Stabilizing effects of cations on lipases depend on the immobilization protocol

Autores
Fernandez Lopez, Laura; Bartolome Cabrero, Rocío; Rodríguez, María Daniela; Dos Santos, Cleiton S.; Rueda, Nazzoly; Fernandez-Lafuente, Roberto
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The effect of an additive on enzyme stability used to be considered an intrinsic feature of a lipase. However, in this paper we have found that the effect of additive on enzyme stability depends on the immobilization protocol. After assaying the effects of diverse chloride salts with different cations on different lipases activity, no relevant effect was detected. Free enzymes or the covalently immobilized enzymes are not stabilized by these cations for any of the studied lipases. However, Mn2+ and Ca2+ (at a concentration of 5 mM) are able to greatly stabilize the lipases from Rhizomucor miehei (RML) and Candida rugosa (CRL) when they are present during the inactivation, but only if the enzymes are immobilized on octyl-agarose (stabilization factor ranging from 20 to 50). The effect was only detected when using more than 2.5 mM of the cations, and reached the maximum value at 5 mM, suggesting a saturation mechanism of action. The stabilization seemed to be based on a specific mechanism, and required the recognition sites to be saturated by the cations. Mg2+ has no effect on enzyme stability for both enzymes, but it is able to suppress the stabilization promoted by the other two cations using CRL; while it has no effect on the cation stabilization when using RML. This is the first report of a cation induced enzyme stabilization effect that depends on the lipase immobilization protocol.
Fil: Fernandez Lopez, Laura. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
Fil: Bartolome Cabrero, Rocío. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
Fil: Rodríguez, María Daniela. Universidad Nacional de Misiones. Facultad de Cs.exactas Quimicas y Naturales. Departamento de Bioquimica Clinica. Laboratorio de Biotecnologia Molecular; Argentina. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Dos Santos, Cleiton S.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidade Estadual Do Ceara; Brasil
Fil: Rueda, Nazzoly. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidad Industrial Santander; Colombia
Fil: Fernandez-Lafuente, Roberto. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
Materia
Cations
Lipases
Inmobilization
Stabilty
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/37568
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/37568
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Stabilizing effects of cations on lipases depend on the immobilization protocolFernandez Lopez, LauraBartolome Cabrero, RocíoRodríguez, María DanielaDos Santos, Cleiton S.Rueda, NazzolyFernandez-Lafuente, RobertoCationsLipasesInmobilizationStabiltyhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2The effect of an additive on enzyme stability used to be considered an intrinsic feature of a lipase. However, in this paper we have found that the effect of additive on enzyme stability depends on the immobilization protocol. After assaying the effects of diverse chloride salts with different cations on different lipases activity, no relevant effect was detected. Free enzymes or the covalently immobilized enzymes are not stabilized by these cations for any of the studied lipases. However, Mn2+ and Ca2+ (at a concentration of 5 mM) are able to greatly stabilize the lipases from Rhizomucor miehei (RML) and Candida rugosa (CRL) when they are present during the inactivation, but only if the enzymes are immobilized on octyl-agarose (stabilization factor ranging from 20 to 50). The effect was only detected when using more than 2.5 mM of the cations, and reached the maximum value at 5 mM, suggesting a saturation mechanism of action. The stabilization seemed to be based on a specific mechanism, and required the recognition sites to be saturated by the cations. Mg2+ has no effect on enzyme stability for both enzymes, but it is able to suppress the stabilization promoted by the other two cations using CRL; while it has no effect on the cation stabilization when using RML. This is the first report of a cation induced enzyme stabilization effect that depends on the lipase immobilization protocol.Fil: Fernandez Lopez, Laura. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; EspañaFil: Bartolome Cabrero, Rocío. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; EspañaFil: Rodríguez, María Daniela. Universidad Nacional de Misiones. Facultad de Cs.exactas Quimicas y Naturales. Departamento de Bioquimica Clinica. Laboratorio de Biotecnologia Molecular; Argentina. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Dos Santos, Cleiton S.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidade Estadual Do Ceara; BrasilFil: Rueda, Nazzoly. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidad Industrial Santander; ColombiaFil: Fernandez-Lafuente, Roberto. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; EspañaRoyal Society of Chemistry2015-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/37568Fernandez Lopez, Laura; Bartolome Cabrero, Rocío; Rodríguez, María Daniela; Dos Santos, Cleiton S.; Rueda, Nazzoly; et al.; Stabilizing effects of cations on lipases depend on the immobilization protocol; Royal Society of Chemistry; RSC Advances; 5; 102; 9-2015; 83868-838752046-2069CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1039/c5ra18344hinfo:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2015/RA/C5RA18344Hinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:33:18Zoai:ri.conicet.gov.ar:11336/37568instacron: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:34982025-09-29 09:33:18.893CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Stabilizing effects of cations on lipases depend on the immobilization protocol
title Stabilizing effects of cations on lipases depend on the immobilization protocol
spellingShingle Stabilizing effects of cations on lipases depend on the immobilization protocol
Fernandez Lopez, Laura
Cations
Lipases
Inmobilization
Stabilty
title_short Stabilizing effects of cations on lipases depend on the immobilization protocol
title_full Stabilizing effects of cations on lipases depend on the immobilization protocol
title_fullStr Stabilizing effects of cations on lipases depend on the immobilization protocol
title_full_unstemmed Stabilizing effects of cations on lipases depend on the immobilization protocol
title_sort Stabilizing effects of cations on lipases depend on the immobilization protocol
dc.creator.none.fl_str_mv Fernandez Lopez, Laura
Bartolome Cabrero, Rocío
Rodríguez, María Daniela
Dos Santos, Cleiton S.
