A kinetic study of the lipase-catalyzed ethanolysis of two short-chain triradylglycerols: Alkylglycerols vs. triacylglycerols

This is the author’s version of a work that was accepted for publication in Journal of Molecular Catalysis B: Enzymatic. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this...

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Published in:Journal of Molecular Catalysis B: Enzymatic
Main Authors: Vázquez, Luis Nuñez, Fernández, Óscar, Blanco, Rosa María, Señoráns Rodríguez, Francisco Javier, Reglero, Guillermo, Torres, Carlos F.
Other Authors: UAM. Departamento de Química Física Aplicada
Format: Article in Journal/Newspaper
Language:English
Published: Elsevier B.V 2014
Subjects:
Online Access:http://hdl.handle.net/10486/660725
https://doi.org/10.1016/j.molcatb.2010.02.010
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spelling ftuamadrid:oai:repositorio.uam.es:10486/660725 2023-05-15T13:44:50+02:00 A kinetic study of the lipase-catalyzed ethanolysis of two short-chain triradylglycerols: Alkylglycerols vs. triacylglycerols Vázquez, Luis Nuñez Fernández, Óscar Blanco, Rosa María Señoráns Rodríguez, Francisco Javier Reglero, Guillermo Torres, Carlos F. UAM. Departamento de Química Física Aplicada 2014-07-08T11:59:05Z application/pdf http://hdl.handle.net/10486/660725 https://doi.org/10.1016/j.molcatb.2010.02.010 eng eng Elsevier B.V Journal of Molecular Catalysis B: Enzymatic http://dx.doi.org/10.1016/j.molcatb.2010.02.010 Comunidad de Madrid. S2009/AGR-1469/ALIBIRD Journal of Molecular Catalysis B: Enzymatic 64.1-2 (2010): 101–106 1381-1177 (print) 1873-3158 (online) http://hdl.handle.net/10486/660725 doi:10.1016/j.molcatb.2010.02.010 101 1-2 106 64 © 2010 Elsevier B.V. All rights reserved. Reconocimiento – NoComercial – SinObraDerivada openAccess Alkylglycerols Butyric Kinetics model Candida antarctica Ethanolysis Lipase Química article info:eu-repo/semantics/acceptedVersion 2014 ftuamadrid https://doi.org/10.1016/j.molcatb.2010.02.010 2022-05-10T23:14:54Z This is the author’s version of a work that was accepted for publication in Journal of Molecular Catalysis B: Enzymatic. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Molecular Catalysis B: Enzymatic, 64, (2010) DOI 10.1016/j.molcatb.2010.02.010 Lipase-catalyzed ethanolysis of two short-chain triradylglycerols, namely tributyrin and 2,3-dibutyroil- 1-O-alkylglycerols, have been studied. Much faster rate of reaction for the ethanolysis of tributyrin than that of 2,3-dibutyroil-1-O-alkylglycerols was attained. A kinetic model for the rate of release of ethyl butyrate and for the inactivation of the lipase has been also studied. The parameter corresponding to the release of ethyl butyrate was one order of magnitude higher for ethanolysis of tributyrin than the corresponding of 2,3-dibutyroil-1-O-alkylglycerols. On the contrary, the stability of Novozym 435 during ethanolysis of 2,3-dibutyroil-1-O-alkylglycerols was higher than the corresponding of tributyrin. At the reaction conditions under study, both ethanolysis reactions take place with high selectivity and yield monoesterified alkylglycerols and sn-2 monobutyrin as the main acylglycerols in the reaction mixtures. This work was supported by the projects AGL2006-02031/ALI and AGL2008-05655 by Ministerio de Ciencia (Spain) and also by Comunidad Autonoma de Madrid (ALIBIRD, project number S-505/AGR-0153) and Consolider-Ingenio FUN-C-FOOD (CSD2007- 00063). Article in Journal/Newspaper Antarc* Antarctica Universidad Autónoma de Madrid (UAM): Biblos-e Archivo Journal of Molecular Catalysis B: Enzymatic 64 1-2 101 106
institution Open Polar
collection Universidad Autónoma de Madrid (UAM): Biblos-e Archivo
op_collection_id ftuamadrid
language English
topic Alkylglycerols
Butyric
Kinetics model
Candida antarctica
Ethanolysis
Lipase
Química
spellingShingle Alkylglycerols
Butyric
Kinetics model
Candida antarctica
Ethanolysis
Lipase
Química
Vázquez, Luis Nuñez
Fernández, Óscar
Blanco, Rosa María
Señoráns Rodríguez, Francisco Javier
Reglero, Guillermo
Torres, Carlos F.
