Production of fish protein hydrolysates from scyliorhinus canicula discards with antihypertensive & antioxidant activities by enzymatic hydrolysis & mathematical optimization using...

Autores
Vázquez, José A.; Blanco, Maria; Massa, Agueda Elena; Amado, Isabel Rodríguez; Pérez Martín, Ricardo I.
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fish discards are of major concern in new EU policies. Alternatives for the management of the new biomass that has to be landed is compulsory. The production of bioactive compounds from fish protein hydrolysates (FPH) has been explored in recent years. However, the viability of Scyliorhinus canicula discards, which might account for up to 90-100% of captures in mixed trawler, gillnet, and longline industrial fisheries, to produce FPH from the muscle with bioactivities has still not been studied in terms of the optimization of the experimental conditions to enhance its production. The effect of pH and temperature on the hydrolysis of the S. canicula muscle was mediated by three commercial proteases using response surface methodology. Temperatures of 64.6 °C and 60.8°C and pHs of 9.40 and 8.90 were established as the best hydrolysis conditions for Alcalase and Esperase, respectively. Optimization of the best conditions for the maximization of antihypertensive and antioxidant activities was performed. Higher Angiotensin-converting enzyme (ACE) activity was found with Esperase. The pH optimum and temperature optimum for antioxidants were 55 ° C/pH8.0 for ABTS/DPPH-Esperase, 63.1 ° C/pH9.0 for DPPH-Alcalase, and 55° C/pH9.0 for ABTS-Alcalase. No hydrolysis was detected when using Protamex.
Fil: Vázquez, José A.. Consejo Superior de Investigaciones Científicas; España
Fil: Blanco, Maria. Consejo Superior de Investigaciones Científicas; España
Fil: Massa, Agueda Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Subsede Instituto Nacional de Investigación y Desarrollo Pesquero; Argentina
Fil: Amado, Isabel Rodríguez. Universidad de Vigo; España
Fil: Pérez Martín, Ricardo I.. Consejo Superior de Investigaciones Científicas; España
Materia
ANTIHYPERTENSIVE ACTIVITY
ANTIOXIDANT ACTIVITY
COMMON FISHERY POLICY
ENZYME HYDROLYSIS
FISH DISCARDS
FISH PROTEIN HYDROLYSATES
RESPONSE SURFACE METHODOLOGY
SCYLIORHINUS CANICULA MUSCLE BY-PRODUCTS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/55459
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/55459
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Production of fish protein hydrolysates from scyliorhinus canicula discards with antihypertensive & antioxidant activities by enzymatic hydrolysis & mathematical optimization using response surface methodologyVázquez, José A.Blanco, MariaMassa, Agueda ElenaAmado, Isabel RodríguezPérez Martín, Ricardo I.ANTIHYPERTENSIVE ACTIVITYANTIOXIDANT ACTIVITYCOMMON FISHERY POLICYENZYME HYDROLYSISFISH DISCARDSFISH PROTEIN HYDROLYSATESRESPONSE SURFACE METHODOLOGYSCYLIORHINUS CANICULA MUSCLE BY-PRODUCTShttps://purl.org/becyt/ford/4.1https://purl.org/becyt/ford/4Fish discards are of major concern in new EU policies. Alternatives for the management of the new biomass that has to be landed is compulsory. The production of bioactive compounds from fish protein hydrolysates (FPH) has been explored in recent years. However, the viability of Scyliorhinus canicula discards, which might account for up to 90-100% of captures in mixed trawler, gillnet, and longline industrial fisheries, to produce FPH from the muscle with bioactivities has still not been studied in terms of the optimization of the experimental conditions to enhance its production. The effect of pH and temperature on the hydrolysis of the S. canicula muscle was mediated by three commercial proteases using response surface methodology. Temperatures of 64.6 °C and 60.8°C and pHs of 9.40 and 8.90 were established as the best hydrolysis conditions for Alcalase and Esperase, respectively. Optimization of the best conditions for the maximization of antihypertensive and antioxidant