Effect of operating variables and kinetics of the lipase catalyzed transesterification of ethylene carbonate and glycerol

Autores
Gutierrez Lazaro, Ana; Velasco, Daniel; Boldrini, Diego Emmanuel; Yustos, Pedro; Esteban, Jesús; Ladero, Miguel
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Glycerol carbonate (GC) is a value-added product originating from the valorization of widely available glycerol (Gly), a side stream from the production of biodiesel. Here we approach the production of this chemical comparing two reactions based on the transesterification of Gly with dimethyl carbonate (DMC) and ethylene carbonate (EC). For the former reaction, it was observed that the free enzyme CALB (lipase B from Candida antarctica) gave the best results, whereas for the latter, Eversa Transform (a genetic modification of Thermomyces lanuginosus lipase) performed better than the rest. With the selected catalysts, their immobilized analogous enzymes Novozym 435 and Lypozyme TL IM, respectively, were also tested. Observing that the yields for the reaction with EC were significantly faster, other operating variables were evaluated, resulting the best performance using a closed system, tert-butanol as solvent, a concentration of enzyme Eversa Transform of 3 % w/w, a molar excess of EC:Gly of 9:1 and a temperature of 60 C. Finally, several runs were conducted at different temperatures and molar ratios of EC:Gly, fitting a kinetic model to all experimental data for the reaction catalyzed with Eversa Transform. This model included the bimolecular transesterification reaction of Gly and EC catalyzed by the lipase and a reversible ring-opening polymerization of EC.
Fil: Gutierrez Lazaro, Ana. Complutense University of Madrid; España
Fil: Velasco, Daniel. Complutense University of Madrid; España
Fil: Boldrini, Diego Emmanuel. 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: Yustos, Pedro. Complutense University of Madrid; España
Fil: Esteban, Jesús. Max Planck Institute for Chemical Energy Conversion. Molecular Catalysis Division; Alemania
Fil: Ladero, Miguel. 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
EVERSA TRANSFORM 2.0
GLYCEROL
GLYCEROL CARBONATE
KINETIC MODEL
LIPOZYME TL 100 L
NOVOZYM 435
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/90798
Acceder
id CONICETDig_0f906925268681362986169d1ce194f5
oai_identifier_str oai:ri.conicet.gov.ar:11336/90798
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Effect of operating variables and kinetics of the lipase catalyzed transesterification of ethylene carbonate and glycerolGutierrez Lazaro, AnaVelasco, DanielBoldrini, Diego EmmanuelYustos, PedroEsteban, JesúsLadero, MiguelEVERSA TRANSFORM 2.0GLYCEROLGLYCEROL CARBONATEKINETIC MODELLIPOZYME TL 100 LNOVOZYM 435https://purl.org/becyt/ford/2.4https://purl.org/becyt/ford/2Glycerol carbonate (GC) is a value-added product originating from the valorization of widely available glycerol (Gly), a side stream from the production of biodiesel. Here we approach the production of this chemical comparing two reactions based on the transesterification of Gly with dimethyl carbonate (DMC) and ethylene carbonate (EC). For the former reaction, it was observed that the free enzyme CALB (lipase B from Candida antarctica) gave the best results, whereas for the latter, Eversa Transform (a genetic modification of Thermomyces lanuginosus lipase) performed better than the rest. With the selected catalysts, their immobilized analogous enzymes Novozym 435 and Lypozyme TL IM, respectively, were also tested. Observing that the yields for the reaction with EC were significantly faster, other operating variables were evaluated, resulting the best performance using a closed system, tert-butanol as solvent, a concentration of enzyme Eversa Transform of 3 % w/w, a molar excess of EC:Gly of 9:1 and a temperature of 60 C. Finally, several runs were conducted at different temperatures and molar ratios of EC:Gly, fitting a kinetic model to all experimental data for the reaction catalyzed with Eversa Transform. This model included the bimolecular transesterification reaction of Gly and EC catalyzed by the lipase and a reversible ring-opening polymerization of EC.Fil: Gutierrez Lazaro, Ana. Complutense University of Madrid; EspañaFil: Velasco, Daniel. Complutense University of Madrid; EspañaFil: Boldrini, Diego Emmanuel. 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: Yustos, Pedro. Complutense University of Madrid; EspañaFil: Esteban, Jesús. Max Planck Institute for Chemical Energy Conversion. Molecular Catalysis Division; AlemaniaFil: Ladero, Miguel. 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; ArgentinaMDPI AG2018-09-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/90798Gutierrez Lazaro, Ana; Velasco, Daniel; Boldrini, Diego Emmanuel; Yustos, Pedro; Esteban, Jesús; et al.; Effect of operating variables and kinetics of the lipase catalyzed transesterification of ethylene carbonate and glycerol; MDPI AG; Fermentation; 4; 3; 5-9-2018; 1-142311-5637CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2311-5637/4/3/75info:eu-repo/semantics/altIdentifier/doi/10.3390/fermentation4030075info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-12-23T14:47:25Zoai:ri.conicet.gov.ar:11336/90798instacron: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:34982025-12-23 14:47:25.556CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Effect of operating variables and kinetics of the lipase catalyzed transesterification of ethylene carbonate and glycerol
title Effect of operating variables and kinetics of the lipase catalyzed transesterification of ethylene carbonate and glycerol
spellingShingle Effect of operating variables and kinetics of the lipase catalyzed transesterification of ethylene carbonate and glycerol
Gutierrez Lazaro, Ana
