Solid/gas biocatalysis: an appropriate tool to study the influence of organic components on kinetics of lipase-catalyzed alcoholysis
International audience The influence of the addition of an extra component in a gaseous reaction medium, on the kinetics of alcoholysis of methyl propionate and n-propanol catalyzed by immobilized lipase B from Candida antarctica was studied in a continuous solid/gas reactor. In this reactor, the so...
Published in: | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics |
---|---|
Main Authors: | , , , |
Other Authors: | , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
HAL CCSD
2003
|
Subjects: | |
Online Access: | https://hal.insa-toulouse.fr/hal-02183212 https://doi.org/10.1016/s1570-9639(03)00262-0 |
id |
ftccsdartic:oai:HAL:hal-02183212v1 |
---|---|
record_format |
openpolar |
spelling |
ftccsdartic:oai:HAL:hal-02183212v1 2023-05-15T13:52:30+02:00 Solid/gas biocatalysis: an appropriate tool to study the influence of organic components on kinetics of lipase-catalyzed alcoholysis Letisse, Fabien Lamare, Sylvain Legoy, Marie-Dominique Graber, Marianne Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP) Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse) Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA) LIttoral ENvironnement et Sociétés - UMRi 7266 (LIENSs) Université de La Rochelle (ULR)-Centre National de la Recherche Scientifique (CNRS) 2003-11 https://hal.insa-toulouse.fr/hal-02183212 https://doi.org/10.1016/s1570-9639(03)00262-0 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/s1570-9639(03)00262-0 hal-02183212 https://hal.insa-toulouse.fr/hal-02183212 doi:10.1016/s1570-9639(03)00262-0 ISSN: 1570-9639 Biochimica et Biophysica Acta Proteins and Proteomics https://hal.insa-toulouse.fr/hal-02183212 Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2003, 1652 (1), pp.27-34. ⟨10.1016/s1570-9639(03)00262-0⟩ Lipase B from Candida antarctica Kinetics Transesterification Organic solvent Diffusional limitation Solid/gas biocatalysis [SDV]Life Sciences [q-bio] info:eu-repo/semantics/article Journal articles 2003 ftccsdartic https://doi.org/10.1016/s1570-9639(03)00262-0 2021-10-24T04:09:48Z International audience The influence of the addition of an extra component in a gaseous reaction medium, on the kinetics of alcoholysis of methyl propionate and n-propanol catalyzed by immobilized lipase B from Candida antarctica was studied in a continuous solid/gas reactor. In this reactor, the solid phase is composed of a packed enzymatic sample, which is percolated by gaseous nitrogen, simultaneously carrying gaseous substrates and additional components to the enzyme while removing reaction products. The system permits to set thermodynamic activity of all gaseous components (substrates or not) independently at the desired values. This allows in particular to study the influence of an extra added component at a constant thermodynamic activity value, contrary to classical solid/liquid system, which involves large variations of thermodynamic activity of added solvent, when performing full kinetic studies. Alcohol inhibition constant (K(I)) and methyl propionate and propanol dissociation constants (K(MP) and K(P)) have been determined in the solid/gas reactor in the presence of 2-methyl-2-butanol, and compared with values previously obtained in the absence of added component and in the presence of water. Complementary experiments were carried out in the presence of an apolar compound (hexane) and led to the conclusion that the effect of added organic component on lipase-catalyzed alcoholysis is related to their competitive inhibitory character towards first substrate methyl propionate. The comparison of data obtained in liquid or with gaseous 2-methyl-2-butanol shows that lower K(MP) and K(I) are found in gaseous medium, which would correspond on the one hand to a lower acylation rate k(2), and on the other hand to a higher binding rate k(1) between substrate and free enzyme in gaseous medium. Article in Journal/Newspaper Antarc* Antarctica Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1652 1 27 34 |
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 |
Lipase B from Candida antarctica Kinetics Transesterification Organic solvent Diffusional limitation Solid/gas biocatalysis [SDV]Life Sciences [q-bio] |
spellingShingle |
