Lipase-Catalyzed Kinetic Resolution of Aryltrimethylsilyl Chiral Alcohols

Lipase-catalyzed kinetic resolution of aryltrimethylsilyl chiral alcohols through a transesterification reaction was studied. The optimal conditions found for the kinetic resolution of m- and p-aryltrimethylsilyl chiral alcohols, led to excellent results, high conversions (c = 50%), high enantiomeri...

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Autores principales: Palmeira, Dayvson J., Abreu, Juliana C., Andrade, Leandro H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2011
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6264554/
https://www.ncbi.nlm.nih.gov/pubmed/22113578
http://dx.doi.org/10.3390/molecules16119697
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author Palmeira, Dayvson J.
Abreu, Juliana C.
Andrade, Leandro H.
author_facet Palmeira, Dayvson J.
Abreu, Juliana C.
Andrade, Leandro H.
author_sort Palmeira, Dayvson J.
collection PubMed
description Lipase-catalyzed kinetic resolution of aryltrimethylsilyl chiral alcohols through a transesterification reaction was studied. The optimal conditions found for the kinetic resolution of m- and p-aryltrimethylsilyl chiral alcohols, led to excellent results, high conversions (c = 50%), high enantiomeric ratios (E > 200) and enantiomeric excesses for the remaining (S)-alcohol and (R)-acetylated product (>99%). However, kinetic resolution of o-aryltrimethylsilyl chiral alcohols did not occur under the same conditions applied to the other isomers.
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spelling pubmed-62645542018-12-10 Lipase-Catalyzed Kinetic Resolution of Aryltrimethylsilyl Chiral Alcohols Palmeira, Dayvson J. Abreu, Juliana C. Andrade, Leandro H. Molecules Article Lipase-catalyzed kinetic resolution of aryltrimethylsilyl chiral alcohols through a transesterification reaction was studied. The optimal conditions found for the kinetic resolution of m- and p-aryltrimethylsilyl chiral alcohols, led to excellent results, high conversions (c = 50%), high enantiomeric ratios (E > 200) and enantiomeric excesses for the remaining (S)-alcohol and (R)-acetylated product (>99%). However, kinetic resolution of o-aryltrimethylsilyl chiral alcohols did not occur under the same conditions applied to the other isomers. MDPI 2011-11-23 /pmc/articles/PMC6264554/ /pubmed/22113578 http://dx.doi.org/10.3390/molecules16119697 Text en © 2011 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Palmeira, Dayvson J.
Abreu, Juliana C.
Andrade, Leandro H.
Lipase-Catalyzed Kinetic Resolution of Aryltrimethylsilyl Chiral Alcohols
title Lipase-Catalyzed Kinetic Resolution of Aryltrimethylsilyl Chiral Alcohols
title_full Lipase-Catalyzed Kinetic Resolution of Aryltrimethylsilyl Chiral Alcohols
title_fullStr Lipase-Catalyzed Kinetic Resolution of Aryltrimethylsilyl Chiral Alcohols
title_full_unstemmed Lipase-Catalyzed Kinetic Resolution of Aryltrimethylsilyl Chiral Alcohols
title_short Lipase-Catalyzed Kinetic Resolution of Aryltrimethylsilyl Chiral Alcohols
title_sort lipase-catalyzed kinetic resolution of aryltrimethylsilyl chiral alcohols
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6264554/
https://www.ncbi.nlm.nih.gov/pubmed/22113578
http://dx.doi.org/10.3390/molecules16119697
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