Non-covalent and covalent immobilization of Candida antarctica Lipase B on chemically modified multiwalled carbon nanotubes for a green acylation process in supercritical CO2
International audience Candida antarctica B lipase (CAL-B) was immobilized on purified and functionalized multiwalled carbon nanotubes (MWCNTs). Both immobilization routes, physical adsorption and covalent bonding, were investigated. MWCNT functionalization by a non-aggressive oxidation by potassium...
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ftccsdartic:oai:HAL:hal-02612257v1 2023-05-15T13:53:12+02:00 Non-covalent and covalent immobilization of Candida antarctica Lipase B on chemically modified multiwalled carbon nanotubes for a green acylation process in supercritical CO2 Bourkaib, Mohamed Chafik Guiavarc’h, Yann Chevalot, Isabelle Delaunay, Stéphane Gleize, Jerome Ghanbaja, Jaafar Valsaque, Fabrice Berrada, Nawal Desforges, Alexandre Vigolo, Brigitte Laboratoire Réactions et Génie des Procédés (LRGP) Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS) Laboratoire de Chimie et Physique - Approche Multi-échelle des Milieux Complexes (LCP-A2MC) Université de Lorraine (UL) Institut Jean Lamour (IJL) Institut de Chimie du CNRS (INC)-Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS) 2020 https://hal.archives-ouvertes.fr/hal-02612257 https://hal.archives-ouvertes.fr/hal-02612257/document https://hal.archives-ouvertes.fr/hal-02612257/file/CatalToday_draftv10_rev2.pdf https://doi.org/10.1016/j.cattod.2019.08.046 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.cattod.2019.08.046 hal-02612257 https://hal.archives-ouvertes.fr/hal-02612257 https://hal.archives-ouvertes.fr/hal-02612257/document https://hal.archives-ouvertes.fr/hal-02612257/file/CatalToday_draftv10_rev2.pdf doi:10.1016/j.cattod.2019.08.046 info:eu-repo/semantics/OpenAccess ISSN: 0920-5861 Catalysis Today https://hal.archives-ouvertes.fr/hal-02612257 Catalysis Today, Elsevier, 2020, 348, pp.26 - 36. ⟨10.1016/j.cattod.2019.08.046⟩ green solvent interactions supercritical CO2 carbon nanotubes Lipase immobilization [CHIM.MATE]Chemical Sciences/Material chemistry [CHIM.CATA]Chemical Sciences/Catalysis [SPI.MAT]Engineering Sciences [physics]/Materials info:eu-repo/semantics/article Journal articles 2020 ftccsdartic https://doi.org/10.1016/j.cattod.2019.08.046 2021-12-19T01:18:50Z International audience Candida antarctica B lipase (CAL-B) was immobilized on purified and functionalized multiwalled carbon nanotubes (MWCNTs). Both immobilization routes, physical adsorption and covalent bonding, were investigated. MWCNT functionalization by a non-aggressive oxidation by potassium permanganate led to an interesting balance between the hydrophilic and the hydrophobic areas of the MWCNT surface; the former being responsible of the good dispersion of MWCNTs in water and the latter having a favorable affinity with CAL-B. The enzyme loadings reached were significant: around 16 wt. % and 21 wt.% for non-covalent and covalent immobilization, respectively. The enzymatic activity was studied with the reaction of O-acylation of geraniol into geranyl acetate by CAL-B in supercritical CO2. Even if a decay in synthesis of geranyl acetate was observed over cycling for both CAL-B@MWCNT catalysts, it was demonstrated that the regioselectivity of CAL-B was unchanged through immobilization on the MWCNT surface for both routes. Interestingly, it was shown that a fully green enzymatic process can be achieved with these prepared CAL-B@MWCNT biocatalyst. Such approach could be transferred to other support/enzyme systems for developing new eco-friendly synthesis processes. Article in Journal/Newspaper Antarc* Antarctica Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) Catalysis Today 348 26 36 |
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 |
green solvent interactions supercritical CO2 carbon nanotubes Lipase immobilization [CHIM.MATE]Chemical Sciences/Material chemistry [CHIM.CATA]Chemical Sciences/Catalysis [SPI.MAT]Engineering Sciences [physics]/Materials |
spellingShingle |
green solvent interactions supercritical CO2 carbon nanotubes Lipase immobilization [CHIM.MATE]Chemical Sciences/Material chemistry [CHIM.CATA]Chemical Sciences/Catalysis [SPI.MAT]Engineering Sciences [physics]/Materials Bourkaib, Mohamed Chafik Guiavarc’h, Yann Chevalot, Isabelle Delaunay, Stéphane Gleize, Jerome Ghanbaja, Jaafar Valsaque, Fabrice Berrada, Nawal Desforges, Alexandre Vigolo, Brigitte Non-covalent and covalent immobilization of Candida antarctica Lipase B on chemically modified multiwalled carbon nanotubes for a green acylation process in supercritical CO2 |