A kinetic study of the lipase-catalyzed ethanolysis of two short-chain triradylglycerols: Alkylglycerols vs. triacylglycerols
topic_facet Alkylglycerols
Butyric
Kinetics model
Candida antarctica
Ethanolysis
Lipase
Química
description This is the author’s version of a work that was accepted for publication in Journal of Molecular Catalysis B: Enzymatic. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Molecular Catalysis B: Enzymatic, 64, (2010) DOI 10.1016/j.molcatb.2010.02.010 Lipase-catalyzed ethanolysis of two short-chain triradylglycerols, namely tributyrin and 2,3-dibutyroil- 1-O-alkylglycerols, have been studied. Much faster rate of reaction for the ethanolysis of tributyrin than that of 2,3-dibutyroil-1-O-alkylglycerols was attained. A kinetic model for the rate of release of ethyl butyrate and for the inactivation of the lipase has been also studied. The parameter corresponding to the release of ethyl butyrate was one order of magnitude higher for ethanolysis of tributyrin than the corresponding of 2,3-dibutyroil-1-O-alkylglycerols. On the contrary, the stability of Novozym 435 during ethanolysis of 2,3-dibutyroil-1-O-alkylglycerols was higher than the corresponding of tributyrin. At the reaction conditions under study, both ethanolysis reactions take place with high selectivity and yield monoesterified alkylglycerols and sn-2 monobutyrin as the main acylglycerols in the reaction mixtures. This work was supported by the projects AGL2006-02031/ALI and AGL2008-05655 by Ministerio de Ciencia (Spain) and also by Comunidad Autonoma de Madrid (ALIBIRD, project number S-505/AGR-0153) and Consolider-Ingenio FUN-C-FOOD (CSD2007- 00063).
author2 UAM. Departamento de Química Física Aplicada
format Article in Journal/Newspaper
author Vázquez, Luis Nuñez
Fernández, Óscar
Blanco, Rosa María
Señoráns Rodríguez, Francisco Javier
Reglero, Guillermo
Torres, Carlos F.
author_facet Vázquez, Luis Nuñez
Fernández, Óscar
Blanco, Rosa María
Señoráns Rodríguez, Francisco Javier
Reglero, Guillermo
Torres, Carlos F.
author_sort Vázquez, Luis Nuñez
title A kinetic study of the lipase-catalyzed ethanolysis of two short-chain triradylglycerols: Alkylglycerols vs. triacylglycerols
title_short A kinetic study of the lipase-catalyzed ethanolysis of two short-chain triradylglycerols: Alkylglycerols vs. triacylglycerols
title_full A kinetic study of the lipase-catalyzed ethanolysis of two short-chain triradylglycerols: Alkylglycerols vs. triacylglycerols
title_fullStr A kinetic study of the lipase-catalyzed ethanolysis of two short-chain triradylglycerols: Alkylglycerols vs. triacylglycerols
title_full_unstemmed A kinetic study of the lipase-catalyzed ethanolysis of two short-chain triradylglycerols: Alkylglycerols vs. triacylglycerols
title_sort kinetic study of the lipase-catalyzed ethanolysis of two short-chain triradylglycerols: alkylglycerols vs. triacylglycerols
publisher Elsevier B.V
publishDate 2014
url http://hdl.handle.net/10486/660725
https://doi.org/10.1016/j.molcatb.2010.02.010
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_relation Journal of Molecular Catalysis B: Enzymatic
http://dx.doi.org/10.1016/j.molcatb.2010.02.010
Comunidad de Madrid. S2009/AGR-1469/ALIBIRD
Journal of Molecular Catalysis B: Enzymatic 64.1-2 (2010): 101–106
1381-1177 (print)
1873-3158 (online)
http://hdl.handle.net/10486/660725
doi:10.1016/j.molcatb.2010.02.010
101
1-2
106
64
op_rights © 2010 Elsevier B.V. All rights reserved.
Reconocimiento – NoComercial – SinObraDerivada
openAccess
op_doi https://doi.org/10.1016/j.molcatb.2010.02.010
container_title Journal of Molecular Catalysis B: Enzymatic
container_volume 64
container_issue 1-2
container_start_page 101
op_container_end_page 106
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