Immobilized heterologous Rhizopus Oryzae lipase as an efficient catalyst in the acetylation of cortexolone

Autores
Quintana, Paula Gabriela; Guillén, Marina; Marciello, Marzia; Valero, Francisco; Palomo, Jose M.; Baldessari, Alicia
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The enzymatic preparation of a monoacetyl derivative of the corticosteroid cortexolone, through a transesterification reaction, is described. The heterologous Rhizopus oryzae lipase, immobilized on three different supports, proved to be an efficient catalyst in the acylation reaction using a complex substrate such as cortexolone. Immobilization of the enzyme on Lewatit 1600 resin at pH = 7 and 25 °C was the best condition for catalysis of the acetylation reaction. The influence of various reaction parameters, such as the nature of the acetylating agent, the solvent, the temperature, and the ratios of acetylating agent to substrate, and enzyme to substrate, was evaluated. Using the response surface methodology and a central composite rotatable design, the specific yield of acetylated cortexolone was optimized by means of the study of the effect of the enzyme (E)/substrate (S) and the acylating agent (A)/substrate ratios. The ratios of 5 (E/S) and 31.6 (A/S) were predicted as the optimal values to reach the maximum specific yield of the product (P): 1.59 mmol P/mmol A·g E. The mild reaction conditions and low environmental impact make the biocatalytic procedure a convenient way to prepare the reported derivative of this biologically active steroid. The regioselective acetylation of cortexolone was achieved by using an immobilized heterologous Rhizopus oryzae lipase. The mild reaction conditions and low environmental impact make the biocatalytic procedure a convenient way to prepare the monoacetyl derivative of this biologically active steroid. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Fil: Quintana, Paula Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Unidad de Microanálisis y Métodos Físicos en Química Orgánica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Unidad de Microanálisis y Métodos Físicos en Química Orgánica; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica; Argentina
Fil: Guillén, Marina. Universitat Autònoma de Barcelona; España
Fil: Marciello, Marzia. Consejo Superior de Investigaciones Científicas; España
Fil: Valero, Francisco. Universitat Autònoma de Barcelona; España
Fil: Palomo, Jose M.. Consejo Superior de Investigaciones Científicas; España
Fil: Baldessari, Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Unidad de Microanálisis y Métodos Físicos en Química Orgánica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Unidad de Microanálisis y Métodos Físicos en Química Orgánica; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica; Argentina
Materia
Acylation
Biocatalysis
Enzymes
Immobilization
Steroids
Supported Catalysts
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:11336/70443
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/70443
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Immobilized heterologous Rhizopus Oryzae lipase as an efficient catalyst in the acetylation of cortexoloneQuintana, Paula GabrielaGuillén, MarinaMarciello, MarziaValero, FranciscoPalomo, Jose M.Baldessari, AliciaAcylationBiocatalysisEnzymesImmobilizationSteroidsSupported Catalystshttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The enzymatic preparation of a monoacetyl derivative of the corticosteroid cortexolone, through a transesterification reaction, is described. The heterologous Rhizopus oryzae lipase, immobilized on three different supports, proved to be an efficient catalyst in the acylation reaction using a complex substrate such as cortexolone. Immobilization of the enzyme on Lewatit 1600 resin at pH = 7 and 25 °C was the best condition for catalysis of the acetylation reaction. The influence of various reaction parameters, such as the nature of the acetylating agent, the solvent, the temperature, and the ratios of acetylating agent to substrate, and enzyme to