Chitosan-immobilized lipases for the catalysis of fatty acid esterifications

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...

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Published in:Enzyme and Microbial Technology
Main Authors: Foresti, María Laura, Ferreira, María Luján
Format: Article in Journal/Newspaper
Language:English
Published: Elsevier Science Inc
Subjects:
Online Access:http://hdl.handle.net/11336/56272
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spelling ftconicet:oai:ri.conicet.gov.ar:11336/56272 2023-10-09T21:47:14+02:00 Chitosan-immobilized lipases for the catalysis of fatty acid esterifications Foresti, María Laura Ferreira, María Luján application/pdf http://hdl.handle.net/11336/56272 eng eng Elsevier Science Inc 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 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 info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ Chitosan Esterification Immobilization Lipase https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion ftconicet https://doi.org/10.1016/j.enzmictec.2006.06.009 2023-09-24T18:59:28Z 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 Article in Journal/Newspaper Antarc* Antarctica CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Argentina Rugosa ENVELOPE(-61.250,-61.250,-62.633,-62.633) Ferreira ENVELOPE(-62.050,-62.050,-64.600,-64.600) Enzyme and Microbial Technology 40 4 769 777
institution Open Polar
collection CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas)
op_collection_id ftconicet
language English
topic Chitosan
Esterification
Immobilization
Lipase
https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
spellingShingle Chitosan
Esterification
Immobilization
Lipase
https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
Foresti, María Laura
Ferreira, María Luján
Chitosan-immobilized lipases for the catalysis of fatty acid esterifications
topic_facet Chitosan
Esterification
Immobilization
Lipase
https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
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%. 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
format Article in Journal/Newspaper
author Foresti, María Laura
Ferreira, María Luján
author_facet Foresti, María Laura
Ferreira, María Luján
author_sort Foresti, María Laura
title Chitosan-immobilized lipases for the catalysis of fatty acid esterifications
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
publisher Elsevier Science Inc
url http://hdl.handle.net/11336/56272
long_lat ENVELOPE(-61.250,-61.250,-62.633,-62.633)
ENVELOPE(-62.050,-62.050,-64.600,-64.600)
geographic Argentina
Rugosa
Ferreira
geographic_facet Argentina
Rugosa
Ferreira
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_relation 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
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
op_rights info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
op_doi https://doi.org/10.1016/j.enzmictec.2006.06.009
container_title Enzyme and Microbial Technology
container_volume 40
container_issue 4
container_start_page 769
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