Rueda, Nazzoly
Fernandez-Lafuente, Roberto
author Fernandez Lopez, Laura
author_facet Fernandez Lopez, Laura
Bartolome Cabrero, Rocío
Rodríguez, María Daniela
Dos Santos, Cleiton S.
Rueda, Nazzoly
Fernandez-Lafuente, Roberto
author_role author
author2 Bartolome Cabrero, Rocío
Rodríguez, María Daniela
Dos Santos, Cleiton S.
Rueda, Nazzoly
Fernandez-Lafuente, Roberto
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Cations
Lipases
Inmobilization
Stabilty
topic Cations
Lipases
Inmobilization
Stabilty
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The effect of an additive on enzyme stability used to be considered an intrinsic feature of a lipase. However, in this paper we have found that the effect of additive on enzyme stability depends on the immobilization protocol. After assaying the effects of diverse chloride salts with different cations on different lipases activity, no relevant effect was detected. Free enzymes or the covalently immobilized enzymes are not stabilized by these cations for any of the studied lipases. However, Mn2+ and Ca2+ (at a concentration of 5 mM) are able to greatly stabilize the lipases from Rhizomucor miehei (RML) and Candida rugosa (CRL) when they are present during the inactivation, but only if the enzymes are immobilized on octyl-agarose (stabilization factor ranging from 20 to 50). The effect was only detected when using more than 2.5 mM of the cations, and reached the maximum value at 5 mM, suggesting a saturation mechanism of action. The stabilization seemed to be based on a specific mechanism, and required the recognition sites to be saturated by the cations. Mg2+ has no effect on enzyme stability for both enzymes, but it is able to suppress the stabilization promoted by the other two cations using CRL; while it has no effect on the cation stabilization when using RML. This is the first report of a cation induced enzyme stabilization effect that depends on the lipase immobilization protocol.
Fil: Fernandez Lopez, Laura. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
Fil: Bartolome Cabrero, Rocío. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
Fil: Rodríguez, María Daniela. Universidad Nacional de Misiones. Facultad de Cs.exactas Quimicas y Naturales. Departamento de Bioquimica Clinica. Laboratorio de Biotecnologia Molecular; Argentina. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Dos Santos, Cleiton S.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidade Estadual Do Ceara; Brasil
Fil: Rueda, Nazzoly. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidad Industrial Santander; Colombia
Fil: Fernandez-Lafuente, Roberto. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
description The effect of an additive on enzyme stability used to be considered an intrinsic feature of a lipase. However, in this paper we have found that the effect of additive on enzyme stability depends on the immobilization protocol. After assaying the effects of diverse chloride salts with different cations on different lipases activity, no relevant effect was detected. Free enzymes or the covalently immobilized enzymes are not stabilized by these cations for any of the studied lipases. However, Mn2+ and Ca2+ (at a concentration of 5 mM) are able to greatly stabilize the lipases from Rhizomucor miehei (RML) and Candida rugosa (CRL) when they are present during the inactivation, but only if the enzymes are immobilized on octyl-agarose (stabilization factor ranging from 20 to 50). The effect was only detected when using more than 2.5 mM of the cations, and reached the maximum value at 5 mM, suggesting a saturation mechanism of action. The stabilization seemed to be based on a specific mechanism, and required the recognition sites to be saturated by the cations. Mg2+ has no effect on enzyme stability for both enzymes, but it is able to suppress the stabilization promoted by the other two cations using CRL; while it has no effect on the cation stabilization when using RML. This is the first report of a cation induced enzyme stabilization effect that depends on the lipase immobilization protocol.
publishDate 2015
dc.date.none.fl_str_mv 2015-09
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/11336/37568
Fernandez Lopez, Laura; Bartolome Cabrero, Rocío; Rodríguez, María Daniela; Dos Santos, Cleiton S.; Rueda, Nazzoly; et al.; Stabilizing effects of cations on lipases depend on the immobilization protocol; Royal Society of Chemistry; RSC Advances; 5; 102; 9-2015; 83868-83875
2046-2069
CONICET Digital
CONICET
url http://hdl.handle.net/11336/37568
identifier_str_mv Fernandez Lopez, Laura; Bartolome Cabrero, Rocío; Rodríguez, María Daniela; Dos Santos, Cleiton S.; Rueda, Nazzoly; et al.; Stabilizing effects of cations on lipases depend on the immobilization protocol; Royal Society of Chemistry; RSC Advances; 5; 102; 9-2015; 83868-83875
2046-2069
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1039/c5ra18344h
info:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2015/RA/C5RA18344H
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Royal Society of Chemistry
publisher.none.fl_str_mv Royal Society of Chemistry
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
_version_ 1844613022245453824
score 13.070432

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