Multiple effects of water on solvent-free enzymatic esterifications

Autores
Foresti, María Laura; Pedernera, Marisa Noemi; Bucala, Veronica; Ferreira, María Luján
Año de publicación
2007
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Enhancement of the catalytic activity of lipases has commonly been performed by biocatalyst modification (immobilization on hydrophobic supports, activatiFon with interfaces, pretreatment with amphiphiles, etc.). In this work, the enhancement of the reaction rates obtained in lipase-catalyzed esterifications is achieved through modification of the number of liquid phases present in the medium in which the reaction takes place. The liquid medium may be constituted by either just one liquid phase or two liquid phases. The split of the liquid phase can be controlled by manipulating the water initially added to the system. As a result of the study of the role of water on the solvent-free enzymatic esterification of oleic acid with ethanol, the addition of relatively high amounts of water showed an unexpected beneficial effect: ester yields increased in systems with high amounts of water initially added. The addition of high amounts of water to the mixture of substrates led to the generation of two-liquid phases systems, in which the fatty acid and the produced ester remained in the organic phase, the added and reaction-generated water migrated to the aqueous phase, and the ethanol partitioned between both phases. The existence of a second aqueous phase from the beginning of the reaction favored the extraction of the water generated in the reaction, with an important reduction of the water content in the organic reactive phase. As a consequence, the increase in the global water content of the reaction medium not only did not favor hydrolysis, but also increased the fatty acid conversion in the first hours of reaction. Together with the lipase hydration and equilibrium shift, effects commonly considered in the literature of lipase-catalyzed esterifications, this manuscript emphasizes another effect of water related to the formation of a two-liquid phases system. Experimental and modeling data from reactions catalyzed with up to 15 biocatalysts (native and immobilized lipases) are presented to analyze the role of water on the rate of solvent-free enzymatic esterifications.
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: Pedernera, Marisa Noemi. 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: Bucala, Veronica. 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
Equilibrium Shift
Hydration
Lipase
Solvent-Free Esterification
Two-Liquid Phase System
Water Effects
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/55389
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/55389
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Multiple effects of water on solvent-free enzymatic esterificationsForesti, María LauraPedernera, Marisa NoemiBucala, VeronicaFerreira, María LujánEquilibrium ShiftHydrationLipaseSolvent-Free EsterificationTwo-Liquid Phase SystemWater Effectshttps://purl.org/becyt/ford/2.4https://purl.org/becyt/ford/2Enhancement of the catalytic activity of lipases has commonly been performed by biocatalyst modification (immobilization on hydrophobic supports, activatiFon with interfaces, pretreatment with amphiphiles, etc.). In this work, the enhancement of the reaction rates obtained in lipase-catalyzed esterifications is achieved through modification of the number of liquid phases present in the medium in which the reaction takes place. The liquid medium may be constituted by either just one liquid phase or two liquid phases. The split of the liquid phase can be controlled by manipulating the water initially added to the system. As a result of the study of the role of water on the solvent-free enzymatic esterification of oleic acid with ethanol, the addition of relatively high amounts of water showed an unexpected beneficial effect: ester yields increased in systems with high amounts of water initially added. The addition of high amounts of water to the mixture of substrates led to the generation of two-liquid phases systems, in which the fatty acid and the produced ester remained in the organic phase, the added and reaction-generated water migrated to the aqueous phase, and the ethanol partitioned between both phases. The existence of a second aqueous phase from the beginning of the reaction favored the extraction of the water generated in the reaction, with an important reduction of the water content in the organic reactive phase. As a consequence, the increase in the global water content of the reaction medium not only did not favor hydrolysis, but also increased the fatty acid conversion in the first hours of reaction. Together with the lipase hydration and equilibrium shift, effects commonly considered in the literature of lipase-catalyzed esterifications, this manuscript emphasizes another effect of water related to the formation of a two-liquid phases system. Experimental and modeling data from reactions catalyzed with up to 15 biocatalysts (native and immobilized lipases) are presented to analyze the role of water on the rate of solvent-free enzymatic esterifications.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: Pedernera, Marisa Noemi. 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: Bucala, Veronica. 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 Inc2007-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/55389Foresti, María Laura; Pedernera, Marisa Noemi; Bucala, Veronica; Ferreira, María Luján; Multiple effects of water on solvent-free enzymatic esterifications; Elsevier Science Inc; Enzyme and Microbial Technology; 41; 1-2; 7-2007; 62-700141-0229CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.enzmictec.2006.11.023info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141022906005886info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:07:05Zoai:ri.conicet.gov.ar:11336/55389instacron: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:34982025-09-10 13:07:05.861CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Multiple effects of water on solvent-free enzymatic esterifications
title Multiple effects of water on solvent-free enzymatic esterifications
spellingShingle Multiple effects of water on solvent-free enzymatic esterifications
Foresti, María Laura
Equilibrium Shift
Hydration
Lipase
Solvent-Free Esterification
Two-Liquid Phase System
Water Effects
