Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols

Lipase B from Candida antarctica immobilized by covalent binding on sebacoyl-activated chitosan-coated magnetic nanoparticles proved to be an efficient biocatalyst (49.2–50% conversion in 3–16 h and >96% enantiomeric excess) for the enzymatic kinetic resolution of some racemic heteroarylethanols...

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Autores principales: Spelmezan, Cristina Georgiana, Bencze, László Csaba, Katona, Gabriel, Irimie, Florin Dan, Paizs, Csaba, Toșa, Monica Ioana
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
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Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7024219/
https://www.ncbi.nlm.nih.gov/pubmed/31952168
http://dx.doi.org/10.3390/molecules25020350
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author Spelmezan, Cristina Georgiana
Bencze, László Csaba
Katona, Gabriel
Irimie, Florin Dan
Paizs, Csaba
Toșa, Monica Ioana
author_facet Spelmezan, Cristina Georgiana
Bencze, László Csaba
Katona, Gabriel
Irimie, Florin Dan
Paizs, Csaba
Toșa, Monica Ioana
author_sort Spelmezan, Cristina Georgiana
collection PubMed
description Lipase B from Candida antarctica immobilized by covalent binding on sebacoyl-activated chitosan-coated magnetic nanoparticles proved to be an efficient biocatalyst (49.2–50% conversion in 3–16 h and >96% enantiomeric excess) for the enzymatic kinetic resolution of some racemic heteroarylethanols through transesterification with vinyl acetate. Under optimal conditions (vinyl acetate, n-hexane, 45 °C), the biocatalyst remains active after 10 cycles.
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spelling pubmed-70242192020-03-19 Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols Spelmezan, Cristina Georgiana Bencze, László Csaba Katona, Gabriel Irimie, Florin Dan Paizs, Csaba Toșa, Monica Ioana Molecules Article Lipase B from Candida antarctica immobilized by covalent binding on sebacoyl-activated chitosan-coated magnetic nanoparticles proved to be an efficient biocatalyst (49.2–50% conversion in 3–16 h and >96% enantiomeric excess) for the enzymatic kinetic resolution of some racemic heteroarylethanols through transesterification with vinyl acetate. Under optimal conditions (vinyl acetate, n-hexane, 45 °C), the biocatalyst remains active after 10 cycles. MDPI 2020-01-15 /pmc/articles/PMC7024219/ /pubmed/31952168 http://dx.doi.org/10.3390/molecules25020350 Text en © 2020 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 (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Spelmezan, Cristina Georgiana
Bencze, László Csaba
Katona, Gabriel
Irimie, Florin Dan
Paizs, Csaba
Toșa, Monica Ioana
Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols
title Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols
title_full Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols
title_fullStr Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols
title_full_unstemmed Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols
title_short Efficient and Stable Magnetic Chitosan-Lipase B from Candida Antarctica Bioconjugates in the Enzymatic Kinetic Resolution of Racemic Heteroarylethanols
title_sort efficient and stable magnetic chitosan-lipase b from candida antarctica bioconjugates in the enzymatic kinetic resolution of racemic heteroarylethanols
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7024219/
https://www.ncbi.nlm.nih.gov/pubmed/31952168
http://dx.doi.org/10.3390/molecules25020350
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