Effect of several reaction parameters in the solvent-free ethyl oleate synthesis using Candida rugosa lipase immobilised on polypropylene

Autores
Foresti, María Laura; Errazu, Alberto Felipe; Ferreira, María Luján
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Lipase from Candida rugosa was immobilised onto polypropylene powder by physical adsorption. The immobilised catalyst (CR/PP) was used in the enzymatic synthesis of ethyl oleate in solvent-free medium. The influence of the initial water content, acidity of the aqueous media added, mass of catalyst, reaction temperature, substrate ratio, etc., on enzymatic activity, has been studied. Comparison of specific enzymatic activities achieved using the prepared catalyst and the crude lipase demonstrated that C. rugosa lipase was interfacially activated upon its adsorption on polypropylene. Besides, immobilisation of the lipase led to enhanced thermal stability. Experimental data reported in this manuscript do not belong to equilibrium data but to enzymatic activity attained in the first 2 h of reaction. After this period, it was shown that, in the current synthesis, deactivation/agglomeration/inhibition of the catalyst prevented further CRL activity. However, 2 h measurements allowed fulfilling the aim of this work: the determination of the best conditions for ethyl oleate production in short periods of time, using an immobilised derivative of a relatively cheap lipase as it is C. rugosa lipase. Best results were achieved in the reaction performed at 45°C and 350 rpm, with an initial stoichiometric ratio of substrates, 20% of aqueous content, and mediated by 50 mg of CR/PP (0.0585 mmol/mg of CR-h). The deleterious effect of ethanol excess and agglomeration of the native and immobilised catalyst have been analysed. © 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: Errazu, Alberto Felipe. 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
Aggregation
Ethyl Oleate Synthesis
Inhibiting Effect
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:11336/57777
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/57777
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Effect of several reaction parameters in the solvent-free ethyl oleate synthesis using Candida rugosa lipase immobilised on polypropyleneForesti, María LauraErrazu, Alberto FelipeFerreira, María LujánAggregationEthyl Oleate SynthesisInhibiting EffectLipaseReaction Parametershttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Lipase from Candida rugosa was immobilised onto polypropylene powder by physical adsorption. The immobilised catalyst (CR/PP) was used in the enzymatic synthesis of ethyl oleate in solvent-free medium. The influence of the initial water content, acidity of the aqueous media added, mass of catalyst, reaction temperature, substrate ratio, etc., on enzymatic activity, has been studied. Comparison of specific enzymatic activities achieved using the prepared catalyst and the crude lipase demonstrated that C. rugosa lipase was interfacially activated upon its adsorption on polypropylene. Besides, immobilisation of the lipase led to enhanced thermal stability. Experimental data reported in this manuscript do not belong to equilibrium data but to enzymatic activity attained in the first 2 h of reaction. After this period, it was shown that, in the current synthesis, deactivation/agglomeration/inhibition of the catalyst prevented further CRL activity. However, 2 h measurements allowed fulfilling the aim of this work: the determination of the best conditions for ethyl oleate production in short periods of time, using an immobilised derivative of a relatively cheap lipase as it is C. rugosa lipase. Best results were achieved in the reaction performed at 45°C and 350 rpm, with an initial stoichiometric ratio of substrates, 20% of aqueous content, and mediated by 50 mg of CR/PP (0.0585 mmol/mg of CR-h). The deleterious effect of ethanol excess and agglomeration of the native and immobilised catalyst have been analysed. © 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: Errazu, Alberto Felipe. 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 Sa2005-08info: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/11336/57777Foresti, María Laura; Errazu, Alberto Felipe; Ferreira, María Luján; Effect of several reaction parameters in the solvent-free ethyl oleate synthesis using Candida rugosa lipase immobilised on polypropylene; Elsevier Science Sa; Biochemical Engineering Journal; 25; 1; 8-2005; 69-771369-703XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bej.2005.04.002info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1369703X05000860info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:35:14Zoai:ri.conicet.gov.ar:11336/57777instacron: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 10:35:14.772CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Effect of several reaction parameters in the solvent-free ethyl oleate synthesis using Candida rugosa lipase immobilised on polypropylene
title Effect of several reaction parameters in the solvent-free ethyl oleate synthesis using Candida rugosa lipase immobilised on polypropylene
spellingShingle Effect of several reaction parameters in the solvent-free ethyl oleate synthesis using Candida rugosa lipase immobilised on polypropylene
Foresti, María Laura
Aggregation
Ethyl Oleate Synthesis
Inhibiting Effect
Lipase
Reaction Parameters
title_short Effect of several reaction parameters in the solvent-free ethyl oleate synthesis using Candida rugosa lipase immobilised on polypropylene
