Enzymatic kinetic resolution of (RS)-1-(Phenyl)ethanols by Burkholderia cepacia lipase immobilized on magnetic nanoparticles

Enzymatic kinetic resolution of (RS)-1-(Phenyl)ethanols by Burkholderia cepacia lipase immobilized on magnetic nanoparticles

Lipase from Burkholderia cepacia immobilized on superparamagnetic nanoparticles using adsorption and chemisorption methodologies was efficiently applied as recyclable biocatalyst in the enzymatic kinetic resolution of (RS)-1-(phenyl)ethanols via transesterification reactions. (R)-Esters and the remaining (S)-alcohols were obtained with excellent enantiomeric excess (> 99%), which corresponds to a perfect process of enzymatic kinetic resolution (conversion 50%, E > 200). The transesterification reactions catalysed with B. cepacia lipase immobilized by the glutaraldehyde method showed the best results in terms of reusability, preserving the enzyme activity (conversion 50%, E > 200) for at least 8 successive cycles.

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Main Authors: Rebelo,Lya P., Netto,Caterina G. C. M., Toma,Henrique E., Andrade,Leandro H.
Format: Digital revista
Language:English
Published: Sociedade Brasileira de Química 2010
Online Access:http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532010000800019
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spelling oai:scielo:S0103-505320100008000192011-10-14Enzymatic kinetic resolution of (RS)-1-(Phenyl)ethanols by Burkholderia cepacia lipase immobilized on magnetic nanoparticlesRebelo,Lya P.Netto,Caterina G. C. M.Toma,Henrique E.Andrade,Leandro H. superparamagnetic nanoparticles lipase transesterification catalysis enantiomeric resolution Lipase from Burkholderia cepacia immobilized on superparamagnetic nanoparticles using adsorption and chemisorption methodologies was efficiently applied as recyclable biocatalyst in the enzymatic kinetic resolution of (RS)-1-(phenyl)ethanols via transesterification reactions. (R)-Esters and the remaining (S)-alcohols were obtained with excellent enantiomeric excess (> 99%), which corresponds to a perfect process of enzymatic kinetic resolution (conversion 50%, E > 200). The transesterification reactions catalysed with B. cepacia lipase immobilized by the glutaraldehyde method showed the best results in terms of reusability, preserving the enzyme activity (conversion 50%, E > 200) for at least 8 successive cycles.info:eu-repo/semantics/openAccessSociedade Brasileira de QuímicaJournal of the Brazilian Chemical Society v.21 n.8 20102010-01-01info:eu-repo/semantics/articletext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532010000800019en10.1590/S0103-50532010000800019
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countrycode BR
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databasecode rev-scielo-br
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region America del Sur
libraryname SciELO
language English
format Digital
author Rebelo,Lya P.
Netto,Caterina G. C. M.
Toma,Henrique E.
Andrade,Leandro H.
spellingShingle Rebelo,Lya P.
Netto,Caterina G. C. M.
Toma,Henrique E.
Andrade,Leandro H.
Enzymatic kinetic resolution of (RS)-1-(Phenyl)ethanols by Burkholderia cepacia lipase immobilized on magnetic nanoparticles
author_facet Rebelo,Lya P.
Netto,Caterina G. C. M.
Toma,Henrique E.
Andrade,Leandro H.
author_sort Rebelo,Lya P.
title Enzymatic kinetic resolution of (RS)-1-(Phenyl)ethanols by Burkholderia cepacia lipase immobilized on magnetic nanoparticles
title_short Enzymatic kinetic resolution of (RS)-1-(Phenyl)ethanols by Burkholderia cepacia lipase immobilized on magnetic nanoparticles
title_full Enzymatic kinetic resolution of (RS)-1-(Phenyl)ethanols by Burkholderia cepacia lipase immobilized on magnetic nanoparticles
title_fullStr Enzymatic kinetic resolution of (RS)-1-(Phenyl)ethanols by Burkholderia cepacia lipase immobilized on magnetic nanoparticles
title_full_unstemmed Enzymatic kinetic resolution of (RS)-1-(Phenyl)ethanols by Burkholderia cepacia lipase immobilized on magnetic nanoparticles
title_sort enzymatic kinetic resolution of (rs)-1-(phenyl)ethanols by burkholderia cepacia lipase immobilized on magnetic nanoparticles
description Lipase from Burkholderia cepacia immobilized on superparamagnetic nanoparticles using adsorption and chemisorption methodologies was efficiently applied as recyclable biocatalyst in the enzymatic kinetic resolution of (RS)-1-(phenyl)ethanols via transesterification reactions. (R)-Esters and the remaining (S)-alcohols were obtained with excellent enantiomeric excess (> 99%), which corresponds to a perfect process of enzymatic kinetic resolution (conversion 50%, E > 200). The transesterification reactions catalysed with B. cepacia lipase immobilized by the glutaraldehyde method showed the best results in terms of reusability, preserving the enzyme activity (conversion 50%, E > 200) for at least 8 successive cycles.
publisher Sociedade Brasileira de Química
publishDate 2010
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532010000800019
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