title_short Multiple effects of water on solvent-free enzymatic esterifications
title_full Multiple effects of water on solvent-free enzymatic esterifications
title_fullStr Multiple effects of water on solvent-free enzymatic esterifications
title_full_unstemmed Multiple effects of water on solvent-free enzymatic esterifications
title_sort Multiple effects of water on solvent-free enzymatic esterifications
dc.creator.none.fl_str_mv Foresti, María Laura
Pedernera, Marisa Noemi
Bucala, Veronica
Ferreira, María Luján
author Foresti, María Laura
author_facet Foresti, María Laura
Pedernera, Marisa Noemi
Bucala, Veronica
Ferreira, María Luján
author_role author
author2 Pedernera, Marisa Noemi
Bucala, Veronica
Ferreira, María Luján
author2_role author
author
author
dc.subject.none.fl_str_mv Equilibrium Shift
Hydration
Lipase
Solvent-Free Esterification
Two-Liquid Phase System
Water Effects
topic Equilibrium Shift
Hydration
Lipase
Solvent-Free Esterification
Two-Liquid Phase System
Water Effects
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Enhancement of the catalytic activity of lipases has commonly been performed by biocatalyst modification (immobilization on hydrophobic supports, activatiFon with interfaces, pretreatment with amphiphiles, etc.). In this work, the enhancement of the reaction rates obtained in lipase-catalyzed esterifications is achieved through modification of the number of liquid phases present in the medium in which the reaction takes place. The liquid medium may be constituted by either just one liquid phase or two liquid phases. The split of the liquid phase can be controlled by manipulating the water initially added to the system. As a result of the study of the role of water on the solvent-free enzymatic esterification of oleic acid with ethanol, the addition of relatively high amounts of water showed an unexpected beneficial effect: ester yields increased in systems with high amounts of water initially added. The addition of high amounts of water to the mixture of substrates led to the generation of two-liquid phases systems, in which the fatty acid and the produced ester remained in the organic phase, the added and reaction-generated water migrated to the aqueous phase, and the ethanol partitioned between both phases. The existence of a second aqueous phase from the beginning of the reaction favored the extraction of the water generated in the reaction, with an important reduction of the water content in the organic reactive phase. As a consequence, the increase in the global water content of the reaction medium not only did not favor hydrolysis, but also increased the fatty acid conversion in the first hours of reaction. Together with the lipase hydration and equilibrium shift, effects commonly considered in the literature of lipase-catalyzed esterifications, this manuscript emphasizes another effect of water related to the formation of a two-liquid phases system. Experimental and modeling data from reactions catalyzed with up to 15 biocatalysts (native and immobilized lipases) are presented to analyze the role of water on the rate of solvent-free enzymatic esterifications.
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: Pedernera, Marisa Noemi. 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: Bucala, Veronica. 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 Enhancement of the catalytic activity of lipases has commonly been performed by biocatalyst modification (immobilization on hydrophobic supports, activatiFon with interfaces, pretreatment with amphiphiles, etc.). In this work, the enhancement of the reaction rates obtained in lipase-catalyzed esterifications is achieved through modification of the number of liquid phases present in the medium in which the reaction takes place. The liquid medium may be constituted by either just one liquid phase or two liquid phases. The split of the liquid phase can be controlled by manipulating the water initially added to the system. As a result of the study of the role of water on the solvent-free enzymatic esterification of oleic acid with ethanol, the addition of relatively high amounts of water showed an unexpected beneficial effect: ester yields increased in systems with high amounts of water initially added. The addition of high amounts of water to the mixture of substrates led to the generation of two-liquid phases systems, in which the fatty acid and the produced ester remained in the organic phase, the added and reaction-generated water migrated to the aqueous phase, and the ethanol partitioned between both phases. The existence of a second aqueous phase from the beginning of the reaction favored the extraction of the water generated in the reaction, with an important reduction of the water content in the organic reactive phase. As a consequence, the increase in the global water content of the reaction medium not only did not favor hydrolysis, but also increased the fatty acid conversion in the first hours of reaction. Together with the lipase hydration and equilibrium shift, effects commonly considered in the literature of lipase-catalyzed esterifications, this manuscript emphasizes another effect of water related to the formation of a two-liquid phases system. Experimental and modeling data from reactions catalyzed with up to 15 biocatalysts (native and immobilized lipases) are presented to analyze the role of water on the rate of solvent-free enzymatic esterifications.
publishDate 2007
dc.date.none.fl_str_mv 2007-07
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/11336/55389
Foresti, María Laura; Pedernera, Marisa Noemi; Bucala, Veronica; Ferreira, María Luján; Multiple effects of water on solvent-free enzymatic esterifications; Elsevier Science Inc; Enzyme and Microbial Technology; 41; 1-2; 7-2007; 62-70
0141-0229
CONICET Digital
CONICET
url http://hdl.handle.net/11336/55389
identifier_str_mv Foresti, María Laura; Pedernera, Marisa Noemi; Bucala, Veronica; Ferreira, María Luján; Multiple effects of water on solvent-free enzymatic esterifications; Elsevier Science Inc; Enzyme and Microbial Technology; 41; 1-2; 7-2007; 62-70
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.2006.11.023
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141022906005886
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
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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score 12.993085

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