Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase

Autores
Quintana, Paula Gabriela; Canet, Albert; Marciello, Marzia; Valero, Francisco; Palomo, José M.; Baldessari, Alicia
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A lipase-catalyzed preparation of ethyl and stearyl esters of chenodeoxycholic acid is described. Stearyl chenodeoxycholate is a new product and both bile acid esters were prepared through an enzymatic approach for the first time. The heterologous Rhizopus oryzae lipase, immobilized on two different supports proved to be an efficient catalyst, even more active than Candida antarctica lipase, in the esterification reaction using a complex substrate such as a bile acid. The immobilization of the enzyme on Octadecyl Sepabeads at pH 7 and 25 °C was the best choice to catalyze the esterification reaction. The influence of various reaction parameters, such as nature of the alcohol, alcohol:substrate ratio, enzyme:substrate ratio, solvent and temperature, was evaluated. Using the response surface methodology and a central composite rotatable design, the conversion of stearyl chenodeoxycholate was optimized by means of the study of the effect of enzyme:substrate ratio and alcohol:substrate ratio. The value 20 for ratios (E/S) and (A/S) was predicted as the optimal value to reach the maximum conversion. However, including economic aspects these ratios can be reduced up to 15. The well-known advantages of biocatalysis and the activity shown by the immobilized heterologous lipase make the reported procedure a convenient way to prepare chenodeoxycholic esters.
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
Fil: Canet, Albert. Universitat Autònoma de Barcelona; España
Fil: Marciello, Marzia. Consejo Superior de Investigaciones Científicas. Instituto de Catalisis y Petroleoquímica; España
Fil: Valero, Francisco. Universitat Autònoma de Barcelona; España
Fil: Palomo, José M.. Consejo Superior de Investigaciones Científicas. Instituto de Catalisis y Petroleoquímica; 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
Materia
Chenodeoxycholic Acid Esters
Enzyme-Catalyzed
Rhizopus Oryzae Lipase
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:11336/18722
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/18722
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipaseQuintana, Paula GabrielaCanet, AlbertMarciello, MarziaValero, FranciscoPalomo, José M.Baldessari, AliciaChenodeoxycholic Acid EstersEnzyme-CatalyzedRhizopus Oryzae LipaseImmobilizationhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1A lipase-catalyzed preparation of ethyl and stearyl esters of chenodeoxycholic acid is described. Stearyl chenodeoxycholate is a new product and both bile acid esters were prepared through an enzymatic approach for the first time. The heterologous Rhizopus oryzae lipase, immobilized on two different supports proved to be an efficient catalyst, even more active than Candida antarctica lipase, in the esterification reaction using a complex substrate such as a bile acid. The immobilization of the enzyme on Octadecyl Sepabeads at pH 7 and 25 °C was the best choice to catalyze the esterification reaction. The influence of various reaction parameters, such as nature of the alcohol, alcohol:substrate ratio, enzyme:substrate ratio, solvent and temperature, was evaluated. Using the response surface methodology and a central composite rotatable design, the conversion of stearyl chenodeoxycholate was optimized by means of the study of the effect of enzyme:substrate ratio and alcohol:substrate ratio. The value 20 for ratios (E/S) and (A/S) was predicted as the optimal value to reach the maximum conversion. However, including economic aspects these ratios can be reduced up to 15. The well-known advantages of biocatalysis and the activity shown by the immobilized heterologous lipase make the reported procedure a convenient way to prepare chenodeoxycholic esters.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; ArgentinaFil: Canet, Albert. Universitat Autònoma de Barcelona; EspañaFil: Marciello, Marzia. Consejo Superior de Investigaciones Científicas. Instituto de Catalisis y Petroleoquímica; EspañaFil: Valero, Francisco. Universitat Autònoma de Barcelona; EspañaFil: Palomo, José M.. Consejo Superior de Investigaciones Científicas. Instituto de Catalisis y Petroleoquímica; 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; ArgentinaElsevier Science2015-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/18722Quintana, Paula Gabriela; Canet, Albert; Marciello, Marzia; Valero, Francisco; Palomo, José M.; et al.; Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 118; 8-2015; 36-421381-1177CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2015.05.008info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1381117715001332info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:52:41Zoai:ri.conicet.gov.ar:11336/18722instacron: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 09:52:41.871CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase
title Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase
spellingShingle Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase
Quintana, Paula Gabriela
Chenodeoxycholic Acid Esters
Enzyme-Catalyzed
Rhizopus Oryzae Lipase
Immobilization
title_short Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase
title_full Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase
title_fullStr Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase
title_full_unstemmed Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase
title_sort Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase
dc.creator.none.fl_str_mv Quintana, Paula Gabriela
Canet, Albert
Marciello, Marzia
Valero, Francisco
Palomo, José M.
