Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2
- Autores
- Fernandez Lopez, Laura; Rueda, Nazoly; Bartolome Cabrero, Rocio; Rodríguez, María Daniela; Albuquerque, Tiago. L.; dos Santos, Jose C. S.; Barbosa, Oveimar; Fernandez-Lafuente, Roberto
- Año de publicación
- 2016
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- A strategy to stabilize octyl (OC)-Rhizomucor miehei lipase (RML) and OC-Candida rugosa lipase (CRL) at pH 10 is necessary to take full advantage of the immobilization of these enzymes on OC-glyoxyl (OCGLX) supports. CaCl2 and MnCl2 have been reported to stabilize OC-RM and OC-CRL at pH 5.0 and 7.0. After screening different buffers, 5 mM CaCl2 was found to be fully soluble in Gly at pH 10. OC-RML was 15 folds stabilized at this pH value by CaCl2, while OC-CRL was not. This salt was used in the preparation of octyl-glyoxyl (OCGLX)-RML, permitting to maintain almost unaltered the OC-RML activity that was 3 fold higher than that of the free. This preparation was 30% and 3 folds more stable in thermal or acetonitrile inactivations respectively than the standard OCGLX one. The stabilizing effect of CaCl2 and MnCl2 on the OCGLX preparations was studied. These salts stabilized both OCGLX-RML preparations, although the one prepared using Ca2+ during the covalent attachment was more stabilized than the standard one by the presence of Ca2+, even 7-8 folds in the presence of aceonitrile. Thus, this additive permits to recover an OCGLX-RML preparation more stable and active than the standard protocol.
Fil: Fernandez Lopez, Laura. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
Fil: Rueda, Nazoly. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidad Industrial Santander; Colombia
Fil: Bartolome Cabrero, Rocio. 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: Albuquerque, Tiago. L.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidade Federal Do Ceará. Departamento de Engenharia Química; Brasil
Fil: dos Santos, Jose C. S.. Universidade Federal Do Ceará. Departamento de Engenharia Química; Brasil. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España
Fil: Barbosa, Oveimar. Universidad del Tolima. Facultad de Ciencias Exactas. Departamento de Química; Colombia
Fil: Fernandez-Lafuente, Roberto. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España - Materia
-
Cations
Covalent Immobilization
Lipase Interfacial Activation
Lipase Stabilization
Octyl-Glyoxyl
Stabilizing Additives - 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:11336/39049
Ver los metadatos del registro completo
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oai:ri.conicet.gov.ar:11336/39049 |
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3498 |
network_name_str |
CONICET Digital (CONICET) |
spelling |
Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2Fernandez Lopez, LauraRueda, NazolyBartolome Cabrero, RocioRodríguez, María DanielaAlbuquerque, Tiago. L.dos Santos, Jose C. S.Barbosa, OveimarFernandez-Lafuente, RobertoCationsCovalent ImmobilizationLipase Interfacial ActivationLipase StabilizationOctyl-GlyoxylStabilizing Additiveshttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2A strategy to stabilize octyl (OC)-Rhizomucor miehei lipase (RML) and OC-Candida rugosa lipase (CRL) at pH 10 is necessary to take full advantage of the immobilization of these enzymes on OC-glyoxyl (OCGLX) supports. CaCl2 and MnCl2 have been reported to stabilize OC-RM and OC-CRL at pH 5.0 and 7.0. After screening different buffers, 5 mM CaCl2 was found to be fully soluble in Gly at pH 10. OC-RML was 15 folds stabilized at this pH value by CaCl2, while OC-CRL was not. This salt was used in the preparation of octyl-glyoxyl (OCGLX)-RML, permitting to maintain almost unaltered the OC-RML activity that was 3 fold higher than that of the free. This preparation was 30% and 3 folds more stable in thermal or acetonitrile inactivations respectively than the standard OCGLX one. The stabilizing effect of CaCl2 and MnCl2 on the OCGLX preparations was studied. These salts stabilized both OCGLX-RML preparations, although the one prepared using Ca2+ during the covalent attachment was more stabilized than the standard one by the presence of Ca2+, even 7-8 folds in the presence of aceonitrile. Thus, this additive permits to recover an OCGLX-RML preparation more stable and active than the standard protocol.Fil: Fernandez Lopez, Laura. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; EspañaFil: Rueda, Nazoly. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidad Industrial Santander; ColombiaFil: Bartolome Cabrero, Rocio. 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: Albuquerque, Tiago. L.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidade Federal Do Ceará. Departamento de Engenharia Química; BrasilFil: dos Santos, Jose C. S.. Universidade Federal Do Ceará. Departamento de Engenharia Química; Brasil. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; EspañaFil: Barbosa, Oveimar. Universidad del Tolima. Facultad de Ciencias Exactas. Departamento de Química; ColombiaFil: Fernandez-Lafuente, Roberto. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; EspañaElsevier2016-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/39049Fernandez Lopez, Laura; Rueda, Nazoly; Bartolome Cabrero, Rocio; Rodríguez, María Daniela; Albuquerque, Tiago. L.; et al.; Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2; Elsevier; Process Biochemistry; 51; 1; 1-2016; 48-521359-51131873-3298CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2015.11.015info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:34:47Zoai:ri.conicet.gov.ar:11336/39049instacron: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 09:34:48.058CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2 |
title |
Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2 |
spellingShingle |
Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2 Fernandez Lopez, Laura Cations Covalent Immobilization Lipase Interfacial Activation Lipase Stabilization Octyl-Glyoxyl Stabilizing Additives |
title_short |
Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2 |
title_full |
Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2 |
title_fullStr |
Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2 |
title_full_unstemmed |
Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2 |
title_sort |
Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2 |
dc.creator.none.fl_str_mv |
Fernandez Lopez, Laura Rueda, Nazoly Bartolome Cabrero, Rocio Rodríguez, María Daniela Albuquerque, Tiago. L. dos Santos, Jose C. S. Barbosa, Oveimar Fernandez-Lafuente, Roberto |
author |
Fernandez Lopez, Laura |
author_facet |
Fernandez Lopez, Laura Rueda, Nazoly Bartolome Cabrero, Rocio Rodríguez, María Daniela Albuquerque, Tiago. L. dos Santos, Jose C. S. Barbosa, Oveimar Fernandez-Lafuente, Roberto |
author_role |
author |
author2 |
Rueda, Nazoly Bartolome Cabrero, Rocio Rodríguez, María Daniela Albuquerque, Tiago. L. dos Santos, Jose C. S. Barbosa, Oveimar Fernandez-Lafuente, Roberto |
author2_role |
author author author author author author author |
dc.subject.none.fl_str_mv |
Cations Covalent Immobilization Lipase Interfacial Activation Lipase Stabilization Octyl-Glyoxyl Stabilizing Additives |
topic |
Cations Covalent Immobilization Lipase Interfacial Activation Lipase Stabilization Octyl-Glyoxyl Stabilizing Additives |
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 strategy to stabilize octyl (OC)-Rhizomucor miehei lipase (RML) and OC-Candida rugosa lipase (CRL) at pH 10 is necessary to take full advantage of the immobilization of these enzymes on OC-glyoxyl (OCGLX) supports. CaCl2 and MnCl2 have been reported to stabilize OC-RM and OC-CRL at pH 5.0 and 7.0. After screening different buffers, 5 mM CaCl2 was found to be fully soluble in Gly at pH 10. OC-RML was 15 folds stabilized at this pH value by CaCl2, while OC-CRL was not. This salt was used in the preparation of octyl-glyoxyl (OCGLX)-RML, permitting to maintain almost unaltered the OC-RML activity that was 3 fold higher than that of the free. This preparation was 30% and 3 folds more stable in thermal or acetonitrile inactivations respectively than the standard OCGLX one. The stabilizing effect of CaCl2 and MnCl2 on the OCGLX preparations was studied. These salts stabilized both OCGLX-RML preparations, although the one prepared using Ca2+ during the covalent attachment was more stabilized than the standard one by the presence of Ca2+, even 7-8 folds in the presence of aceonitrile. Thus, this additive permits to recover an OCGLX-RML preparation more stable and active than the standard protocol. Fil: Fernandez Lopez, Laura. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España Fil: Rueda, Nazoly. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidad Industrial Santander; Colombia Fil: Bartolome Cabrero, Rocio. 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: Albuquerque, Tiago. L.. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España. Universidade Federal Do Ceará. Departamento de Engenharia Química; Brasil Fil: dos Santos, Jose C. S.. Universidade Federal Do Ceará. Departamento de Engenharia Química; Brasil. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España Fil: Barbosa, Oveimar. Universidad del Tolima. Facultad de Ciencias Exactas. Departamento de Química; Colombia Fil: Fernandez-Lafuente, Roberto. Consejo Superior de Investigaciones Científicas. Instituto de Catálisis y Petroleoquímica; España |
description |
A strategy to stabilize octyl (OC)-Rhizomucor miehei lipase (RML) and OC-Candida rugosa lipase (CRL) at pH 10 is necessary to take full advantage of the immobilization of these enzymes on OC-glyoxyl (OCGLX) supports. CaCl2 and MnCl2 have been reported to stabilize OC-RM and OC-CRL at pH 5.0 and 7.0. After screening different buffers, 5 mM CaCl2 was found to be fully soluble in Gly at pH 10. OC-RML was 15 folds stabilized at this pH value by CaCl2, while OC-CRL was not. This salt was used in the preparation of octyl-glyoxyl (OCGLX)-RML, permitting to maintain almost unaltered the OC-RML activity that was 3 fold higher than that of the free. This preparation was 30% and 3 folds more stable in thermal or acetonitrile inactivations respectively than the standard OCGLX one. The stabilizing effect of CaCl2 and MnCl2 on the OCGLX preparations was studied. These salts stabilized both OCGLX-RML preparations, although the one prepared using Ca2+ during the covalent attachment was more stabilized than the standard one by the presence of Ca2+, even 7-8 folds in the presence of aceonitrile. Thus, this additive permits to recover an OCGLX-RML preparation more stable and active than the standard protocol. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-01 |
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/11336/39049 Fernandez Lopez, Laura; Rueda, Nazoly; Bartolome Cabrero, Rocio; Rodríguez, María Daniela; Albuquerque, Tiago. L.; et al.; Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2; Elsevier; Process Biochemistry; 51; 1; 1-2016; 48-52 1359-5113 1873-3298 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/39049 |
identifier_str_mv |
Fernandez Lopez, Laura; Rueda, Nazoly; Bartolome Cabrero, Rocio; Rodríguez, María Daniela; Albuquerque, Tiago. L.; et al.; Improved immobilization and stabilization of lipase from Rhizomucor miehei on octyl-glyoxyl agarose beads by using CaCl2; Elsevier; Process Biochemistry; 51; 1; 1-2016; 48-52 1359-5113 1873-3298 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2015.11.015 |
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 |
publisher.none.fl_str_mv |
Elsevier |
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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1844613078790963200 |
score |
13.070432 |