Upgrading collagenous smooth hound by-products: Effect of hydrolysis conditions, in vitro gastrointestinal digestion and encapsulation on bioactive properties

Collagenous by-products derived from smooth hound (Mustelus mustelus) were studied using trypsin hydrolysis to obtain protein hydrolysates with ACE (angiotensin converting enzyme) and/or PEP (prolyl endopeptidase)-inhibitory activities. Most of the hydrolysates were mainly composed of short peptides...

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Detalles Bibliográficos
Autores: Lajmi, Khouloud, Gómez Estaca, Joaquín, Hammamia, Mohamed, Martínez Álvarez, Óscar
Tipo de recurso: artículo
Estado:Versión enviada para evaluación y publicación
Fecha de publicación:2019
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/178379
Acceso en línea:http://hdl.handle.net/10261/178379
Access Level:acceso abierto
Palabra clave:Protein Hydrolysates
Prolyl endopeptidase-inhibitory activity
ACE-inhibitory activity
Response surface methodology
Trypsin
Encapsulation
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spelling Upgrading collagenous smooth hound by-products: Effect of hydrolysis conditions, in vitro gastrointestinal digestion and encapsulation on bioactive propertiesLajmi, KhouloudGómez Estaca, JoaquínHammamia, MohamedMartínez Álvarez, ÓscarProtein HydrolysatesProlyl endopeptidase-inhibitory activityACE-inhibitory activityResponse surface methodologyTrypsinEncapsulationCollagenous by-products derived from smooth hound (Mustelus mustelus) were studied using trypsin hydrolysis to obtain protein hydrolysates with ACE (angiotensin converting enzyme) and/or PEP (prolyl endopeptidase)-inhibitory activities. Most of the hydrolysates were mainly composed of short peptides. A response surface methodology (RSM) was used to optimize the conditions of hydrolysis (pH 7, 8 or 9, and temperatures of 35, 45 or 55ºC), which led to a higher degree of hydrolysis (DH=3.4%), as well as to an increase in ACE and PEP-inhibitory activities (maximal inhibitions of 68.1 and 81.7%, respectively). According to the model used, neither hydrolysis temperature nor pH in the ranges studied had a significant effect on DH, whereas PEP-inhibitory activity was significantly affected by both factors. pH had a significant effect on ACE-inhibitory activity. Optimum conditions of hydrolysis to obtain maximum activity differed for the two activities: 35ºC/pH 7 for PEP-inhibitory activity and 45.9ºC/pH 9 for ACE-inhibitory activity. The results suggested that these biological activities were influenced by peptide sequence rather than peptide length. This was also confirmed by the amino acid composition and molecular weight (MW) profiles. The ACE-inhibitory activity of the most potent hydrolysate was evaluated after in vitro gastrointestinal digestion. The results showed a worsening of the activity, which was related to small peptide losses and to the appearance of new low MW peptides.Hydrolysate encapsulation using an alginate-whey protein isolate microsphere improved the ACE-inhibitory activity (IC50=0.24 mg/ml).This research was financed by the Spanish Ministry of Economy and Competitiveness project with reference AGL2014-52825-R, and co-funded with European Union ERDF funds (European Regional Development Fund)). Author Lajmi Khouloud was funded by the Ministry of Higher Education and Scientific Research of Tunisia.Peer reviewedElsevierMinisterio de Economía, Industria y Competitividad (España)European CommissionConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201920192019info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Preprintinfo:eu-repo/semantics/submittedVersionhttp://hdl.handle.net/10261/178379reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/AGL2014-52825-Rhttps://doi.org/10.1016/j.fbio.2019.01.014Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1783792026-05-22T06:33:51Z
dc.title.none.fl_str_mv Upgrading collagenous smooth hound by-products: Effect of hydrolysis conditions, in vitro gastrointestinal digestion and encapsulation on bioactive properties
title Upgrading collagenous smooth hound by-products: Effect of hydrolysis conditions, in vitro gastrointestinal digestion and encapsulation on bioactive properties
