Influence of Water on Enzymatic Esterification of Racemic Ketoprofen with Ethanol in a Solvent-Free System
The effect of water added in the kinetic resolution of rac-ketoprofen with ethanol catalyzed with Candida antarctica lipase B was investigated under reaction conditions and at a molecular level. The reaction was performed at 45 oC for 24 h with the commercial biocatalyst known as Novozym 435. The a...
Published in: | Topics in Catalysis |
---|---|
Main Authors: | , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Springer/Plenum Publishers
|
Subjects: | |
Online Access: | http://hdl.handle.net/11336/107896 |
id |
ftconicet:oai:ri.conicet.gov.ar:11336/107896 |
---|---|
record_format |
openpolar |
spelling |
ftconicet:oai:ri.conicet.gov.ar:11336/107896 2023-10-09T21:45:45+02:00 Influence of Water on Enzymatic Esterification of Racemic Ketoprofen with Ethanol in a Solvent-Free System Toledo, Victoria Llerena Suster, Carlos Rafael Ruscitti, Claudia Beatriz Collins, Sebastián Enrique Briand, Laura Estefania application/pdf http://hdl.handle.net/11336/107896 eng eng Springer/Plenum Publishers info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/content/pdf/10.1007%2Fs11244-019-01184-z.pdf info:eu-repo/semantics/altIdentifier/doi/10.1007/s11244-019-01184-z http://hdl.handle.net/11336/107896 Toledo, Victoria; Llerena Suster, Carlos Rafael; Ruscitti, Claudia Beatriz; Collins, Sebastián Enrique; Briand, Laura Estefania; Influence of Water on Enzymatic Esterification of Racemic Ketoprofen with Ethanol in a Solvent-Free System; Springer/Plenum Publishers; Topics In Catalysis; 62; 12; 5-2019; 968-976 1022-5528 CONICET Digital CONICET info:eu-repo/semantics/restrictedAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ ENZYMATIC FEXIBILITY ENZYMES H/D ISOTOPIC EXCHANGE CANDIDA ANTARCTICA LIPASE B https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion ftconicet https://doi.org/10.1007/s11244-019-01184-z 2023-09-24T19:18:45Z The effect of water added in the kinetic resolution of rac-ketoprofen with ethanol catalyzed with Candida antarctica lipase B was investigated under reaction conditions and at a molecular level. The reaction was performed at 45 oC for 24 h with the commercial biocatalyst known as Novozym 435. The addition of water from 0.5 to 10 % v/v to the reaction medium enhances the specific activity (from 2 to 4 micromol.mg-1.h^-1), enantiomeric ratio E (1 towards 5), enantiomeric factor EF (0.1 towards 0.5) and the enantiomeric excess towards dexketoprofen (above 50%). At a molecular level, the rate of H/D isotopic exchange of the amide hydrogen of the lipase B of Candida antarctica demonstrated that the enzyme exposed to dehydrated ethanol possesses highly flexible sites (45% of the sites are exchanged with a rate of 30 min^-1) and the addition of water diminishes the rate of H/D exchange altering the flexibility (the exchange rate falls down to 2.7 - 0.06 min^-1). Additional studies on the secondary structure suggest that the beta-sheet structure lead to slowest exchange H-amide sites. Fil: Toledo, Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas "Dr. Jorge J. Ronco". Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Ciencias Aplicadas; Argentina Fil: Llerena Suster, Carlos Rafael. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina Fil: Ruscitti, Claudia Beatriz. Universidad Nacional de La Plata; Argentina Fil: Collins, Sebastián Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina Fil: ... Article in Journal/Newspaper Antarc* Antarctica CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Argentina Toledo ENVELOPE(-67.317,-67.317,-73.700,-73.700) Topics in Catalysis 62 12-16 968 976 |
institution |
Open Polar |
collection |
CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) |
op_collection_id |
ftconicet |
language |
English |
topic |
ENZYMATIC FEXIBILITY ENZYMES H/D ISOTOPIC EXCHANGE CANDIDA ANTARCTICA LIPASE B https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 |
spellingShingle |
