Chitosan-immobilized lipases for the catalysis of fatty acid esterifications
- Autores
- Foresti, María Laura; Ferreira, María Luján
- Año de publicación
- 2007
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Lipases from Candida rugosa, Pseudomonas fluorescens and Candida antarctica B were immobilized onto chitosan and glutaraldehyde-pretreated chitosan powders. The prepared biocatalysts were assayed in the direct esterification of oleic acid and ethanol to produce the ethyl oleate. In order to maximize ester production and avoid solvent-related costs (the solvent itself, solvent recovery and solvent recycle), the synthesis of ethyl oleate was performed in a solvent-free system. The different structures of the lipases chosen for the catalysis led to very different activity levels, with C. antarctica B derivatives being the most active ones. The parametric study performed revealed that the best operation conditions for ester synthesis are found at mild temperatures (35-45 °C), and in "biphasic systems" (two liquid phases), generated upon addition of relatively high quantities of water to the mixture of substrates. The reduction of the concentration of water in the organic reactive phase of biphasic systems favored ester synthesis, with higher ester yields in the first hours of reaction than those measured in systems with no added water. In the optimum conditions mentioned the biocatalyst resulting from the immobilization of lipase from C. antarctica B onto untreated chitosan powder led to 75% conversion of the fatty acid in 24 h of reaction. The stability of this catalyst also proved to be very attractive with five consecutive 24 h uses with a residual activity of 90-95%.
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
-
Chitosan
Esterification
Immobilization
Lipase - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/56272
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Chitosan-immobilized lipases for the catalysis of fatty acid esterificationsForesti, María LauraFerreira, María LujánChitosanEsterificationImmobilizationLipasehttps://purl.org/becyt/ford/2.4https://purl.org/becyt/ford/2Lipases from Candida rugosa, Pseudomonas fluorescens and Candida antarctica B were immobilized onto chitosan and glutaraldehyde-pretreated chitosan powders. The prepared biocatalysts were assayed in the direct esterification of oleic acid and ethanol to produce the ethyl oleate. In order to maximize ester production and avoid solvent-related costs (the solvent itself, solvent recovery and solvent recycle), the synthesis of ethyl oleate was performed in a solvent-free system. The different structures of the lipases chosen for the catalysis led to very different activity levels, with C. antarctica B derivatives being the most active ones. The parametric study performed revealed that the best operation conditions for ester synthesis are found at mild temperatures (35-45 °C), and in "biphasic systems" (two liquid phases), generated upon addition of relatively high quantities of water to the mixture of substrates. The reduction of the concentration of water in the organic reactive phase of biphasic systems favored ester synthesis, with higher ester yields in the first hours of reaction than those measured in systems with no added water. In the optimum conditions mentioned the biocatalyst resulting from the immobilization of lipase from C. antarctica B onto untreated chitosan powder led to 75% conversion of the fatty acid in 24 h of reaction. The stability of this catalyst also proved to be very attractive with five consecutive 24 h uses with a residual activity of 90-95%.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 Science Inc2007-03info: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/11336/56272Foresti, María Laura; Ferreira, María Luján; Chitosan-immobilized lipases for the catalysis of fatty acid esterifications; Elsevier Science Inc; Enzyme and Microbial Technology; 40; 4; 3-2007; 769-7770141-0229CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.enzmictec.2006.06.009info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S014102290600336Xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:52:47Zoai:ri.conicet.gov.ar:11336/56272instacron: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:34982025-09-03 09:52:47.852CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Chitosan-immobilized lipases for the catalysis of fatty acid esterifications |
title |
Chitosan-immobilized lipases for the catalysis of fatty acid esterifications |
spellingShingle |
Chitosan-immobilized lipases for the catalysis of fatty acid esterifications Foresti, María Laura Chitosan Esterification Immobilization Lipase |
title_short |
Chitosan-immobilized lipases for the catalysis of fatty acid esterifications |
title_full |
Chitosan-immobilized lipases for the catalysis of fatty acid esterifications |
title_fullStr |
Chitosan-immobilized lipases for the catalysis of fatty acid esterifications |
title_full_unstemmed |
Chitosan-immobilized lipases for the catalysis of fatty acid esterifications |
title_sort |
Chitosan-immobilized lipases for the catalysis of fatty acid esterifications |
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 |
Chitosan Esterification Immobilization Lipase |
topic |
Chitosan Esterification Immobilization Lipase |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 |
dc.description.none.fl_txt_mv |
Lipases from Candida rugosa, Pseudomonas fluorescens and Candida antarctica B were immobilized onto chitosan and glutaraldehyde-pretreated chitosan powders. The prepared biocatalysts were assayed in the direct esterification of oleic acid and ethanol to produce the ethyl oleate. In order to maximize ester production and avoid solvent-related costs (the solvent itself, solvent recovery and solvent recycle), the synthesis of ethyl oleate was performed in a solvent-free system. The different structures of the lipases chosen for the catalysis led to very different activity levels, with C. antarctica B derivatives being the most active ones. The parametric study performed revealed that the best operation conditions for ester synthesis are found at mild temperatures (35-45 °C), and in "biphasic systems" (two liquid phases), generated upon addition of relatively high quantities of water to the mixture of substrates. The reduction of the concentration of water in the organic reactive phase of biphasic systems favored ester synthesis, with higher ester yields in the first hours of reaction than those measured in systems with no added water. In the optimum conditions mentioned the biocatalyst resulting from the immobilization of lipase from C. antarctica B onto untreated chitosan powder led to 75% conversion of the fatty acid in 24 h of reaction. The stability of this catalyst also proved to be very attractive with five consecutive 24 h uses with a residual activity of 90-95%. 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 |
Lipases from Candida rugosa, Pseudomonas fluorescens and Candida antarctica B were immobilized onto chitosan and glutaraldehyde-pretreated chitosan powders. The prepared biocatalysts were assayed in the direct esterification of oleic acid and ethanol to produce the ethyl oleate. In order to maximize ester production and avoid solvent-related costs (the solvent itself, solvent recovery and solvent recycle), the synthesis of ethyl oleate was performed in a solvent-free system. The different structures of the lipases chosen for the catalysis led to very different activity levels, with C. antarctica B derivatives being the most active ones. The parametric study performed revealed that the best operation conditions for ester synthesis are found at mild temperatures (35-45 °C), and in "biphasic systems" (two liquid phases), generated upon addition of relatively high quantities of water to the mixture of substrates. The reduction of the concentration of water in the organic reactive phase of biphasic systems favored ester synthesis, with higher ester yields in the first hours of reaction than those measured in systems with no added water. In the optimum conditions mentioned the biocatalyst resulting from the immobilization of lipase from C. antarctica B onto untreated chitosan powder led to 75% conversion of the fatty acid in 24 h of reaction. The stability of this catalyst also proved to be very attractive with five consecutive 24 h uses with a residual activity of 90-95%. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007-03 |
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/11336/56272 Foresti, María Laura; Ferreira, María Luján; Chitosan-immobilized lipases for the catalysis of fatty acid esterifications; Elsevier Science Inc; Enzyme and Microbial Technology; 40; 4; 3-2007; 769-777 0141-0229 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/56272 |
identifier_str_mv |
Foresti, María Laura; Ferreira, María Luján; Chitosan-immobilized lipases for the catalysis of fatty acid esterifications; Elsevier Science Inc; Enzyme and Microbial Technology; 40; 4; 3-2007; 769-777 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.2006.06.009 info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S014102290600336X |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-nd/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 |
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1842269182760058880 |
score |
13.13397 |