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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Published in:Molecules
Main Authors: Spelmezan, Cristina Georgiana, Bencze, László Csaba, Katona, Gabriel, Irimie, Florin Dan, Paizs, Csaba, Toșa, Monica Ioana
Format: Text
Language:English
Published: MDPI 2020
Subjects:
Article
Antarc*
Antarctica
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7024219/
http://www.ncbi.nlm.nih.gov/pubmed/31952168
https://doi.org/10.3390/molecules25020350
id ftpubmed:oai:pubmedcentral.nih.gov:7024219
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spelling ftpubmed:oai:pubmedcentral.nih.gov:7024219 2023-05-15T14:03:03+02:00 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 2020-01-15 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7024219/ http://www.ncbi.nlm.nih.gov/pubmed/31952168 https://doi.org/10.3390/molecules25020350 en eng MDPI http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7024219/ http://www.ncbi.nlm.nih.gov/pubmed/31952168 http://dx.doi.org/10.3390/molecules25020350 © 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/). CC-BY Article Text 2020 ftpubmed https://doi.org/10.3390/molecules25020350 2020-03-22T01:21:57Z 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. Text Antarc* Antarctica PubMed Central (PMC) Molecules 25 2 350
institution Open Polar
collection PubMed Central (PMC)
op_collection_id ftpubmed
language English
topic Article
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
topic_facet Article
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.
format Text
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
title 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_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_sort efficient and stable magnetic chitosan-lipase b from candida antarctica bioconjugates in the enzymatic kinetic resolution of racemic heteroarylethanols
publisher MDPI
publishDate 2020
url http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7024219/
http://www.ncbi.nlm.nih.gov/pubmed/31952168
https://doi.org/10.3390/molecules25020350
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_relation http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7024219/
http://www.ncbi.nlm.nih.gov/pubmed/31952168
http://dx.doi.org/10.3390/molecules25020350
op_rights © 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/).
op_rightsnorm CC-BY
op_doi https://doi.org/10.3390/molecules25020350
container_title Molecules
container_volume 25
container_issue 2
container_start_page 350
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