Reversible immobilization of lipases on octyl-glutamic agarose beads: a mixed adsorption that reinforces enzyme immobilization

Autores
Rueda, Nazzoly; Dos Santos, Cleiton S.; Rodríguez, María Daniela; Albuquerque, Tiago L.; Barbosa, Oveimar; Torres, Rodrigo; Ortiz, Claudia; Fernandez Lafuente, Roberto
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A new octyl-glutamic(OCGLU) heterofunctional agarose bead has been prepared. It has been compared to octyl-agarose (OC) in their performance to immobilize 5 different lipases, those from Candida antarctica (A (CALA) and B (CALB)), from Thermomyces lanuginosus (TLL), from Rhizomucor miehei (RML) and from Candida rugosa (CRL) and a phospholipase (Lecitase ultra, LU). The immobilization rate was very similar using both supports, and the increase of activity versus p-nitrophenyl butyrate were also very similar. The effects on enzyme stability of the immobilization on OCGLU compared to the conventional OC was quite diverse, in some cases reducing the enzyme stability while in other examples the enzyme stability improved more than hundredfold. Curiously, the highest stabilizations were found under pH conditions where the free enzyme could not be adsorbed on a support just bearing glutamic groups on its surface, suggesting that the mechanism of stabilization may be a quite complex one that should consider the hydrophilization of the support surface, the cationic and anionic groups of glutamic, the likely partition of organic solvents from the support surface, positive and negative enzyme-support interactions, etc. Even though the lipases adsorption was very strong, the support could be regenerated and reused by incubation in ionic detergents.
Fil: Rueda, Nazzoly. Universidad Industrial Santander; Colombia. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
Fil: Dos Santos, Cleiton S.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidade Federal do Ceará; Brasil
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
Fil: Albuquerque, Tiago L.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidade Federal do Ceará; Brasil
Fil: Barbosa, Oveimar. Universidad del Tolima. Facultad de Ciencias Exactas. Departamento de Química; Colombia
Fil: Torres, Rodrigo. Universidad Industrial Santander; Colombia
Fil: Ortiz, Claudia. Universidad Industrial Santander; Colombia
Fil: Fernandez Lafuente, Roberto. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
Materia
Enzyme Stabilization
Heterofunctional Supports
Ion Exchange
Lipase Interfacial Activation
Prevention of Enzyme Leakage
Reversible Immobilization
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:11336/39050
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/39050
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Reversible immobilization of lipases on octyl-glutamic agarose beads: a mixed adsorption that reinforces enzyme immobilizationRueda, NazzolyDos Santos, Cleiton S.Rodríguez, María DanielaAlbuquerque, Tiago L.Barbosa, OveimarTorres, RodrigoOrtiz, ClaudiaFernandez Lafuente, RobertoEnzyme StabilizationHeterofunctional SupportsIon ExchangeLipase Interfacial ActivationPrevention of Enzyme LeakageReversible Immobilizationhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2A new octyl-glutamic(OCGLU) heterofunctional agarose bead has been prepared. It has been compared to octyl-agarose (OC) in their performance to immobilize 5 different lipases, those from Candida antarctica (A (CALA) and B (CALB)), from Thermomyces lanuginosus (TLL), from Rhizomucor miehei (RML) and from Candida rugosa (CRL) and a phospholipase (Lecitase ultra, LU). The immobilization rate was very similar using both supports, and the increase of activity versus p-nitrophenyl butyrate were also very similar. The effects on enzyme stability of the immobilization on OCGLU compared to the conventional OC was quite diverse, in some cases reducing the enzyme stability while in other examples the