activities was performed. Higher Angiotensin-converting enzyme (ACE) activity was found with Esperase. The pH optimum and temperature optimum for antioxidants were 55 ° C/pH8.0 for ABTS/DPPH-Esperase, 63.1 ° C/pH9.0 for DPPH-Alcalase, and 55° C/pH9.0 for ABTS-Alcalase. No hydrolysis was detected when using Protamex.Fil: Vázquez, José A.. Consejo Superior de Investigaciones Científicas; EspañaFil: Blanco, Maria. Consejo Superior de Investigaciones Científicas; EspañaFil: Massa, Agueda Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Subsede Instituto Nacional de Investigación y Desarrollo Pesquero; ArgentinaFil: Amado, Isabel Rodríguez. Universidad de Vigo; EspañaFil: Pérez Martín, Ricardo I.. Consejo Superior de Investigaciones Científicas; EspañaMolecular Diversity Preservation International2017-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/55459Vázquez, José A.; Blanco, Maria; Massa, Agueda Elena; Amado, Isabel Rodríguez; Pérez Martín, Ricardo I.; Production of fish protein hydrolysates from scyliorhinus canicula discards with antihypertensive & antioxidant activities by enzymatic hydrolysis & mathematical optimization using response surface methodology; Molecular Diversity Preservation International; Marine Drugs; 15; 10; 10-20171660-3397CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3390/md15100306info:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/1660-3397/15/10/306info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-08-25T15:06:28Zoai:ri.conicet.gov.ar:11336/55459instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982026-08-25 15:06:28.893CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Production of fish protein hydrolysates from scyliorhinus canicula discards with antihypertensive & antioxidant activities by enzymatic hydrolysis & mathematical optimization using response surface methodology
title Production of fish protein hydrolysates from scyliorhinus canicula discards with antihypertensive & antioxidant activities by enzymatic hydrolysis & mathematical optimization using response surface methodology
spellingShingle Production of fish protein hydrolysates from scyliorhinus canicula discards with antihypertensive & antioxidant activities by enzymatic hydrolysis & mathematical optimization using response surface methodology
Vázquez, José A.
ANTIHYPERTENSIVE ACTIVITY
ANTIOXIDANT ACTIVITY
COMMON FISHERY POLICY
ENZYME HYDROLYSIS
FISH DISCARDS
FISH PROTEIN HYDROLYSATES
RESPONSE SURFACE METHODOLOGY
SCYLIORHINUS CANICULA MUSCLE BY-PRODUCTS
title_short Production of fish protein hydrolysates from scyliorhinus canicula discards with antihypertensive & antioxidant activities by enzymatic hydrolysis & mathematical optimization using response surface methodology
title_full Production of fish protein hydrolysates from scyliorhinus canicula discards with antihypertensive & antioxidant activities by enzymatic hydrolysis & mathematical optimization using response surface methodology
title_fullStr Production of fish protein hydrolysates from scyliorhinus canicula discards with antihypertensive & antioxidant activities by enzymatic hydrolysis & mathematical optimization using response surface methodology
title_full_unstemmed Production of fish protein hydrolysates from scyliorhinus canicula discards with antihypertensive & antioxidant activities by enzymatic hydrolysis & mathematical optimization using response surface methodology
title_sort Production of fish protein hydrolysates from scyliorhinus canicula discards with antihypertensive & antioxidant activities by enzymatic hydrolysis & mathematical optimization using response surface methodology
dc.creator.none.fl_str_mv Vázquez, José A.
Blanco, Maria
Massa, Agueda Elena
Amado, Isabel Rodríguez
Pérez Martín, Ricardo I.
author Vázquez, José A.
author_facet Vázquez, José A.
Blanco, Maria
Massa, Agueda Elena
Amado, Isabel Rodríguez
Pérez Martín, Ricardo I.
author_role author
author2 Blanco, Maria
Massa, Agueda Elena
Amado, Isabel Rodríguez
Pérez Martín, Ricardo I.
