Improved racemate resolution of pentan-2-ol and trans-(Z)-cyclooct-5-ene-1,2-diol by lipase catalysis
International audience Lipases are important catalysts in chiral synthesis due to their wide substrate recognition combined witha high stereoselectivity. We demonstrate here that the state, free or immobilized, of Candida antarcticalipase B (CaLB) affects enantioselectivity and also alters the tempe...
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ftccsdartic:oai:HAL:hal-01432549v1 |
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Open Polar |
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Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) |
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ftccsdartic |
language |
English |
topic |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [CHIM]Chemical Sciences |
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[SDV.BIO]Life Sciences [q-bio]/Biotechnology [CHIM]Chemical Sciences Graber, Marianne Rouillard, Hervé Delatouche, Régis Fniter, Najla Belkhiria, Belsem Bonnet, Antoine Domon, Lisiane Thiéry, Valérie Improved racemate resolution of pentan-2-ol and trans-(Z)-cyclooct-5-ene-1,2-diol by lipase catalysis |
topic_facet |
[SDV.BIO]Life Sciences [q-bio]/Biotechnology [CHIM]Chemical Sciences |
description |
International audience Lipases are important catalysts in chiral synthesis due to their wide substrate recognition combined witha high stereoselectivity. We demonstrate here that the state, free or immobilized, of Candida antarcticalipase B (CaLB) affects enantioselectivity and also alters the temperature dependancy of the enzyme. Thisindicates that CaLB undergoes various conformations induced by its interaction with the different immo-bilization supports studied. Molecular imprinting experiments, using immobilized enzyme co-dried withmimic substrate molecules, enhanced the enantiomeric ratio two-fold or three-fold, depending on theimmobilization support. The structure of the acyl donor has a pronounced effect on CaLB catalyzed res-olution, due to the proximity of the acyl and alcohol moieties during catalysis. When the acylation ofpentan-2-ol was examined, we found that the 3C methyl propanoate donor afforded the highest resolu-tion. Trans-(Z)-cyclooct-5-en-1,2-diol was used as a model racemic substrate to study the ability of lipaseto catalyze the resolution of difunctionalized compounds. There was a clear enhancement in the enan-tiomer selectivity of the biotransformation of the diol when vinyl butanoate is used as the acyl donor. Theconversion and enantiomeric excess of (1R,2R)-monoacetates were enhanced, using immobilized CaLB,when the chain length of the donors increased from C2 to C4. |
author2 |
LIttoral ENvironnement et Sociétés - UMRi 7266 (LIENSs) Université de La Rochelle (ULR)-Centre National de la Recherche Scientifique (CNRS) 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 |
Graber, Marianne Rouillard, Hervé Delatouche, Régis Fniter, Najla Belkhiria, Belsem Bonnet, Antoine Domon, Lisiane Thiéry, Valérie |
author_facet |
Graber, Marianne Rouillard, Hervé Delatouche, Régis Fniter, Najla Belkhiria, Belsem Bonnet, Antoine Domon, Lisiane Thiéry, Valérie |
author_sort |
Graber, Marianne |
title |
Improved racemate resolution of pentan-2-ol and trans-(Z)-cyclooct-5-ene-1,2-diol by lipase catalysis |
title_short |
Improved racemate resolution of pentan-2-ol and trans-(Z)-cyclooct-5-ene-1,2-diol by lipase catalysis |
title_full |
Improved racemate resolution of pentan-2-ol and trans-(Z)-cyclooct-5-ene-1,2-diol by lipase catalysis |
title_fullStr |
Improved racemate resolution of pentan-2-ol and trans-(Z)-cyclooct-5-ene-1,2-diol by lipase catalysis |
title_full_unstemmed |
Improved racemate resolution of pentan-2-ol and trans-(Z)-cyclooct-5-ene-1,2-diol by lipase catalysis |
title_sort |
improved racemate resolution of pentan-2-ol and trans-(z)-cyclooct-5-ene-1,2-diol by lipase catalysis |
publisher |
HAL CCSD |
publishDate |
2016 |
url |
https://hal.archives-ouvertes.fr/hal-01432549 https://hal.archives-ouvertes.fr/hal-01432549/document https://hal.archives-ouvertes.fr/hal-01432549/file/Revised%20Manuscrip%20r%C3%A9visions%20accept%C3%A9est.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Captions%20to%20Figures.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%201.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%202.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%203.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%204.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%205.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%206.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Scheme%201.pdf https://doi.org/10.1016/j.jbiotec.2016.09.010 |
genre |
Antarc* |
genre_facet |
Antarc* |
op_source |
