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...
Published in: | Journal of Molecular Catalysis B: Enzymatic |
---|---|
Main Authors: | , , , , , |
Other Authors: | |
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 |
id |
ftuamadrid:oai:repositorio.uam.es:10486/660725 |
---|---|
record_format |
openpolar |
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 |
_version_ |
1766207322710867968 |