substrate, was evaluated. Using the response surface methodology and a central composite rotatable design, the specific yield of acetylated cortexolone was optimized by means of the study of the effect of the enzyme (E)/substrate (S) and the acylating agent (A)/substrate ratios. The ratios of 5 (E/S) and 31.6 (A/S) were predicted as the optimal values to reach the maximum specific yield of the product (P): 1.59 mmol P/mmol A·g E. The mild reaction conditions and low environmental impact make the biocatalytic procedure a convenient way to prepare the reported derivative of this biologically active steroid. The regioselective acetylation of cortexolone was achieved by using an immobilized heterologous Rhizopus oryzae lipase. The mild reaction conditions and low environmental impact make the biocatalytic procedure a convenient way to prepare the monoacetyl derivative of this biologically active steroid. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.Fil: Quintana, Paula Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Unidad de Microanálisis y Métodos Físicos en Química Orgánica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Unidad de Microanálisis y Métodos Físicos en Química Orgánica; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica; ArgentinaFil: Guillén, Marina. Universitat Autònoma de Barcelona; EspañaFil: Marciello, Marzia. Consejo Superior de Investigaciones Científicas; EspañaFil: Valero, Francisco. Universitat Autònoma de Barcelona; EspañaFil: Palomo, Jose M.. Consejo Superior de Investigaciones Científicas; EspañaFil: Baldessari, Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Unidad de Microanálisis y Métodos Físicos en Química Orgánica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Unidad de Microanálisis y Métodos Físicos en Química Orgánica; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica; ArgentinaWiley VCH Verlag2012-08info: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/11336/70443Quintana, Paula Gabriela; Guillén, Marina; Marciello, Marzia; Valero, Francisco; Palomo, Jose M.; et al.; Immobilized heterologous Rhizopus Oryzae lipase as an efficient catalyst in the acetylation of cortexolone; Wiley VCH Verlag; European Journal of Organic Chemistry; 23; 8-2012; 4306-43121434-193XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1002/ejoc.201200178info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/ejoc.201200178info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:44:01Zoai:ri.conicet.gov.ar:11336/70443instacron: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 09:44:01.363CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Immobilized heterologous Rhizopus Oryzae lipase as an efficient catalyst in the acetylation of cortexolone
title Immobilized heterologous Rhizopus Oryzae lipase as an efficient catalyst in the acetylation of cortexolone
spellingShingle Immobilized heterologous Rhizopus Oryzae lipase as an efficient catalyst in the acetylation of cortexolone
Quintana, Paula Gabriela
Acylation
Biocatalysis
Enzymes
Immobilization
Steroids
Supported Catalysts
title_short Immobilized heterologous Rhizopus Oryzae lipase as an efficient catalyst in the acetylation of cortexolone
title_full Immobilized heterologous Rhizopus Oryzae lipase as an efficient catalyst in the acetylation of cortexolone
title_fullStr Immobilized heterologous Rhizopus Oryzae lipase as an efficient catalyst in the acetylation of cortexolone
title_full_unstemmed Immobilized heterologous Rhizopus Oryzae lipase as an efficient catalyst in the acetylation of cortexolone
title_sort Immobilized heterologous Rhizopus Oryzae lipase as an efficient catalyst in the acetylation of cortexolone
dc.creator.none.fl_str_mv Quintana, Paula Gabriela
Guillén, Marina
Marciello, Marzia
Valero, Francisco
Palomo, Jose M.
Baldessari, Alicia
author Quintana, Paula Gabriela
author_facet Quintana, Paula Gabriela
Guillén, Marina
Marciello, Marzia
Valero, Francisco
Palomo, Jose M.
Baldessari, Alicia
author_role author
author2 Guillén, Marina
Marciello, Marzia
Valero, Francisco
Palomo, Jose M.