Lipase B from Candida antarctica Kinetics Transesterification Organic solvent Diffusional limitation Solid/gas biocatalysis [SDV]Life Sciences [q-bio] Letisse, Fabien Lamare, Sylvain Legoy, Marie-Dominique Graber, Marianne Solid/gas biocatalysis: an appropriate tool to study the influence of organic components on kinetics of lipase-catalyzed alcoholysis |
topic_facet |
Lipase B from Candida antarctica Kinetics Transesterification Organic solvent Diffusional limitation Solid/gas biocatalysis [SDV]Life Sciences [q-bio] |
description |
International audience The influence of the addition of an extra component in a gaseous reaction medium, on the kinetics of alcoholysis of methyl propionate and n-propanol catalyzed by immobilized lipase B from Candida antarctica was studied in a continuous solid/gas reactor. In this reactor, the solid phase is composed of a packed enzymatic sample, which is percolated by gaseous nitrogen, simultaneously carrying gaseous substrates and additional components to the enzyme while removing reaction products. The system permits to set thermodynamic activity of all gaseous components (substrates or not) independently at the desired values. This allows in particular to study the influence of an extra added component at a constant thermodynamic activity value, contrary to classical solid/liquid system, which involves large variations of thermodynamic activity of added solvent, when performing full kinetic studies. Alcohol inhibition constant (K(I)) and methyl propionate and propanol dissociation constants (K(MP) and K(P)) have been determined in the solid/gas reactor in the presence of 2-methyl-2-butanol, and compared with values previously obtained in the absence of added component and in the presence of water. Complementary experiments were carried out in the presence of an apolar compound (hexane) and led to the conclusion that the effect of added organic component on lipase-catalyzed alcoholysis is related to their competitive inhibitory character towards first substrate methyl propionate. The comparison of data obtained in liquid or with gaseous 2-methyl-2-butanol shows that lower K(MP) and K(I) are found in gaseous medium, which would correspond on the one hand to a lower acylation rate k(2), and on the other hand to a higher binding rate k(1) between substrate and free enzyme in gaseous medium. |
author2 |
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP) Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse) Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA) LIttoral ENvironnement et Sociétés - UMRi 7266 (LIENSs) Université de La Rochelle (ULR)-Centre National de la Recherche Scientifique (CNRS) |
format |
Article in Journal/Newspaper |
author |
Letisse, Fabien Lamare, Sylvain Legoy, Marie-Dominique Graber, Marianne |
author_facet |
Letisse, Fabien Lamare, Sylvain Legoy, Marie-Dominique Graber, Marianne |
author_sort |
Letisse, Fabien |
title |
Solid/gas biocatalysis: an appropriate tool to study the influence of organic components on kinetics of lipase-catalyzed alcoholysis |
title_short |
Solid/gas biocatalysis: an appropriate tool to study the influence of organic components on kinetics of lipase-catalyzed alcoholysis |
title_full |
Solid/gas biocatalysis: an appropriate tool to study the influence of organic components on kinetics of lipase-catalyzed alcoholysis |
title_fullStr |
Solid/gas biocatalysis: an appropriate tool to study the influence of organic components on kinetics of lipase-catalyzed alcoholysis |
title_full_unstemmed |
Solid/gas biocatalysis: an appropriate tool to study the influence of organic components on kinetics of lipase-catalyzed alcoholysis |
title_sort |
solid/gas biocatalysis: an appropriate tool to study the influence of organic components on kinetics of lipase-catalyzed alcoholysis |
publisher |
HAL CCSD |
publishDate |
2003 |
url |
https://hal.insa-toulouse.fr/hal-02183212 https://doi.org/10.1016/s1570-9639(03)00262-0 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ISSN: 1570-9639 Biochimica et Biophysica Acta Proteins and Proteomics https://hal.insa-toulouse.fr/hal-02183212 Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2003, 1652 (1), pp.27-34. ⟨10.1016/s1570-9639(03)00262-0⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/s1570-9639(03)00262-0 hal-02183212 https://hal.insa-toulouse.fr/hal-02183212 doi:10.1016/s1570-9639(03)00262-0 |
op_doi |
https://doi.org/10.1016/s1570-9639(03)00262-0 |
container_title |
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics |
container_volume |
1652 |
container_issue |
1 |
container_start_page |
27 |
op_container_end_page |
34 |
_version_ |
1766256793647841280 |