Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis

Autores
Foresti, María Laura; Alimenti, G. A.; Ferreira, María Luján
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Lipase from Candida rugosa adsorbed on polypropylene powder (CR/PP) was subjected to activation pre-treatments in order to enhance its activity in solvent-free ethyl oleate synthesis. The lipase activation achieved upon adsorption onto a hydrophobic support like PP was further enhanced through oil-water interfacial activation and bioimprinting of the immobilized catalyst. Several aliphatic hydrocarbons/buffer pH 7 mixtures were used in the pre-activation of CR/PP with specific activity increments of up to 29%. Molecular bioimprinting was also performed, with specific activity enhancement of near 70% with respect to non-treated CR/PP. The effect of several fatty acids used as templates and the water present in the reaction medium was studied. The oil-water activation and bioimprinting treatments that led to the best activities were assayed at the immobilization step. Instead of pre-treating CR/PP adsorbed in buffer medium, interfacial activation with octane/buffer and bioimprinting with a mix of fatty acids were carried out in the immobilization vial. The best results were found for CR/PP immobilized in 5/95 octane/buffer (v/v, %) medium. In that way, a biocatalyst with enhanced specific activity is obtained right from the immobilization vial with no need of further activation steps prior to reaction. © 2004 Elsevier Inc. All rights reserved.
Fil: Foresti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Alimenti, G. A.. Universidad Nacional del Sur. Departamento de Química; Argentina
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Materia
Adsorbed Lipase
Bioimprinting
Interfacial Activation
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:11336/57696
Acceder
id CONICETDig_28985653b7d073fcbf614f45917d659a
oai_identifier_str oai:ri.conicet.gov.ar:11336/57696
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesisForesti, María LauraAlimenti, G. A.Ferreira, María LujánAdsorbed LipaseBioimprintingInterfacial Activationhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Lipase from Candida rugosa adsorbed on polypropylene powder (CR/PP) was subjected to activation pre-treatments in order to enhance its activity in solvent-free ethyl oleate synthesis. The lipase activation achieved upon adsorption onto a hydrophobic support like PP was further enhanced through oil-water interfacial activation and bioimprinting of the immobilized catalyst. Several aliphatic hydrocarbons/buffer pH 7 mixtures were used in the pre-activation of CR/PP with specific activity increments of up to 29%. Molecular bioimprinting was also performed, with specific activity enhancement of near 70% with respect to non-treated CR/PP. The effect of several fatty acids used as templates and the water present in the reaction medium was studied. The oil-water activation and bioimprinting treatments that led to the best activities were assayed at the immobilization step. Instead of pre-treating CR/PP adsorbed in buffer medium, interfacial activation with octane/buffer and bioimprinting with a mix of fatty acids were carried out in the immobilization vial. The best results were found for CR/PP immobilized in 5/95 octane/buffer (v/v, %) medium. In that way, a biocatalyst with enhanced specific activity is obtained right from the immobilization vial with no need of further activation steps prior to reaction. © 2004 Elsevier Inc. All rights reserved.Fil: Foresti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaFil: Alimenti, G. A.. Universidad Nacional del Sur. Departamento de Química; ArgentinaFil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaElsevier Science Inc2005-02info: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/11336/57696Foresti, María Laura; Alimenti, G. A.; Ferreira, María Luján; Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis; Elsevier Science Inc; Enzyme and Microbial Technology; 36; 2-3; 2-2005; 338-3490141-0229CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.enzmictec.2004.09.012info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141022904002911info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:17:53Zoai:ri.conicet.gov.ar:11336/57696instacron: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 12:17:53.595CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis
title Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis
spellingShingle Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis
Foresti, María Laura
Adsorbed Lipase
Bioimprinting
Interfacial Activation
title_short Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis
title_full Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis
title_fullStr Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis
title_full_unstemmed Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis
title_sort Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis
dc.creator.none.fl_str_mv Foresti, María Laura
Alimenti, G. A.
Ferreira, María Luján
author Foresti, María Laura
author_facet Foresti, María Laura
Alimenti, G. A.
Ferreira, María Luján
author_role author
author2 Alimenti, G. A.
Ferreira, María Luján
author2_role author
author
dc.subject.none.fl_str_mv Adsorbed Lipase
Bioimprinting
Interfacial Activation
topic Adsorbed Lipase
Bioimprinting
Interfacial Activation
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Lipase from Candida rugosa adsorbed on polypropylene powder (CR/PP) was subjected to activation pre-treatments in order to enhance its activity in solvent-free ethyl oleate synthesis. The lipase activation achieved upon adsorption onto a hydrophobic support like PP was further enhanced through oil-water interfacial activation and bioimprinting of the immobilized catalyst. Several aliphatic hydrocarbons/buffer pH 7 mixtures were used in the pre-activation of CR/PP with specific activity increments of up to 29%. Molecular bioimprinting was also performed, with specific activity enhancement of near 70% with respect to non-treated CR/PP. The effect of several fatty acids used as templates and the water present in the reaction medium was studied. The oil-water activation and bioimprinting treatments that led to the best activities were assayed at the immobilization step. Instead of pre-treating CR/PP adsorbed in buffer medium, interfacial activation with octane/buffer and bioimprinting with a mix of fatty acids were carried out in the immobilization vial. The best results were found for CR/PP immobilized in 5/95 octane/buffer (v/v, %) medium. In that way, a biocatalyst with enhanced specific activity is obtained right from the immobilization vial with no need of further activation steps prior to reaction. © 2004 Elsevier Inc. All rights reserved.
Fil: Foresti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Alimenti, G. A.. Universidad Nacional del Sur. Departamento de Química; Argentina
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
description Lipase from Candida rugosa adsorbed on polypropylene powder (CR/PP) was subjected to activation pre-treatments in order to enhance its activity in solvent-free ethyl oleate synthesis. The lipase activation achieved upon adsorption onto a hydrophobic support like PP was further enhanced through oil-water interfacial activation and bioimprinting of the immobilized catalyst. Several aliphatic hydrocarbons/buffer pH 7 mixtures were used in the pre-activation of CR/PP with specific activity increments of up to 29%. Molecular bioimprinting was also performed, with specific activity enhancement of near 70% with respect to non-treated CR/PP. The effect of several fatty acids used as templates and the water present in the reaction medium was studied. The oil-water activation and bioimprinting treatments that led to the best activities were assayed at the immobilization step. Instead of pre-treating CR/PP adsorbed in buffer medium, interfacial activation with octane/buffer and bioimprinting with a mix of fatty acids were carried out in the immobilization vial. The best results were found for CR/PP immobilized in 5/95 octane/buffer (v/v, %) medium. In that way, a biocatalyst with enhanced specific activity is obtained right from the immobilization vial with no need of further activation steps prior to reaction. © 2004 Elsevier Inc. All rights reserved.
publishDate 2005
dc.date.none.fl_str_mv 2005-02
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/11336/57696
Foresti, María Laura; Alimenti, G. A.; Ferreira, María Luján; Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis; Elsevier Science Inc; Enzyme and Microbial Technology; 36; 2-3; 2-2005; 338-349
0141-0229
CONICET Digital
CONICET
url http://hdl.handle.net/11336/57696
identifier_str_mv Foresti, María Laura; Alimenti, G. A.; Ferreira, María Luján; Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis; Elsevier Science Inc; Enzyme and Microbial Technology; 36; 2-3; 2-2005; 338-349
0141-0229
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.enzmictec.2004.09.012
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141022904002911
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
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science Inc
publisher.none.fl_str_mv Elsevier Science Inc
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_ 1846782605997899776
score 12.982451

Publicaciones similares