enzyme stability improved more than hundredfold. Curiously, the highest stabilizations were found under pH conditions where the free enzyme could not be adsorbed on a support just bearing glutamic groups on its surface, suggesting that the mechanism of stabilization may be a quite complex one that should consider the hydrophilization of the support surface, the cationic and anionic groups of glutamic, the likely partition of organic solvents from the support surface, positive and negative enzyme-support interactions, etc. Even though the lipases adsorption was very strong, the support could be regenerated and reused by incubation in ionic detergents.Fil: Rueda, Nazzoly. Universidad Industrial Santander; Colombia. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; EspañaFil: Dos Santos, Cleiton S.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidade Federal do Ceará; BrasilFil: 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; EspañaFil: Albuquerque, Tiago L.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidade Federal do Ceará; BrasilFil: Barbosa, Oveimar. Universidad del Tolima. Facultad de Ciencias Exactas. Departamento de Química; ColombiaFil: Torres, Rodrigo. Universidad Industrial Santander; ColombiaFil: Ortiz, Claudia. Universidad Industrial Santander; ColombiaFil: Fernandez Lafuente, Roberto. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; EspañaElsevier Science2016-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/39050Rueda, Nazzoly; Dos Santos, Cleiton S.; Rodríguez, María Daniela; Albuquerque, Tiago L.; Barbosa, Oveimar; et al.; Reversible immobilization of lipases on octyl-glutamic agarose beads: a mixed adsorption that reinforces enzyme immobilization; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 128; 9-2016; 10-181381-11771873-3158CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1381117716300327info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2016.03.002info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:09:03Zoai:ri.conicet.gov.ar:11336/39050instacron: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:34982025-10-22 11:09:03.932CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Reversible immobilization of lipases on octyl-glutamic agarose beads: a mixed adsorption that reinforces enzyme immobilization
title Reversible immobilization of lipases on octyl-glutamic agarose beads: a mixed adsorption that reinforces enzyme immobilization
spellingShingle Reversible immobilization of lipases on octyl-glutamic agarose beads: a mixed adsorption that reinforces enzyme immobilization
Rueda, Nazzoly
Enzyme Stabilization
Heterofunctional Supports
Ion Exchange
Lipase Interfacial Activation
Prevention of Enzyme Leakage
Reversible Immobilization
title_short Reversible immobilization of lipases on octyl-glutamic agarose beads: a mixed adsorption that reinforces enzyme immobilization
title_full Reversible immobilization of lipases on octyl-glutamic agarose beads: a mixed adsorption that reinforces enzyme immobilization
title_fullStr Reversible immobilization of lipases on octyl-glutamic agarose beads: a mixed adsorption that reinforces enzyme immobilization
title_full_unstemmed Reversible immobilization of lipases on octyl-glutamic agarose beads: a mixed adsorption that reinforces enzyme immobilization
title_sort Reversible immobilization of lipases on octyl-glutamic agarose beads: a mixed adsorption that reinforces enzyme immobilization
dc.creator.none.fl_str_mv Rueda, Nazzoly
Dos Santos, Cleiton S.
Rodríguez, María Daniela
Albuquerque, Tiago L.
Barbosa, Oveimar
Torres, Rodrigo
Ortiz, Claudia
Fernandez Lafuente, Roberto
author Rueda, Nazzoly
author_facet Rueda, Nazzoly
Dos Santos, Cleiton S.
Rodríguez, María Daniela
Albuquerque, Tiago L.
Barbosa, Oveimar
Torres, Rodrigo
Ortiz, Claudia
Fernandez Lafuente, Roberto
author_role author
author2 Dos Santos, Cleiton S.
Rodríguez, María Daniela
Albuquerque, Tiago L.
