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...
Published in: | Journal of Molecular Catalysis B: Enzymatic |
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ftunivnantes:oai:HAL:hal-01450644v1 2023-05-15T13:31:54+02:00 Kinetic study of 2-butanol O-acylation and sec-butylamine N-acylation catalyzed by Candida antarctica lipase B Le Joubioux, Florian Achour, Oussama Bridiau, Nicolas Graber, Marianne Maugard, Thierry LIttoral ENvironnement et Sociétés (LIENSs) La Rochelle Université (ULR)-Centre National de la Recherche Scientifique (CNRS) ANR Expenantio ANR-08-CP2D-0010,EXPENANTIO,Vers une voie durable pour la synthèse de molécules chirales: approches expérimentales et théoriques innovantes pour la compréhension des bases moléculaires de l'énantiosélectivité des lipases et des estérases - Towards green synthesis of chiral molecules(2008) 2011 https://hal.science/hal-01450644 https://hal.science/hal-01450644/document https://hal.science/hal-01450644/file/publi1_florian%20HAL.pdf https://doi.org/10.1016/j.molcatb.2011.02.012 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2011.02.012 hal-01450644 https://hal.science/hal-01450644 https://hal.science/hal-01450644/document https://hal.science/hal-01450644/file/publi1_florian%20HAL.pdf doi:10.1016/j.molcatb.2011.02.012 info:eu-repo/semantics/OpenAccess ISSN: 1381-1177 Journal of Molecular Catalysis B: Enzymatic https://hal.science/hal-01450644 Journal of Molecular Catalysis B: Enzymatic, 2011, 70 (3-4), pp.108-113. ⟨10.1016/j.molcatb.2011.02.012⟩ Candida antarctica lipase B Chemoselectivity Enantioselectivity Kinetic mechanism O/N-acylation [SDV.BIO]Life Sciences [q-bio]/Biotechnology [CHIM.ORGA]Chemical Sciences/Organic chemistry [CHIM.CATA]Chemical Sciences/Catalysis info:eu-repo/semantics/article Journal articles 2011 ftunivnantes https://doi.org/10.1016/j.molcatb.2011.02.012 2023-03-08T05:01:27Z 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 kinetic parameters were calculated: the enantiomeric ratios (E) were evaluated and confirmed the preference of C. antarctica lipase B for the (R)-enantiomer, which was consistent with the literature. The enantioselectivity 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 C. antarctica lipase B was evaluated, showing that C. 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 Université de Nantes: HAL-UNIV-NANTES Journal of Molecular Catalysis B: Enzymatic 70 3-4 108 113 |
institution |
Open Polar |
collection |
Université de Nantes: HAL-UNIV-NANTES |
op_collection_id |
ftunivnantes |
language |
English |
topic |
Candida antarctica lipase B Chemoselectivity Enantioselectivity Kinetic mechanism O/N-acylation [SDV.BIO]Life Sciences [q-bio]/Biotechnology [CHIM.ORGA]Chemical Sciences/Organic chemistry [CHIM.CATA]Chemical Sciences/Catalysis |
spellingShingle |
Candida antarctica lipase B Chemoselectivity Enantioselectivity Kinetic mechanism O/N-acylation [SDV.BIO]Life Sciences [q-bio]/Biotechnology [CHIM.ORGA]Chemical Sciences/Organic chemistry [CHIM.CATA]Chemical Sciences/Catalysis Le Joubioux, Florian Achour, Oussama 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 |
Candida antarctica lipase B Chemoselectivity Enantioselectivity Kinetic mechanism O/N-acylation [SDV.BIO]Life Sciences [q-bio]/Biotechnology [CHIM.ORGA]Chemical Sciences/Organic chemistry [CHIM.CATA]Chemical Sciences/Catalysis |
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 kinetic parameters were calculated: the enantiomeric ratios (E) were evaluated and confirmed the preference of C. antarctica lipase B for the (R)-enantiomer, which was consistent with the literature. The enantioselectivity 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 C. antarctica lipase B was evaluated, showing that C. 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 (LIENSs) La Rochelle Université (ULR)-Centre National de la Recherche Scientifique (CNRS) ANR Expenantio ANR-08-CP2D-0010,EXPENANTIO,Vers une voie durable pour la synthèse de molécules chirales: approches expérimentales et théoriques innovantes pour la compréhension des bases moléculaires de l'énantiosélectivité des lipases et des estérases - Towards green synthesis of chiral molecules(2008) |
format |
Article in Journal/Newspaper |
author |
Le Joubioux, Florian Achour, Oussama Bridiau, Nicolas Graber, Marianne Maugard, Thierry |
author_facet |
Le Joubioux, Florian Achour, Oussama 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.science/hal-01450644 https://hal.science/hal-01450644/document https://hal.science/hal-01450644/file/publi1_florian%20HAL.pdf https://doi.org/10.1016/j.molcatb.2011.02.012 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
ISSN: 1381-1177 Journal of Molecular Catalysis B: Enzymatic https://hal.science/hal-01450644 Journal of Molecular Catalysis B: Enzymatic, 2011, 70 (3-4), pp.108-113. ⟨10.1016/j.molcatb.2011.02.012⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2011.02.012 hal-01450644 https://hal.science/hal-01450644 https://hal.science/hal-01450644/document https://hal.science/hal-01450644/file/publi1_florian%20HAL.pdf doi:10.1016/j.molcatb.2011.02.012 |
op_rights |
info:eu-repo/semantics/OpenAccess |
op_doi |
https://doi.org/10.1016/j.molcatb.2011.02.012 |
container_title |
Journal of Molecular Catalysis B: Enzymatic |
container_volume |
70 |
container_issue |
3-4 |
container_start_page |
108 |
op_container_end_page |
113 |
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1766022316786974720 |