ISSN: 0168-1656 Journal of Biotechnology https://hal.archives-ouvertes.fr/hal-01432549 Journal of Biotechnology, Elsevier, 2016, 238, pp.60-68. ⟨10.1016/j.jbiotec.2016.09.010⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jbiotec.2016.09.010 hal-01432549 https://hal.archives-ouvertes.fr/hal-01432549 https://hal.archives-ouvertes.fr/hal-01432549/document https://hal.archives-ouvertes.fr/hal-01432549/file/Revised%20Manuscrip%20r%C3%A9visions%20accept%C3%A9est.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Captions%20to%20Figures.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%201.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%202.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%203.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%204.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%205.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%206.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Scheme%201.pdf doi:10.1016/j.jbiotec.2016.09.010 |
op_rights |
info:eu-repo/semantics/OpenAccess |
op_doi |
https://doi.org/10.1016/j.jbiotec.2016.09.010 |
container_title |
Journal of Biotechnology |
container_volume |
238 |
container_start_page |
60 |
op_container_end_page |
68 |
_version_ |
1766190411153408000 |
spelling |
ftccsdartic:oai:HAL:hal-01432549v1 2023-05-15T13:43:33+02:00 Improved racemate resolution of pentan-2-ol and trans-(Z)-cyclooct-5-ene-1,2-diol by lipase catalysis Graber, Marianne Rouillard, Hervé Delatouche, Régis Fniter, Najla Belkhiria, Belsem Bonnet, Antoine Domon, Lisiane Thiéry, Valérie LIttoral ENvironnement et Sociétés - UMRi 7266 (LIENSs) Université de La Rochelle (ULR)-Centre National de la Recherche Scientifique (CNRS) 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) 2016-09-23 https://hal.archives-ouvertes.fr/hal-01432549 https://hal.archives-ouvertes.fr/hal-01432549/document https://hal.archives-ouvertes.fr/hal-01432549/file/Revised%20Manuscrip%20r%C3%A9visions%20accept%C3%A9est.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Captions%20to%20Figures.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%201.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%202.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%203.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%204.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%205.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%206.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Scheme%201.pdf https://doi.org/10.1016/j.jbiotec.2016.09.010 en eng HAL CCSD Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jbiotec.2016.09.010 hal-01432549 https://hal.archives-ouvertes.fr/hal-01432549 https://hal.archives-ouvertes.fr/hal-01432549/document https://hal.archives-ouvertes.fr/hal-01432549/file/Revised%20Manuscrip%20r%C3%A9visions%20accept%C3%A9est.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Captions%20to%20Figures.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%201.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%202.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%203.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%204.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%205.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Figure%206.pdf https://hal.archives-ouvertes.fr/hal-01432549/file/Scheme%201.pdf doi:10.1016/j.jbiotec.2016.09.010 info:eu-repo/semantics/OpenAccess ISSN: 0168-1656 Journal of Biotechnology https://hal.archives-ouvertes.fr/hal-01432549 Journal of Biotechnology, Elsevier, 2016, 238, pp.60-68. ⟨10.1016/j.jbiotec.2016.09.010⟩ [SDV.BIO]Life Sciences [q-bio]/Biotechnology [CHIM]Chemical Sciences info:eu-repo/semantics/article Journal articles 2016 ftccsdartic https://doi.org/10.1016/j.jbiotec.2016.09.010 2021-11-07T04:06:02Z International audience Lipases are important catalysts in chiral synthesis due to their wide substrate recognition combined witha high stereoselectivity. We demonstrate here that the state, free or immobilized, of Candida antarcticalipase B (CaLB) affects enantioselectivity and also alters the temperature dependancy of the enzyme. Thisindicates that CaLB undergoes various conformations induced by its interaction with the different immo-bilization supports studied. Molecular imprinting experiments, using immobilized enzyme co-dried withmimic substrate molecules, enhanced the enantiomeric ratio two-fold or three-fold, depending on theimmobilization support. The structure of the acyl donor has a pronounced effect on CaLB catalyzed res-olution, due to the proximity of the acyl and alcohol moieties during catalysis. When the acylation ofpentan-2-ol was examined, we found that the 3C methyl propanoate donor afforded the highest resolu-tion. Trans-(Z)-cyclooct-5-en-1,2-diol was used as a model racemic substrate to study the ability of lipaseto catalyze the resolution of difunctionalized compounds. There was a clear enhancement in the enan-tiomer selectivity of the biotransformation of the diol when vinyl butanoate is used as the acyl donor. Theconversion and enantiomeric excess of (1R,2R)-monoacetates were enhanced, using immobilized CaLB,when the chain length of the donors increased from C2 to C4. Article in Journal/Newspaper Antarc* Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) Journal of Biotechnology 238 60 68 |