Barbosa, Oveimar
Torres, Rodrigo
Ortiz, Claudia
Fernandez Lafuente, Roberto
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Enzyme Stabilization
Heterofunctional Supports
Ion Exchange
Lipase Interfacial Activation
Prevention of Enzyme Leakage
Reversible Immobilization
topic Enzyme Stabilization
Heterofunctional Supports
Ion Exchange
Lipase Interfacial Activation
Prevention of Enzyme Leakage
Reversible Immobilization
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv A new octyl-glutamic(OCGLU) heterofunctional agarose bead has been prepared. It has been compared to octyl-agarose (OC) in their performance to immobilize 5 different lipases, those from Candida antarctica (A (CALA) and B (CALB)), from Thermomyces lanuginosus (TLL), from Rhizomucor miehei (RML) and from Candida rugosa (CRL) and a phospholipase (Lecitase ultra, LU). The immobilization rate was very similar using both supports, and the increase of activity versus p-nitrophenyl butyrate were also very similar. The effects on enzyme stability of the immobilization on OCGLU compared to the conventional OC was quite diverse, in some cases reducing the enzyme stability while in other examples the enzyme stability improved more than hundredfold. Curiously, the highest stabilizations were found under pH conditions where the free enzyme could not be adsorbed on a support just bearing glutamic groups on its surface, suggesting that the mechanism of stabilization may be a quite complex one that should consider the hydrophilization of the support surface, the cationic and anionic groups of glutamic, the likely partition of organic solvents from the support surface, positive and negative enzyme-support interactions, etc. Even though the lipases adsorption was very strong, the support could be regenerated and reused by incubation in ionic detergents.
Fil: Rueda, Nazzoly. Universidad Industrial Santander; Colombia. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
Fil: Dos Santos, Cleiton S.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidade Federal do Ceará; Brasil
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
Fil: Albuquerque, Tiago L.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidade Federal do Ceará; Brasil
Fil: Barbosa, Oveimar. Universidad del Tolima. Facultad de Ciencias Exactas. Departamento de Química; Colombia
Fil: Torres, Rodrigo. Universidad Industrial Santander; Colombia
Fil: Ortiz, Claudia. Universidad Industrial Santander; Colombia
Fil: Fernandez Lafuente, Roberto. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
description A new octyl-glutamic(OCGLU) heterofunctional agarose bead has been prepared. It has been compared to octyl-agarose (OC) in their performance to immobilize 5 different lipases, those from Candida antarctica (A (CALA) and B (CALB)), from Thermomyces lanuginosus (TLL), from Rhizomucor miehei (RML) and from Candida rugosa (CRL) and a phospholipase (Lecitase ultra, LU). The immobilization rate was very similar using both supports, and the increase of activity versus p-nitrophenyl butyrate were also very similar. The effects on enzyme stability of the immobilization on OCGLU compared to the conventional OC was quite diverse, in some cases reducing the enzyme stability while in other examples the enzyme stability improved more than hundredfold. Curiously, the highest stabilizations were found under pH conditions where the free enzyme could not be adsorbed on a support just bearing glutamic groups on its surface, suggesting that the mechanism of stabilization may be a quite complex one that should consider the hydrophilization of the support surface, the cationic and anionic groups of glutamic, the likely partition of organic solvents from the support surface, positive and negative enzyme-support interactions, etc. Even though the lipases adsorption was very strong, the support could be regenerated and reused by incubation in ionic detergents.
publishDate 2016
dc.date.none.fl_str_mv 2016-09
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/11336/39050
Rueda, Nazzoly; Dos Santos, Cleiton S.; Rodríguez, María Daniela; Albuquerque, Tiago L.; Barbosa, Oveimar; et al.; Reversible immobilization of lipases on octyl-glutamic agarose beads: a mixed adsorption that reinforces enzyme immobilization; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 128; 9-2016; 10-18
1381-1177
1873-3158
CONICET Digital
CONICET
url http://hdl.handle.net/11336/39050
identifier_str_mv Rueda, Nazzoly; Dos Santos, Cleiton S.; Rodríguez, María Daniela; Albuquerque, Tiago L.; Barbosa, Oveimar; et al.; Reversible immobilization of lipases on octyl-glutamic agarose beads: a mixed adsorption that reinforces enzyme immobilization; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 128; 9-2016; 10-18
1381-1177
1873-3158
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1381117716300327
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2016.03.002
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 Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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_ 1846781429594193920
score 12.982451

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