ENZYMATIC FEXIBILITY ENZYMES H/D ISOTOPIC EXCHANGE CANDIDA ANTARCTICA LIPASE B https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 Toledo, Victoria Llerena Suster, Carlos Rafael Ruscitti, Claudia Beatriz Collins, Sebastián Enrique Briand, Laura Estefania Influence of Water on Enzymatic Esterification of Racemic Ketoprofen with Ethanol in a Solvent-Free System |
topic_facet |
ENZYMATIC FEXIBILITY ENZYMES H/D ISOTOPIC EXCHANGE CANDIDA ANTARCTICA LIPASE B https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 |
description |
The effect of water added in the kinetic resolution of rac-ketoprofen with ethanol catalyzed with Candida antarctica lipase B was investigated under reaction conditions and at a molecular level. The reaction was performed at 45 oC for 24 h with the commercial biocatalyst known as Novozym 435. The addition of water from 0.5 to 10 % v/v to the reaction medium enhances the specific activity (from 2 to 4 micromol.mg-1.h^-1), enantiomeric ratio E (1 towards 5), enantiomeric factor EF (0.1 towards 0.5) and the enantiomeric excess towards dexketoprofen (above 50%). At a molecular level, the rate of H/D isotopic exchange of the amide hydrogen of the lipase B of Candida antarctica demonstrated that the enzyme exposed to dehydrated ethanol possesses highly flexible sites (45% of the sites are exchanged with a rate of 30 min^-1) and the addition of water diminishes the rate of H/D exchange altering the flexibility (the exchange rate falls down to 2.7 - 0.06 min^-1). Additional studies on the secondary structure suggest that the beta-sheet structure lead to slowest exchange H-amide sites. Fil: Toledo, Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Ciencias Aplicadas "Dr. Jorge J. Ronco". Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Ciencias Aplicadas; Argentina Fil: Llerena Suster, Carlos Rafael. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina Fil: Ruscitti, Claudia Beatriz. Universidad Nacional de La Plata; Argentina Fil: Collins, Sebastián Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina Fil: ... |
format |
Article in Journal/Newspaper |
author |
Toledo, Victoria Llerena Suster, Carlos Rafael Ruscitti, Claudia Beatriz Collins, Sebastián Enrique Briand, Laura Estefania |
author_facet |
Toledo, Victoria Llerena Suster, Carlos Rafael Ruscitti, Claudia Beatriz Collins, Sebastián Enrique Briand, Laura Estefania |
author_sort |
Toledo, Victoria |
title |
Influence of Water on Enzymatic Esterification of Racemic Ketoprofen with Ethanol in a Solvent-Free System |
title_short |
Influence of Water on Enzymatic Esterification of Racemic Ketoprofen with Ethanol in a Solvent-Free System |
title_full |
Influence of Water on Enzymatic Esterification of Racemic Ketoprofen with Ethanol in a Solvent-Free System |
title_fullStr |
Influence of Water on Enzymatic Esterification of Racemic Ketoprofen with Ethanol in a Solvent-Free System |
title_full_unstemmed |
Influence of Water on Enzymatic Esterification of Racemic Ketoprofen with Ethanol in a Solvent-Free System |
title_sort |
influence of water on enzymatic esterification of racemic ketoprofen with ethanol in a solvent-free system |
publisher |
Springer/Plenum Publishers |
url |
http://hdl.handle.net/11336/107896 |
long_lat |
ENVELOPE(-67.317,-67.317,-73.700,-73.700) |
geographic |
Argentina Toledo |
geographic_facet |
Argentina Toledo |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/content/pdf/10.1007%2Fs11244-019-01184-z.pdf info:eu-repo/semantics/altIdentifier/doi/10.1007/s11244-019-01184-z http://hdl.handle.net/11336/107896 Toledo, Victoria; Llerena Suster, Carlos Rafael; Ruscitti, Claudia Beatriz; Collins, Sebastián Enrique; Briand, Laura Estefania; Influence of Water on Enzymatic Esterification of Racemic Ketoprofen with Ethanol in a Solvent-Free System; Springer/Plenum Publishers; Topics In Catalysis; 62; 12; 5-2019; 968-976 1022-5528 CONICET Digital CONICET |
op_rights |
info:eu-repo/semantics/restrictedAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
op_doi |
https://doi.org/10.1007/s11244-019-01184-z |
container_title |
Topics in Catalysis |
container_volume |
62 |
container_issue |
12-16 |
container_start_page |
968 |
op_container_end_page |
976 |
_version_ |
1779321408724140032 |