Baldessari, Alicia
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Acylation
Biocatalysis
Enzymes
Immobilization
Steroids
Supported Catalysts
topic Acylation
Biocatalysis
Enzymes
Immobilization
Steroids
Supported Catalysts
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The enzymatic preparation of a monoacetyl derivative of the corticosteroid cortexolone, through a transesterification reaction, is described. The heterologous Rhizopus oryzae lipase, immobilized on three different supports, proved to be an efficient catalyst in the acylation reaction using a complex substrate such as cortexolone. Immobilization of the enzyme on Lewatit 1600 resin at pH = 7 and 25 °C was the best condition for catalysis of the acetylation reaction. The influence of various reaction parameters, such as the nature of the acetylating agent, the solvent, the temperature, and the ratios of acetylating agent to substrate, and enzyme to substrate, was evaluated. Using the response surface methodology and a central composite rotatable design, the specific yield of acetylated cortexolone was optimized by means of the study of the effect of the enzyme (E)/substrate (S) and the acylating agent (A)/substrate ratios. The ratios of 5 (E/S) and 31.6 (A/S) were predicted as the optimal values to reach the maximum specific yield of the product (P): 1.59 mmol P/mmol A·g E. The mild reaction conditions and low environmental impact make the biocatalytic procedure a convenient way to prepare the reported derivative of this biologically active steroid. The regioselective acetylation of cortexolone was achieved by using an immobilized heterologous Rhizopus oryzae lipase. The mild reaction conditions and low environmental impact make the biocatalytic procedure a convenient way to prepare the monoacetyl derivative of this biologically active steroid. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Fil: Quintana, Paula Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Unidad de Microanálisis y Métodos Físicos en Química Orgánica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Unidad de Microanálisis y Métodos Físicos en Química Orgánica; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica; Argentina
Fil: Guillén, Marina. Universitat Autònoma de Barcelona; España
Fil: Marciello, Marzia. Consejo Superior de Investigaciones Científicas; España
Fil: Valero, Francisco. Universitat Autònoma de Barcelona; España
Fil: Palomo, Jose M.. Consejo Superior de Investigaciones Científicas; España
Fil: Baldessari, Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Unidad de Microanálisis y Métodos Físicos en Química Orgánica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Unidad de Microanálisis y Métodos Físicos en Química Orgánica; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica; Argentina
description The enzymatic preparation of a monoacetyl derivative of the corticosteroid cortexolone, through a transesterification reaction, is described. The heterologous Rhizopus oryzae lipase, immobilized on three different supports, proved to be an efficient catalyst in the acylation reaction using a complex substrate such as cortexolone. Immobilization of the enzyme on Lewatit 1600 resin at pH = 7 and 25 °C was the best condition for catalysis of the acetylation reaction. The influence of various reaction parameters, such as the nature of the acetylating agent, the solvent, the temperature, and the ratios of acetylating agent to substrate, and enzyme to substrate, was evaluated. Using the response surface methodology and a central composite rotatable design, the specific yield of acetylated cortexolone was optimized by means of the study of the effect of the enzyme (E)/substrate (S) and the acylating agent (A)/substrate ratios. The ratios of 5 (E/S) and 31.6 (A/S) were predicted as the optimal values to reach the maximum specific yield of the product (P): 1.59 mmol P/mmol A·g E. The mild reaction conditions and low environmental impact make the biocatalytic procedure a convenient way to prepare the reported derivative of this biologically active steroid. The regioselective acetylation of cortexolone was achieved by using an immobilized heterologous Rhizopus oryzae lipase. The mild reaction conditions and low environmental impact make the biocatalytic procedure a convenient way to prepare the monoacetyl derivative of this biologically active steroid. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
publishDate 2012
dc.date.none.fl_str_mv 2012-08
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/11336/70443
Quintana, Paula Gabriela; Guillén, Marina; Marciello, Marzia; Valero, Francisco; Palomo, Jose M.; et al.; Immobilized heterologous Rhizopus Oryzae lipase as an efficient catalyst in the acetylation of cortexolone; Wiley VCH Verlag; European Journal of Organic Chemistry; 23; 8-2012; 4306-4312
1434-193X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/70443
identifier_str_mv Quintana, Paula Gabriela; Guillén, Marina; Marciello, Marzia; Valero, Francisco; Palomo, Jose M.; et al.; Immobilized heterologous Rhizopus Oryzae lipase as an efficient catalyst in the acetylation of cortexolone; Wiley VCH Verlag; European Journal of Organic Chemistry; 23; 8-2012; 4306-4312
1434-193X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1002/ejoc.201200178
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/ejoc.201200178
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 Wiley VCH Verlag
publisher.none.fl_str_mv Wiley VCH Verlag
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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score 13.070432

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