Lipase-catalyzed transesterification in organic media: solvent effects on equilibrium and individual rate constants.

International audience The kinetics of the immobilized lipase B from Candida antarctica have been studied in organic solvents. This enzyme has been shown to be slightly affected by the water content of the organic media, and it does not seem to be subject to mass transfer limitations. On the other h...

Full description

Bibliographic Details
Main Authors: García-Alles, L, Gotor, V
Other Authors: Universidad de Oviedo
Format: Article in Journal/Newspaper
Language:English
Published: HAL CCSD 1998
Subjects:
Online Access:https://hal.insa-toulouse.fr/hal-03367179
id ftccsdartic:oai:HAL:hal-03367179v1
record_format openpolar
spelling ftccsdartic:oai:HAL:hal-03367179v1 2023-05-15T13:58:32+02:00 Lipase-catalyzed transesterification in organic media: solvent effects on equilibrium and individual rate constants. García-Alles, L Gotor, V Universidad de Oviedo 1998-09-20 https://hal.insa-toulouse.fr/hal-03367179 en eng HAL CCSD Wiley info:eu-repo/semantics/altIdentifier/pmid/10099389 hal-03367179 https://hal.insa-toulouse.fr/hal-03367179 PUBMED: 10099389 ISSN: 0006-3592 EISSN: 1097-0290 Biotechnology and Bioengineering https://hal.insa-toulouse.fr/hal-03367179 Biotechnology and Bioengineering, Wiley, 1998, 59 (6), pp.684-94 MESH: 1-Butanol MESH: Acylation MESH: Lipase MESH: Solvents MESH: Water MESH: Binding Sites MESH: Candida MESH: Catalysis MESH: Chemistry Organic MESH: Diffusion MESH: Esterification MESH: Ethanol MESH: Kinetics [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology [SDV.BIO]Life Sciences [q-bio]/Biotechnology info:eu-repo/semantics/article Journal articles 1998 ftccsdartic 2021-10-09T22:22:10Z International audience The kinetics of the immobilized lipase B from Candida antarctica have been studied in organic solvents. This enzyme has been shown to be slightly affected by the water content of the organic media, and it does not seem to be subject to mass transfer limitations. On the other hand, some evidence indicates that the catalytic mechanism of reactions catalyzed by this lipase proceeds through the acyl-enzyme intermediate. Moreover, despite the fact that the immobilization support dramatically enhances the catalytic power of the enzyme, it does not interfere with the intrinsic solvent effect. Consequently, this enzyme preparation becomes optimum for studying the role played by the organic solvent in catalysis. To this end, we have measured the acylation and deacylation individual rate constants, and the binding equilibrium constant for the ester, in several organic environments. Data obtained show that the major effect of the organic solvent is on substrate binding, and that the catalytic steps are almost unaffected by the solvent, indicating the desolvation of the transition state. However, the strong decrease in binding for hydrophilic solvents such as THF and dioxane, compared to the rest of solvents, cannot be easily explained by means of thermodynamic arguments (desolvation of the ester substrate). For this reason, data have been considered as an indication of the existence of an unknown step in the catalytic pathway occurring prior to formation of the acyl-enzyme intermediate. Article in Journal/Newspaper Antarc* Antarctica Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe)
institution Open Polar
collection Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe)
op_collection_id ftccsdartic
language English
topic MESH: 1-Butanol
MESH: Acylation
MESH: Lipase
MESH: Solvents
MESH: Water
MESH: Binding Sites
MESH: Candida
MESH: Catalysis
MESH: Chemistry
Organic
MESH: Diffusion
MESH: Esterification
MESH: Ethanol
MESH: Kinetics
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
[SDV.BIO]Life Sciences [q-bio]/Biotechnology
spellingShingle MESH: 1-Butanol
MESH: Acylation
MESH: Lipase
MESH: Solvents
MESH: Water
MESH: Binding Sites
MESH: Candida
MESH: Catalysis
MESH: Chemistry
Organic
MESH: Diffusion
MESH: Esterification
MESH: Ethanol
MESH: Kinetics
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
[SDV.BIO]Life Sciences [q-bio]/Biotechnology
García-Alles, L
Gotor, V
Lipase-catalyzed transesterification in organic media: solvent effects on equilibrium and individual rate constants.
topic_facet MESH: 1-Butanol
MESH: Acylation
MESH: Lipase
MESH: Solvents
MESH: Water
MESH: Binding Sites
MESH: Candida
MESH: Catalysis
MESH: Chemistry
Organic
MESH: Diffusion
MESH: Esterification
MESH: Ethanol
MESH: Kinetics
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
[SDV.BIO]Life Sciences [q-bio]/Biotechnology
description International audience The kinetics of the immobilized lipase B from Candida antarctica have been studied in organic solvents. This enzyme has been shown to be slightly affected by the water content of the organic media, and it does not seem to be subject to mass transfer limitations. On the other hand, some evidence indicates that the catalytic mechanism of reactions catalyzed by this lipase proceeds through the acyl-enzyme intermediate. Moreover, despite the fact that the immobilization support dramatically enhances the catalytic power of the enzyme, it does not interfere with the intrinsic solvent effect. Consequently, this enzyme preparation becomes optimum for studying the role played by the organic solvent in catalysis. To this end, we have measured the acylation and deacylation individual rate constants, and the binding equilibrium constant for the ester, in several organic environments. Data obtained show that the major effect of the organic solvent is on substrate binding, and that the catalytic steps are almost unaffected by the solvent, indicating the desolvation of the transition state. However, the strong decrease in binding for hydrophilic solvents such as THF and dioxane, compared to the rest of solvents, cannot be easily explained by means of thermodynamic arguments (desolvation of the ester substrate). For this reason, data have been considered as an indication of the existence of an unknown step in the catalytic pathway occurring prior to formation of the acyl-enzyme intermediate.
author2 Universidad de Oviedo
format Article in Journal/Newspaper
author García-Alles, L
Gotor, V
author_facet García-Alles, L
Gotor, V
author_sort García-Alles, L
title Lipase-catalyzed transesterification in organic media: solvent effects on equilibrium and individual rate constants.
title_short Lipase-catalyzed transesterification in organic media: solvent effects on equilibrium and individual rate constants.
title_full Lipase-catalyzed transesterification in organic media: solvent effects on equilibrium and individual rate constants.
title_fullStr Lipase-catalyzed transesterification in organic media: solvent effects on equilibrium and individual rate constants.
title_full_unstemmed Lipase-catalyzed transesterification in organic media: solvent effects on equilibrium and individual rate constants.
title_sort lipase-catalyzed transesterification in organic media: solvent effects on equilibrium and individual rate constants.
publisher HAL CCSD
publishDate 1998
url https://hal.insa-toulouse.fr/hal-03367179
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source ISSN: 0006-3592
EISSN: 1097-0290
Biotechnology and Bioengineering
https://hal.insa-toulouse.fr/hal-03367179
Biotechnology and Bioengineering, Wiley, 1998, 59 (6), pp.684-94
op_relation info:eu-repo/semantics/altIdentifier/pmid/10099389
hal-03367179
https://hal.insa-toulouse.fr/hal-03367179
PUBMED: 10099389
_version_ 1766266880119537664