Kinetic study of 2-butanol O-acylation and sec-butylamine N-acylation catalyzed by Candida antarctica lipase B
International audience The aim of this work was to study the differential behavior shown by Candida antarctica lipase B during the O-acylation and N-acylation of monofunctional alcohols and monofunctional amines. To achieve this, 2-butanol and sec-butylamine were used as model molecules. Yields, kin...
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ftccsdartic:oai:HAL:hal-00790682v1 2023-05-15T14:04:01+02:00 Kinetic study of 2-butanol O-acylation and sec-butylamine N-acylation catalyzed by Candida antarctica lipase B Le Joubioux, Florian Oussama, A. Bridiau, Nicolas Graber, Marianne Maugard, Thierry LIttoral ENvironnement et Sociétés - UMRi 7266 (LIENSs) Université de La Rochelle (ULR)-Centre National de la Recherche Scientifique (CNRS) 2011-07-14 https://hal.archives-ouvertes.fr/hal-00790682 https://hal.archives-ouvertes.fr/hal-00790682/document https://hal.archives-ouvertes.fr/hal-00790682/file/publi1_florian_HAL.pdf en eng HAL CCSD Elsevier hal-00790682 https://hal.archives-ouvertes.fr/hal-00790682 https://hal.archives-ouvertes.fr/hal-00790682/document https://hal.archives-ouvertes.fr/hal-00790682/file/publi1_florian_HAL.pdf info:eu-repo/semantics/OpenAccess ISSN: 1381-1177 Journal of Molecular Catalysis B: Enzymatic https://hal.archives-ouvertes.fr/hal-00790682 Journal of Molecular Catalysis B: Enzymatic, Elsevier, 2011, 70, pp.108-113 [SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology info:eu-repo/semantics/article Journal articles 2011 ftccsdartic 2021-10-24T15:23:21Z International audience The aim of this work was to study the differential behavior shown by Candida antarctica lipase B during the O-acylation and N-acylation of monofunctional alcohols and monofunctional amines. To achieve this, 2-butanol and sec-butylamine were used as model molecules. Yields, kinetics and enantioselectivity were studied for both reactions. Although a steady-state ordered ternary complex bi-bi mechanism was obtained for the O-acylation of 2- butanol, a ping-pong bi-bi mechanism was obtained for the N-acylation in case of low sec- butylamine concentrations. The values of apparent kinetics parameters were calculated: the enantiomeric ratios (E) were evaluated and confirmed the preference of Candida antarctica lipase B for the (R)-enantiomer, which was consistent with the literature. The nantioselectivity was calculated for the alcohol (E ≈ 3.17) and for the amine (E ≈ 1.34). Concerning the O-acylation, the yields were found to be very similar for both enantiomers R and S. However, both initial rates and yields of the (R)-enantiomer N-acylation were higher than those of the (S)-enantiomer. In the last part of our study, the chemoselectivity of Candida antarctica lipase B was evaluated, showing that Candida antarctica lipase B was a chemoselective enzyme that preferentially catalyzed the O-acylation to the detriment of the N-acylation (C ≈ 92, for the selective acylation of (R)-enantiomers). These results provide new insights for the synthesis of products issued from the selective acylation of multifunctional substrates such as amino-alcohols. Article in Journal/Newspaper Antarc* Antarctica Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) |
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Open Polar |
collection |
Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) |
op_collection_id |
ftccsdartic |
language |
English |
topic |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology |
spellingShingle |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology Le Joubioux, Florian Oussama, A. Bridiau, Nicolas Graber, Marianne Maugard, Thierry Kinetic study of 2-butanol O-acylation and sec-butylamine N-acylation catalyzed by Candida antarctica lipase B |
topic_facet |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [INFO.INFO-BT]Computer Science [cs]/Biotechnology |
description |
International audience The aim of this work was to study the differential behavior shown by Candida antarctica lipase B during the O-acylation and N-acylation of monofunctional alcohols and monofunctional amines. To achieve this, 2-butanol and sec-butylamine were used as model molecules. Yields, kinetics and enantioselectivity were studied for both reactions. Although a steady-state ordered ternary complex bi-bi mechanism was obtained for the O-acylation of 2- butanol, a ping-pong bi-bi mechanism was obtained for the N-acylation in case of low sec- butylamine concentrations. The values of apparent kinetics parameters were calculated: the enantiomeric ratios (E) were evaluated and confirmed the preference of Candida antarctica lipase B for the (R)-enantiomer, which was consistent with the literature. The nantioselectivity was calculated for the alcohol (E ≈ 3.17) and for the amine (E ≈ 1.34). Concerning the O-acylation, the yields were found to be very similar for both enantiomers R and S. However, both initial rates and yields of the (R)-enantiomer N-acylation were higher than those of the (S)-enantiomer. In the last part of our study, the chemoselectivity of Candida antarctica lipase B was evaluated, showing that Candida antarctica lipase B was a chemoselective enzyme that preferentially catalyzed the O-acylation to the detriment of the N-acylation (C ≈ 92, for the selective acylation of (R)-enantiomers). These results provide new insights for the synthesis of products issued from the selective acylation of multifunctional substrates such as amino-alcohols. |
author2 |
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 |
Le Joubioux, Florian Oussama, A. Bridiau, Nicolas Graber, Marianne Maugard, Thierry |
author_facet |
Le Joubioux, Florian Oussama, A. Bridiau, Nicolas Graber, Marianne Maugard, Thierry |
author_sort |
Le Joubioux, Florian |
title |
Kinetic study of 2-butanol O-acylation and sec-butylamine N-acylation catalyzed by Candida antarctica lipase B |
title_short |
Kinetic study of 2-butanol O-acylation and sec-butylamine N-acylation catalyzed by Candida antarctica lipase B |
title_full |
Kinetic study of 2-butanol O-acylation and sec-butylamine N-acylation catalyzed by Candida antarctica lipase B |
title_fullStr |
Kinetic study of 2-butanol O-acylation and sec-butylamine N-acylation catalyzed by Candida antarctica lipase B |
title_full_unstemmed |
Kinetic study of 2-butanol O-acylation and sec-butylamine N-acylation catalyzed by Candida antarctica lipase B |
title_sort |
kinetic study of 2-butanol o-acylation and sec-butylamine n-acylation catalyzed by candida antarctica lipase b |
publisher |
HAL CCSD |
publishDate |
2011 |
url |
https://hal.archives-ouvertes.fr/hal-00790682 https://hal.archives-ouvertes.fr/hal-00790682/document https://hal.archives-ouvertes.fr/hal-00790682/file/publi1_florian_HAL.pdf |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ISSN: 1381-1177 Journal of Molecular Catalysis B: Enzymatic https://hal.archives-ouvertes.fr/hal-00790682 Journal of Molecular Catalysis B: Enzymatic, Elsevier, 2011, 70, pp.108-113 |
op_relation |
hal-00790682 https://hal.archives-ouvertes.fr/hal-00790682 https://hal.archives-ouvertes.fr/hal-00790682/document https://hal.archives-ouvertes.fr/hal-00790682/file/publi1_florian_HAL.pdf |
op_rights |
info:eu-repo/semantics/OpenAccess |
_version_ |
1766274954830020608 |