Baldessari, Alicia
author Quintana, Paula Gabriela
author_facet Quintana, Paula Gabriela
Canet, Albert
Marciello, Marzia
Valero, Francisco
Palomo, José M.
Baldessari, Alicia
author_role author
author2 Canet, Albert
Marciello, Marzia
Valero, Francisco
Palomo, José M.
Baldessari, Alicia
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Chenodeoxycholic Acid Esters
Enzyme-Catalyzed
Rhizopus Oryzae Lipase
Immobilization
topic Chenodeoxycholic Acid Esters
Enzyme-Catalyzed
Rhizopus Oryzae Lipase
Immobilization
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv A lipase-catalyzed preparation of ethyl and stearyl esters of chenodeoxycholic acid is described. Stearyl chenodeoxycholate is a new product and both bile acid esters were prepared through an enzymatic approach for the first time. The heterologous Rhizopus oryzae lipase, immobilized on two different supports proved to be an efficient catalyst, even more active than Candida antarctica lipase, in the esterification reaction using a complex substrate such as a bile acid. The immobilization of the enzyme on Octadecyl Sepabeads at pH 7 and 25 °C was the best choice to catalyze the esterification reaction. The influence of various reaction parameters, such as nature of the alcohol, alcohol:substrate ratio, enzyme:substrate ratio, solvent and temperature, was evaluated. Using the response surface methodology and a central composite rotatable design, the conversion of stearyl chenodeoxycholate was optimized by means of the study of the effect of enzyme:substrate ratio and alcohol:substrate ratio. The value 20 for ratios (E/S) and (A/S) was predicted as the optimal value to reach the maximum conversion. However, including economic aspects these ratios can be reduced up to 15. The well-known advantages of biocatalysis and the activity shown by the immobilized heterologous lipase make the reported procedure a convenient way to prepare chenodeoxycholic esters.
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
Fil: Canet, Albert. Universitat Autònoma de Barcelona; España
Fil: Marciello, Marzia. Consejo Superior de Investigaciones Científicas. Instituto de Catalisis y Petroleoquímica; España
Fil: Valero, Francisco. Universitat Autònoma de Barcelona; España
Fil: Palomo, José M.. Consejo Superior de Investigaciones Científicas. Instituto de Catalisis y Petroleoquímica; 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
description A lipase-catalyzed preparation of ethyl and stearyl esters of chenodeoxycholic acid is described. Stearyl chenodeoxycholate is a new product and both bile acid esters were prepared through an enzymatic approach for the first time. The heterologous Rhizopus oryzae lipase, immobilized on two different supports proved to be an efficient catalyst, even more active than Candida antarctica lipase, in the esterification reaction using a complex substrate such as a bile acid. The immobilization of the enzyme on Octadecyl Sepabeads at pH 7 and 25 °C was the best choice to catalyze the esterification reaction. The influence of various reaction parameters, such as nature of the alcohol, alcohol:substrate ratio, enzyme:substrate ratio, solvent and temperature, was evaluated. Using the response surface methodology and a central composite rotatable design, the conversion of stearyl chenodeoxycholate was optimized by means of the study of the effect of enzyme:substrate ratio and alcohol:substrate ratio. The value 20 for ratios (E/S) and (A/S) was predicted as the optimal value to reach the maximum conversion. However, including economic aspects these ratios can be reduced up to 15. The well-known advantages of biocatalysis and the activity shown by the immobilized heterologous lipase make the reported procedure a convenient way to prepare chenodeoxycholic esters.
publishDate 2015
dc.date.none.fl_str_mv 2015-08
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/11336/18722
Quintana, Paula Gabriela; Canet, Albert; Marciello, Marzia; Valero, Francisco; Palomo, José M.; et al.; Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 118; 8-2015; 36-42
1381-1177
CONICET Digital
CONICET
url http://hdl.handle.net/11336/18722
identifier_str_mv Quintana, Paula Gabriela; Canet, Albert; Marciello, Marzia; Valero, Francisco; Palomo, José M.; et al.; Enzyme-catalyzed preparation of chenodeoxycholic esters by an immobilized heterologous Rhizopus oryzae lipase; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 118; 8-2015; 36-42
1381-1177
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.molcatb.2015.05.008
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1381117715001332
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
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score 13.070432

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