EVERSA TRANSFORM 2.0
GLYCEROL
GLYCEROL CARBONATE
KINETIC MODEL
LIPOZYME TL 100 L
NOVOZYM 435
title_short Effect of operating variables and kinetics of the lipase catalyzed transesterification of ethylene carbonate and glycerol
title_full Effect of operating variables and kinetics of the lipase catalyzed transesterification of ethylene carbonate and glycerol
title_fullStr Effect of operating variables and kinetics of the lipase catalyzed transesterification of ethylene carbonate and glycerol
title_full_unstemmed Effect of operating variables and kinetics of the lipase catalyzed transesterification of ethylene carbonate and glycerol
title_sort Effect of operating variables and kinetics of the lipase catalyzed transesterification of ethylene carbonate and glycerol
dc.creator.none.fl_str_mv Gutierrez Lazaro, Ana
Velasco, Daniel
Boldrini, Diego Emmanuel
Yustos, Pedro
Esteban, Jesús
Ladero, Miguel
author Gutierrez Lazaro, Ana
author_facet Gutierrez Lazaro, Ana
Velasco, Daniel
Boldrini, Diego Emmanuel
Yustos, Pedro
Esteban, Jesús
Ladero, Miguel
author_role author
author2 Velasco, Daniel
Boldrini, Diego Emmanuel
Yustos, Pedro
Esteban, Jesús
Ladero, Miguel
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv EVERSA TRANSFORM 2.0
GLYCEROL
GLYCEROL CARBONATE
KINETIC MODEL
LIPOZYME TL 100 L
NOVOZYM 435
topic EVERSA TRANSFORM 2.0
GLYCEROL
GLYCEROL CARBONATE
KINETIC MODEL
LIPOZYME TL 100 L
NOVOZYM 435
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Glycerol carbonate (GC) is a value-added product originating from the valorization of widely available glycerol (Gly), a side stream from the production of biodiesel. Here we approach the production of this chemical comparing two reactions based on the transesterification of Gly with dimethyl carbonate (DMC) and ethylene carbonate (EC). For the former reaction, it was observed that the free enzyme CALB (lipase B from Candida antarctica) gave the best results, whereas for the latter, Eversa Transform (a genetic modification of Thermomyces lanuginosus lipase) performed better than the rest. With the selected catalysts, their immobilized analogous enzymes Novozym 435 and Lypozyme TL IM, respectively, were also tested. Observing that the yields for the reaction with EC were significantly faster, other operating variables were evaluated, resulting the best performance using a closed system, tert-butanol as solvent, a concentration of enzyme Eversa Transform of 3 % w/w, a molar excess of EC:Gly of 9:1 and a temperature of 60 C. Finally, several runs were conducted at different temperatures and molar ratios of EC:Gly, fitting a kinetic model to all experimental data for the reaction catalyzed with Eversa Transform. This model included the bimolecular transesterification reaction of Gly and EC catalyzed by the lipase and a reversible ring-opening polymerization of EC.
Fil: Gutierrez Lazaro, Ana. Complutense University of Madrid; España
Fil: Velasco, Daniel. Complutense University of Madrid; España
Fil: Boldrini, Diego Emmanuel. 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: Yustos, Pedro. Complutense University of Madrid; España
Fil: Esteban, Jesús. Max Planck Institute for Chemical Energy Conversion. Molecular Catalysis Division; Alemania
Fil: Ladero, Miguel. 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 Glycerol carbonate (GC) is a value-added product originating from the valorization of widely available glycerol (Gly), a side stream from the production of biodiesel. Here we approach the production of this chemical comparing two reactions based on the transesterification of Gly with dimethyl carbonate (DMC) and ethylene carbonate (EC). For the former reaction, it was observed that the free enzyme CALB (lipase B from Candida antarctica) gave the best results, whereas for the latter, Eversa Transform (a genetic modification of Thermomyces lanuginosus lipase) performed better than the rest. With the selected catalysts, their immobilized analogous enzymes Novozym 435 and Lypozyme TL IM, respectively, were also tested. Observing that the yields for the reaction with EC were significantly faster, other operating variables were evaluated, resulting the best performance using a closed system, tert-butanol as solvent, a concentration of enzyme Eversa Transform of 3 % w/w, a molar excess of EC:Gly of 9:1 and a temperature of 60 C. Finally, several runs were conducted at different temperatures and molar ratios of EC:Gly, fitting a kinetic model to all experimental data for the reaction catalyzed with Eversa Transform. This model included the bimolecular transesterification reaction of Gly and EC catalyzed by the lipase and a reversible ring-opening polymerization of EC.
publishDate 2018
dc.date.none.fl_str_mv 2018-09-05
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/11336/90798
Gutierrez Lazaro, Ana; Velasco, Daniel; Boldrini, Diego Emmanuel; Yustos, Pedro; Esteban, Jesús; et al.; Effect of operating variables and kinetics of the lipase catalyzed transesterification of ethylene carbonate and glycerol; MDPI AG; Fermentation; 4; 3; 5-9-2018; 1-14
2311-5637
CONICET Digital
CONICET
url http://hdl.handle.net/11336/90798
identifier_str_mv Gutierrez Lazaro, Ana; Velasco, Daniel; Boldrini, Diego Emmanuel; Yustos, Pedro; Esteban, Jesús; et al.; Effect of operating variables and kinetics of the lipase catalyzed transesterification of ethylene carbonate and glycerol; MDPI AG; Fermentation; 4; 3; 5-9-2018; 1-14
2311-5637
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2311-5637/4/3/75
info:eu-repo/semantics/altIdentifier/doi/10.3390/fermentation4030075
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv MDPI AG
publisher.none.fl_str_mv MDPI AG
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
_version_ 1852335823455780864
score 12.952241

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