title_full Effect of several reaction parameters in the solvent-free ethyl oleate synthesis using Candida rugosa lipase immobilised on polypropylene
title_fullStr Effect of several reaction parameters in the solvent-free ethyl oleate synthesis using Candida rugosa lipase immobilised on polypropylene
title_full_unstemmed Effect of several reaction parameters in the solvent-free ethyl oleate synthesis using Candida rugosa lipase immobilised on polypropylene
title_sort Effect of several reaction parameters in the solvent-free ethyl oleate synthesis using Candida rugosa lipase immobilised on polypropylene
dc.creator.none.fl_str_mv Foresti, María Laura
Errazu, Alberto Felipe
Ferreira, María Luján
author Foresti, María Laura
author_facet Foresti, María Laura
Errazu, Alberto Felipe
Ferreira, María Luján
author_role author
author2 Errazu, Alberto Felipe
Ferreira, María Luján
author2_role author
author
dc.subject.none.fl_str_mv Aggregation
Ethyl Oleate Synthesis
Inhibiting Effect
Lipase
Reaction Parameters
topic Aggregation
Ethyl Oleate Synthesis
Inhibiting Effect
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 Lipase from Candida rugosa was immobilised onto polypropylene powder by physical adsorption. The immobilised catalyst (CR/PP) was used in the enzymatic synthesis of ethyl oleate in solvent-free medium. The influence of the initial water content, acidity of the aqueous media added, mass of catalyst, reaction temperature, substrate ratio, etc., on enzymatic activity, has been studied. Comparison of specific enzymatic activities achieved using the prepared catalyst and the crude lipase demonstrated that C. rugosa lipase was interfacially activated upon its adsorption on polypropylene. Besides, immobilisation of the lipase led to enhanced thermal stability. Experimental data reported in this manuscript do not belong to equilibrium data but to enzymatic activity attained in the first 2 h of reaction. After this period, it was shown that, in the current synthesis, deactivation/agglomeration/inhibition of the catalyst prevented further CRL activity. However, 2 h measurements allowed fulfilling the aim of this work: the determination of the best conditions for ethyl oleate production in short periods of time, using an immobilised derivative of a relatively cheap lipase as it is C. rugosa lipase. Best results were achieved in the reaction performed at 45°C and 350 rpm, with an initial stoichiometric ratio of substrates, 20% of aqueous content, and mediated by 50 mg of CR/PP (0.0585 mmol/mg of CR-h). The deleterious effect of ethanol excess and agglomeration of the native and immobilised catalyst have been analysed. © 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: Errazu, Alberto Felipe. 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 Lipase from Candida rugosa was immobilised onto polypropylene powder by physical adsorption. The immobilised catalyst (CR/PP) was used in the enzymatic synthesis of ethyl oleate in solvent-free medium. The influence of the initial water content, acidity of the aqueous media added, mass of catalyst, reaction temperature, substrate ratio, etc., on enzymatic activity, has been studied. Comparison of specific enzymatic activities achieved using the prepared catalyst and the crude lipase demonstrated that C. rugosa lipase was interfacially activated upon its adsorption on polypropylene. Besides, immobilisation of the lipase led to enhanced thermal stability. Experimental data reported in this manuscript do not belong to equilibrium data but to enzymatic activity attained in the first 2 h of reaction. After this period, it was shown that, in the current synthesis, deactivation/agglomeration/inhibition of the catalyst prevented further CRL activity. However, 2 h measurements allowed fulfilling the aim of this work: the determination of the best conditions for ethyl oleate production in short periods of time, using an immobilised derivative of a relatively cheap lipase as it is C. rugosa lipase. Best results were achieved in the reaction performed at 45°C and 350 rpm, with an initial stoichiometric ratio of substrates, 20% of aqueous content, and mediated by 50 mg of CR/PP (0.0585 mmol/mg of CR-h). The deleterious effect of ethanol excess and agglomeration of the native and immobilised catalyst have been analysed. © 2005 Elsevier B.V. All rights reserved.
publishDate 2005
dc.date.none.fl_str_mv 2005-08
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/11336/57777
Foresti, María Laura; Errazu, Alberto Felipe; Ferreira, María Luján; Effect of several reaction parameters in the solvent-free ethyl oleate synthesis using Candida rugosa lipase immobilised on polypropylene; Elsevier Science Sa; Biochemical Engineering Journal; 25; 1; 8-2005; 69-77
1369-703X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/57777
identifier_str_mv Foresti, María Laura; Errazu, Alberto Felipe; Ferreira, María Luján; Effect of several reaction parameters in the solvent-free ethyl oleate synthesis using Candida rugosa lipase immobilised on polypropylene; Elsevier Science Sa; Biochemical Engineering Journal; 25; 1; 8-2005; 69-77
1369-703X
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.bej.2005.04.002
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1369703X05000860
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 Sa
publisher.none.fl_str_mv Elsevier Science Sa
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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