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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/39050
Ver los metadatos del registro completo
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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 Técnicas2025-09-29T09:40:27Zoai: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:34982025-09-29 09:40:27.675CONICET 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 |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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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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1844613279694979072 |
score |
13.070432 |