author2_role author
author
author
author
dc.subject.none.fl_str_mv ANTIHYPERTENSIVE ACTIVITY
ANTIOXIDANT ACTIVITY
COMMON FISHERY POLICY
ENZYME HYDROLYSIS
FISH DISCARDS
FISH PROTEIN HYDROLYSATES
RESPONSE SURFACE METHODOLOGY
SCYLIORHINUS CANICULA MUSCLE BY-PRODUCTS
topic ANTIHYPERTENSIVE ACTIVITY
ANTIOXIDANT ACTIVITY
COMMON FISHERY POLICY
ENZYME HYDROLYSIS
FISH DISCARDS
FISH PROTEIN HYDROLYSATES
RESPONSE SURFACE METHODOLOGY
SCYLIORHINUS CANICULA MUSCLE BY-PRODUCTS
purl_subject.fl_str_mv https://purl.org/becyt/ford/4.1
https://purl.org/becyt/ford/4
dc.description.none.fl_txt_mv Fish discards are of major concern in new EU policies. Alternatives for the management of the new biomass that has to be landed is compulsory. The production of bioactive compounds from fish protein hydrolysates (FPH) has been explored in recent years. However, the viability of Scyliorhinus canicula discards, which might account for up to 90-100% of captures in mixed trawler, gillnet, and longline industrial fisheries, to produce FPH from the muscle with bioactivities has still not been studied in terms of the optimization of the experimental conditions to enhance its production. The effect of pH and temperature on the hydrolysis of the S. canicula muscle was mediated by three commercial proteases using response surface methodology. Temperatures of 64.6 °C and 60.8°C and pHs of 9.40 and 8.90 were established as the best hydrolysis conditions for Alcalase and Esperase, respectively. Optimization of the best conditions for the maximization of antihypertensive and antioxidant activities was performed. Higher Angiotensin-converting enzyme (ACE) activity was found with Esperase. The pH optimum and temperature optimum for antioxidants were 55 ° C/pH8.0 for ABTS/DPPH-Esperase, 63.1 ° C/pH9.0 for DPPH-Alcalase, and 55° C/pH9.0 for ABTS-Alcalase. No hydrolysis was detected when using Protamex.
Fil: Vázquez, José A.. Consejo Superior de Investigaciones Científicas; España
Fil: Blanco, Maria. Consejo Superior de Investigaciones Científicas; España
Fil: Massa, Agueda Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Subsede Instituto Nacional de Investigación y Desarrollo Pesquero; Argentina
Fil: Amado, Isabel Rodríguez. Universidad de Vigo; España
Fil: Pérez Martín, Ricardo I.. Consejo Superior de Investigaciones Científicas; España
description Fish discards are of major concern in new EU policies. Alternatives for the management of the new biomass that has to be landed is compulsory. The production of bioactive compounds from fish protein hydrolysates (FPH) has been explored in recent years. However, the viability of Scyliorhinus canicula discards, which might account for up to 90-100% of captures in mixed trawler, gillnet, and longline industrial fisheries, to produce FPH from the muscle with bioactivities has still not been studied in terms of the optimization of the experimental conditions to enhance its production. The effect of pH and temperature on the hydrolysis of the S. canicula muscle was mediated by three commercial proteases using response surface methodology. Temperatures of 64.6 °C and 60.8°C and pHs of 9.40 and 8.90 were established as the best hydrolysis conditions for Alcalase and Esperase, respectively. Optimization of the best conditions for the maximization of antihypertensive and antioxidant activities was performed. Higher Angiotensin-converting enzyme (ACE) activity was found with Esperase. The pH optimum and temperature optimum for antioxidants were 55 ° C/pH8.0 for ABTS/DPPH-Esperase, 63.1 ° C/pH9.0 for DPPH-Alcalase, and 55° C/pH9.0 for ABTS-Alcalase. No hydrolysis was detected when using Protamex.
publishDate 2017
dc.date.none.fl_str_mv 2017-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/55459
Vázquez, José A.; Blanco, Maria; Massa, Agueda Elena; Amado, Isabel Rodríguez; Pérez Martín, Ricardo I.; Production of fish protein hydrolysates from scyliorhinus canicula discards with antihypertensive & antioxidant activities by enzymatic hydrolysis & mathematical optimization using response surface methodology; Molecular Diversity Preservation International; Marine Drugs; 15; 10; 10-2017
1660-3397
CONICET Digital
CONICET
url http://hdl.handle.net/11336/55459
identifier_str_mv Vázquez, José A.; Blanco, Maria; Massa, Agueda Elena; Amado, Isabel Rodríguez; Pérez Martín, Ricardo I.; Production of fish protein hydrolysates from scyliorhinus canicula discards with antihypertensive & antioxidant activities by enzymatic hydrolysis & mathematical optimization using response surface methodology; Molecular Diversity Preservation International; Marine Drugs; 15; 10; 10-2017
1660-3397
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3390/md15100306
info:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/1660-3397/15/10/306
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Molecular Diversity Preservation International
publisher.none.fl_str_mv Molecular Diversity Preservation International
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.364332

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