Effect of Operating Variables and Kinetics of the Lipase Catalyzed Transesterification of Ethylene Carbonate and Glycerol

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 carbon...

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Detalles Bibliográficos
Autores: Gutiérrez Lázaro, Ana, Velasco Conde, Daniel, Boldrini, Diego, Yustos Cuesta, Pedro, Esteban, Jesus, Ladero Galán, Miguel
Tipo de recurso: artículo
Fecha de publicación:2018
País:España
Institución:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:inglés
OAI Identifier:oai:docta.ucm.es:20.500.14352/12602
Acceso en línea:https://hdl.handle.net/20.500.14352/12602
Access Level:acceso abierto
Palabra clave:glycerol
glycerol carbonate
Novozym 435
Lipozyme TL 100 L
Eversa Transform 2.0
kinetic model
Ingeniería química
Materiales
3303 Ingeniería y Tecnología Químicas
3312 Tecnología de Materiales
id ES_730d184776eae4e59fc94f85a46c6eeb
oai_identifier_str oai:docta.ucm.es:20.500.14352/12602
network_acronym_str ES
network_name_str España
repository_id_str
spelling Effect of Operating Variables and Kinetics of the Lipase Catalyzed Transesterification of Ethylene Carbonate and GlycerolGutiérrez Lázaro, AnaVelasco Conde, DanielBoldrini, DiegoYustos Cuesta, PedroEsteban, JesusLadero Galán, Miguelglycerolglycerol carbonateNovozym 435Lipozyme TL 100 LEversa Transform 2.0kinetic modelIngeniería químicaMateriales3303 Ingeniería y Tecnología Químicas3312 Tecnología de MaterialesGlycerol 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). When using DMC, it was observed that the free enzyme CALB (lipase B from Candida antarctica) gave the best results, whereas Eversa Transform (a genetic modification of Thermomyces lanuginosus lipase) performed better than the rest if EC was the reagent. 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.MDPIUniversidad Complutense de Madrid20182018-09-0520182018-09-05journal articlehttp://purl.org/coar/resource_type/c_6501info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/12602reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Atribución 3.0 Españahttps://creativecommons.org/licenses/by/3.0/es/info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/126022026-06-02T12:44:21Z
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
Gutiérrez Lázaro, Ana
glycerol
glycerol carbonate
Novozym 435
Lipozyme TL 100 L
Eversa Transform 2.0
kinetic model
Ingeniería química
Materiales
3303 Ingeniería y Tecnología Químicas
3312 Tecnología de Materiales
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 Gutiérrez Lázaro, Ana
Velasco Conde, Daniel
Boldrini, Diego
Yustos Cuesta, Pedro
Esteban, Jesus
Ladero Galán, Miguel
author Gutiérrez Lázaro, Ana
author_facet Gutiérrez Lázaro, Ana
Velasco Conde, Daniel
Boldrini, Diego
Yustos Cuesta, Pedro
Esteban, Jesus
Ladero Galán, Miguel
author_role author
author2 Velasco Conde, Daniel
Boldrini, Diego
Yustos Cuesta, Pedro
Esteban, Jesus
Ladero Galán, Miguel
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv glycerol
glycerol carbonate
Novozym 435
Lipozyme TL 100 L
Eversa Transform 2.0
kinetic model
Ingeniería química
Materiales
3303 Ingeniería y Tecnología Químicas
3312 Tecnología de Materiales
topic glycerol
glycerol carbonate
Novozym 435
Lipozyme TL 100 L
Eversa Transform 2.0
kinetic model
Ingeniería química
Materiales
3303 Ingeniería y Tecnología Químicas
3312 Tecnología de Materiales
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). When using DMC, it was observed that the free enzyme CALB (lipase B from Candida antarctica) gave the best results, whereas Eversa Transform (a genetic modification of Thermomyces lanuginosus lipase) performed better than the rest if EC was the reagent. 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
2018-09-05
2018
2018-09-05
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.14352/12602
url https://hdl.handle.net/20.500.14352/12602
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Atribución 3.0 España
https://creativecommons.org/licenses/by/3.0/es/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Atribución 3.0 España
https://creativecommons.org/licenses/by/3.0/es/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:Docta Complutense
instname:Universidad Complutense de Madrid (UCM)
instname_str Universidad Complutense de Madrid (UCM)
reponame_str Docta Complutense
collection Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869410780807430144
score 15.300724

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