos IIIConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202320232023info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/334611reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2020-116142RB-I00The underlying dataset has been published as supplementary material of the article in the publisher platform at DOI 10.3390/md21020131https://doi.org/10.3390/md21020131Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3346112026-05-22T06:33:51Z
dc.title.none.fl_str_mv Identification of ACE I-inhibitory peptides released by the hydrolysis of tub gurnard (Chelidonichthys lucerna) skin proteins and the impact of their in silico gastrointestinal digestion
title Identification of ACE I-inhibitory peptides released by the hydrolysis of tub gurnard (Chelidonichthys lucerna) skin proteins and the impact of their in silico gastrointestinal digestion
spellingShingle Identification of ACE I-inhibitory peptides released by the hydrolysis of tub gurnard (Chelidonichthys lucerna) skin proteins and the impact of their in silico gastrointestinal digestion
Bougatef, Hajer
By-catch
Protein hydrolysates
Angiotensin converting enzyme
Bioactive peptides
Upgrading
Fish skin
Tub gurnard
Functional ingredient
Chelidonichthys lucerna
title_short Identification of ACE I-inhibitory peptides released by the hydrolysis of tub gurnard (Chelidonichthys lucerna) skin proteins and the impact of their in silico gastrointestinal digestion
title_full Identification of ACE I-inhibitory peptides released by the hydrolysis of tub gurnard (Chelidonichthys lucerna) skin proteins and the impact of their in silico gastrointestinal digestion
title_fullStr Identification of ACE I-inhibitory peptides released by the hydrolysis of tub gurnard (Chelidonichthys lucerna) skin proteins and the impact of their in silico gastrointestinal digestion
title_full_unstemmed Identification of ACE I-inhibitory peptides released by the hydrolysis of tub gurnard (Chelidonichthys lucerna) skin proteins and the impact of their in silico gastrointestinal digestion
title_sort Identification of ACE I-inhibitory peptides released by the hydrolysis of tub gurnard (Chelidonichthys lucerna) skin proteins and the impact of their in silico gastrointestinal digestion
dc.creator.none.fl_str_mv Bougatef, Hajer
Vega-Fernández, Cristina de la
Sila, Assaâd
Bougatef, Ali
Martínez Álvarez, Óscar
author Bougatef, Hajer
author_facet Bougatef, Hajer
Vega-Fernández, Cristina de la
Sila, Assaâd
Bougatef, Ali
Martínez Álvarez, Óscar
author_role author
author2 Vega-Fernández, Cristina de la
Sila, Assaâd
Bougatef, Ali
Martínez Álvarez, Óscar
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia, Innovación y Universidades (España)
Agencia Estatal de Investigación (España)
European Commission
Universidad Complutense de Madrid
Consejo Superior de Investigaciones Científicas (España)
Instituto de Salud Carlos III
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv By-catch
Protein hydrolysates
Angiotensin converting enzyme
Bioactive peptides
Upgrading
Fish skin
Tub gurnard
Functional ingredient
Chelidonichthys lucerna
topic By-catch
Protein hydrolysates
Angiotensin converting enzyme
Bioactive peptides
Upgrading
Fish skin
Tub gurnard
Functional ingredient
Chelidonichthys lucerna
description This article belongs to the Special Issue Sustainable Valorization of Seafood By-Products through Recovery of Valuable Bioactive Compounds.
publishDate 2023
dc.date.none.fl_str_mv 2023
2023
2023
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/334611
url http://hdl.handle.net/10261/334611
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2020-116142RB-I00
The underlying dataset has been published as supplementary material of the article in the publisher platform at DOI 10.3390/md21020131
https://doi.org/10.3390/md21020131

dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
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repository.mail.fl_str_mv
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