spellingShingle Upgrading collagenous smooth hound by-products: Effect of hydrolysis conditions, in vitro gastrointestinal digestion and encapsulation on bioactive properties
Lajmi, Khouloud
Protein Hydrolysates
Prolyl endopeptidase-inhibitory activity
ACE-inhibitory activity
Response surface methodology
Trypsin
Encapsulation
title_short Upgrading collagenous smooth hound by-products: Effect of hydrolysis conditions, in vitro gastrointestinal digestion and encapsulation on bioactive properties
title_full Upgrading collagenous smooth hound by-products: Effect of hydrolysis conditions, in vitro gastrointestinal digestion and encapsulation on bioactive properties
title_fullStr Upgrading collagenous smooth hound by-products: Effect of hydrolysis conditions, in vitro gastrointestinal digestion and encapsulation on bioactive properties
title_full_unstemmed Upgrading collagenous smooth hound by-products: Effect of hydrolysis conditions, in vitro gastrointestinal digestion and encapsulation on bioactive properties
title_sort Upgrading collagenous smooth hound by-products: Effect of hydrolysis conditions, in vitro gastrointestinal digestion and encapsulation on bioactive properties
dc.creator.none.fl_str_mv Lajmi, Khouloud
Gómez Estaca, Joaquín
Hammamia, Mohamed
Martínez Álvarez, Óscar
author Lajmi, Khouloud
author_facet Lajmi, Khouloud
Gómez Estaca, Joaquín
Hammamia, Mohamed
Martínez Álvarez, Óscar
author_role author
author2 Gómez Estaca, Joaquín
Hammamia, Mohamed
Martínez Álvarez, Óscar
author2_role author
author
author
dc.contributor.none.fl_str_mv Ministerio de Economía, Industria y Competitividad (España)
European Commission
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Protein Hydrolysates
Prolyl endopeptidase-inhibitory activity
ACE-inhibitory activity
Response surface methodology
Trypsin
Encapsulation
topic Protein Hydrolysates
Prolyl endopeptidase-inhibitory activity
ACE-inhibitory activity
Response surface methodology
Trypsin
Encapsulation
description Collagenous by-products derived from smooth hound (Mustelus mustelus) were studied using trypsin hydrolysis to obtain protein hydrolysates with ACE (angiotensin converting enzyme) and/or PEP (prolyl endopeptidase)-inhibitory activities. Most of the hydrolysates were mainly composed of short peptides. A response surface methodology (RSM) was used to optimize the conditions of hydrolysis (pH 7, 8 or 9, and temperatures of 35, 45 or 55ºC), which led to a higher degree of hydrolysis (DH=3.4%), as well as to an increase in ACE and PEP-inhibitory activities (maximal inhibitions of 68.1 and 81.7%, respectively). According to the model used, neither hydrolysis temperature nor pH in the ranges studied had a significant effect on DH, whereas PEP-inhibitory activity was significantly affected by both factors. pH had a significant effect on ACE-inhibitory activity. Optimum conditions of hydrolysis to obtain maximum activity differed for the two activities: 35ºC/pH 7 for PEP-inhibitory activity and 45.9ºC/pH 9 for ACE-inhibitory activity. The results suggested that these biological activities were influenced by peptide sequence rather than peptide length. This was also confirmed by the amino acid composition and molecular weight (MW) profiles. The ACE-inhibitory activity of the most potent hydrolysate was evaluated after in vitro gastrointestinal digestion. The results showed a worsening of the activity, which was related to small peptide losses and to the appearance of new low MW peptides.Hydrolysate encapsulation using an alginate-whey protein isolate microsphere improved the ACE-inhibitory activity (IC50=0.24 mg/ml).
publishDate 2019
dc.date.none.fl_str_mv 2019
2019
2019
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Preprint
info:eu-repo/semantics/submittedVersion
format article
status_str submittedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/178379
url http://hdl.handle.net/10261/178379
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/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/AGL2014-52825-R
https://doi.org/10.1016/j.fbio.2019.01.014
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,812429

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