Solvent-free ethyl oleate synthesis mediated by lipase from Candida antarctica B adsorbed on polypropylene powder

Autores
Foresti, María Laura; Ferreira, María Luján
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The enzymatic synthesis of ethyl oleate by direct esterification of oleic acid and ethanol in solvent-free media has been studied. Native lipase from Candida antarctica B and Candida antarctica B lipase adsorbed on powdered polypropylene were used with promising results. The influence of different parameters such us temperature, mass of lipase and aqueous content of reaction medium, on conversion profiles has been carefully studied. High water contents that ensured the co-existence of two liquid phases gave the best results, with conversions of up to 78.6% in 7 h of reaction. Pre-treatment with octane/buffer mixtures significantly reduced agglomeration of the immobilized catalyst, leading to important increments in specific enzymatic activity, when compared with non-pre-treated biocatalyst. Lipase desorption from PP has also been studied. © 2005 Elsevier B.V. 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: 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
Agglomeration
Desorption
Ethyl Oleate
Lipase
Reaction Parameters
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:11336/57695
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Solvent-free ethyl oleate synthesis mediated by lipase from Candida antarctica B adsorbed on polypropylene powderForesti, María LauraFerreira, María LujánAgglomerationDesorptionEthyl OleateLipaseReaction Parametershttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2The enzymatic synthesis of ethyl oleate by direct esterification of oleic acid and ethanol in solvent-free media has been studied. Native lipase from Candida antarctica B and Candida antarctica B lipase adsorbed on powdered polypropylene were used with promising results. The influence of different parameters such us temperature, mass of lipase and aqueous content of reaction medium, on conversion profiles has been carefully studied. High water contents that ensured the co-existence of two liquid phases gave the best results, with conversions of up to 78.6% in 7 h of reaction. Pre-treatment with octane/buffer mixtures significantly reduced agglomeration of the immobilized catalyst, leading to important increments in specific enzymatic activity, when compared with non-pre-treated biocatalyst. Lipase desorption from PP has also been studied. © 2005 Elsevier B.V. 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: 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 Science2005-10info: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/11336/57695Foresti, María Laura; Ferreira, María Luján; Solvent-free ethyl oleate synthesis mediated by lipase from Candida antarctica B adsorbed on polypropylene powder; Elsevier Science; Catalysis Today; 107-108; 10-2005; 23-300920-5861CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.cattod.2005.07.053info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0920586105003561info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:38:33Zoai:ri.conicet.gov.ar:11336/57695instacron: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 11:38:34.112CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Solvent-free ethyl oleate synthesis mediated by lipase from Candida antarctica B adsorbed on polypropylene powder
title Solvent-free ethyl oleate synthesis mediated by lipase from Candida antarctica B adsorbed on polypropylene powder
spellingShingle Solvent-free ethyl oleate synthesis mediated by lipase from Candida antarctica B adsorbed on polypropylene powder
Foresti, María Laura
Agglomeration
Desorption
Ethyl Oleate
Lipase
Reaction Parameters
title_short Solvent-free ethyl oleate synthesis mediated by lipase from Candida antarctica B adsorbed on polypropylene powder
title_full Solvent-free ethyl oleate synthesis mediated by lipase from Candida antarctica B adsorbed on polypropylene powder
title_fullStr Solvent-free ethyl oleate synthesis mediated by lipase from Candida antarctica B adsorbed on polypropylene powder
title_full_unstemmed Solvent-free ethyl oleate synthesis mediated by lipase from Candida antarctica B adsorbed on polypropylene powder
title_sort Solvent-free ethyl oleate synthesis mediated by lipase from Candida antarctica B adsorbed on polypropylene powder
dc.creator.none.fl_str_mv Foresti, María Laura
Ferreira, María Luján
author Foresti, María Laura
author_facet Foresti, María Laura
Ferreira, María Luján
author_role author
author2 Ferreira, María Luján
author2_role author
dc.subject.none.fl_str_mv Agglomeration
Desorption
Ethyl Oleate
Lipase
Reaction Parameters
topic Agglomeration
Desorption
Ethyl Oleate
Lipase
Reaction Parameters
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The enzymatic synthesis of ethyl oleate by direct esterification of oleic acid and ethanol in solvent-free media has been studied. Native lipase from Candida antarctica B and Candida antarctica B lipase adsorbed on powdered polypropylene were used with promising results. The influence of different parameters such us temperature, mass of lipase and aqueous content of reaction medium, on conversion profiles has been carefully studied. High water contents that ensured the co-existence of two liquid phases gave the best results, with conversions of up to 78.6% in 7 h of reaction. Pre-treatment with octane/buffer mixtures significantly reduced agglomeration of the immobilized catalyst, leading to important increments in specific enzymatic activity, when compared with non-pre-treated biocatalyst. Lipase desorption from PP has also been studied. © 2005 Elsevier B.V. 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: 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 The enzymatic synthesis of ethyl oleate by direct esterification of oleic acid and ethanol in solvent-free media has been studied. Native lipase from Candida antarctica B and Candida antarctica B lipase adsorbed on powdered polypropylene were used with promising results. The influence of different parameters such us temperature, mass of lipase and aqueous content of reaction medium, on conversion profiles has been carefully studied. High water contents that ensured the co-existence of two liquid phases gave the best results, with conversions of up to 78.6% in 7 h of reaction. Pre-treatment with octane/buffer mixtures significantly reduced agglomeration of the immobilized catalyst, leading to important increments in specific enzymatic activity, when compared with non-pre-treated biocatalyst. Lipase desorption from PP has also been studied. © 2005 Elsevier B.V. All rights reserved.
publishDate 2005
dc.date.none.fl_str_mv 2005-10
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/11336/57695
Foresti, María Laura; Ferreira, María Luján; Solvent-free ethyl oleate synthesis mediated by lipase from Candida antarctica B adsorbed on polypropylene powder; Elsevier Science; Catalysis Today; 107-108; 10-2005; 23-30
0920-5861
CONICET Digital
CONICET
url http://hdl.handle.net/11336/57695
identifier_str_mv Foresti, María Laura; Ferreira, María Luján; Solvent-free ethyl oleate synthesis mediated by lipase from Candida antarctica B adsorbed on polypropylene powder; Elsevier Science; Catalysis Today; 107-108; 10-2005; 23-30
0920-5861
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.cattod.2005.07.053
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0920586105003561
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
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 12.982451

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