topic_facet |
green solvent interactions supercritical CO2 carbon nanotubes Lipase immobilization [CHIM.MATE]Chemical Sciences/Material chemistry [CHIM.CATA]Chemical Sciences/Catalysis [SPI.MAT]Engineering Sciences [physics]/Materials |
description |
International audience Candida antarctica B lipase (CAL-B) was immobilized on purified and functionalized multiwalled carbon nanotubes (MWCNTs). Both immobilization routes, physical adsorption and covalent bonding, were investigated. MWCNT functionalization by a non-aggressive oxidation by potassium permanganate led to an interesting balance between the hydrophilic and the hydrophobic areas of the MWCNT surface; the former being responsible of the good dispersion of MWCNTs in water and the latter having a favorable affinity with CAL-B. The enzyme loadings reached were significant: around 16 wt. % and 21 wt.% for non-covalent and covalent immobilization, respectively. The enzymatic activity was studied with the reaction of O-acylation of geraniol into geranyl acetate by CAL-B in supercritical CO2. Even if a decay in synthesis of geranyl acetate was observed over cycling for both CAL-B@MWCNT catalysts, it was demonstrated that the regioselectivity of CAL-B was unchanged through immobilization on the MWCNT surface for both routes. Interestingly, it was shown that a fully green enzymatic process can be achieved with these prepared CAL-B@MWCNT biocatalyst. Such approach could be transferred to other support/enzyme systems for developing new eco-friendly synthesis processes. |
author2 |
Laboratoire Réactions et Génie des Procédés (LRGP) Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS) Laboratoire de Chimie et Physique - Approche Multi-échelle des Milieux Complexes (LCP-A2MC) Université de Lorraine (UL) Institut Jean Lamour (IJL) Institut de Chimie du CNRS (INC)-Université de Lorraine (UL)-Centre National de la Recherche Scientifique (CNRS) |
format |
Article in Journal/Newspaper |
author |
Bourkaib, Mohamed Chafik Guiavarc’h, Yann Chevalot, Isabelle Delaunay, Stéphane Gleize, Jerome Ghanbaja, Jaafar Valsaque, Fabrice Berrada, Nawal Desforges, Alexandre Vigolo, Brigitte |
author_facet |
Bourkaib, Mohamed Chafik Guiavarc’h, Yann Chevalot, Isabelle Delaunay, Stéphane Gleize, Jerome Ghanbaja, Jaafar Valsaque, Fabrice Berrada, Nawal Desforges, Alexandre Vigolo, Brigitte |
author_sort |
Bourkaib, Mohamed Chafik |
title |
Non-covalent and covalent immobilization of Candida antarctica Lipase B on chemically modified multiwalled carbon nanotubes for a green acylation process in supercritical CO2 |
title_short |
Non-covalent and covalent immobilization of Candida antarctica Lipase B on chemically modified multiwalled carbon nanotubes for a green acylation process in supercritical CO2 |
title_full |
Non-covalent and covalent immobilization of Candida antarctica Lipase B on chemically modified multiwalled carbon nanotubes for a green acylation process in supercritical CO2 |
title_fullStr |
Non-covalent and covalent immobilization of Candida antarctica Lipase B on chemically modified multiwalled carbon nanotubes for a green acylation process in supercritical CO2 |
title_full_unstemmed |
Non-covalent and covalent immobilization of Candida antarctica Lipase B on chemically modified multiwalled carbon nanotubes for a green acylation process in supercritical CO2 |
title_sort |
non-covalent and covalent immobilization of candida antarctica lipase b on chemically modified multiwalled carbon nanotubes for a green acylation process in supercritical co2 |
publisher |
HAL CCSD |
publishDate |
2020 |
url |
https://hal.archives-ouvertes.fr/hal-02612257 https://hal.archives-ouvertes.fr/hal-02612257/document https://hal.archives-ouvertes.fr/hal-02612257/file/CatalToday_draftv10_rev2.pdf https://doi.org/10.1016/j.cattod.2019.08.046 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ISSN: 0920-5861 Catalysis Today https://hal.archives-ouvertes.fr/hal-02612257 Catalysis Today, Elsevier, 2020, 348, pp.26 - 36. ⟨10.1016/j.cattod.2019.08.046⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.cattod.2019.08.046 hal-02612257 https://hal.archives-ouvertes.fr/hal-02612257 https://hal.archives-ouvertes.fr/hal-02612257/document https://hal.archives-ouvertes.fr/hal-02612257/file/CatalToday_draftv10_rev2.pdf doi:10.1016/j.cattod.2019.08.046 |
op_rights |
info:eu-repo/semantics/OpenAccess |
op_doi |
https://doi.org/10.1016/j.cattod.2019.08.046 |
container_title |
Catalysis Today |
container_volume |
348 |
container_start_page |
26 |
op_container_end_page |
36 |
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1766258169891258368 |