Lipase on carbon nanotubes – an active, selective, stable and easy-to-optimize nanobiocatalyst for kinetic resolutions

An efficient biocatalyst was obtained by covalent immobilization of lipase B from C. antarctica on functionalized SwCNTs for the kinetic resolution of some aryl-ethanols in batch and continuous-flow modes.

Bibliographic Details
Published in:Reaction Chemistry & Engineering
Main Authors: Gal, Cristian Andrei, Barabás, Laura Edit, Bartha Vári, Judith-Hajnal, Moisă, Mădălina Elena, Balogh-Weiser, Diana, Bencze, László Csaba, Poppe, László, Paizs, Csaba, Toșa, Monica Ioana
Other Authors: European Social Fund, Nemzeti Kutatási Fejlesztési és Innovációs Hivatal
Format: Article in Journal/Newspaper
Language:English
Published: Royal Society of Chemistry (RSC) 2021
Subjects:
Antarc*
Antarctica
Online Access:http://dx.doi.org/10.1039/d1re00342a
http://pubs.rsc.org/en/content/articlepdf/2021/RE/D1RE00342A
id crroyalschem:10.1039/d1re00342a
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spelling crroyalschem:10.1039/d1re00342a 2024-09-15T17:42:59+00:00 Lipase on carbon nanotubes – an active, selective, stable and easy-to-optimize nanobiocatalyst for kinetic resolutions Gal, Cristian Andrei Barabás, Laura Edit Bartha Vári, Judith-Hajnal Moisă, Mădălina Elena Balogh-Weiser, Diana Bencze, László Csaba Poppe, László Paizs, Csaba Toșa, Monica Ioana European Social Fund Nemzeti Kutatási Fejlesztési és Innovációs Hivatal 2021 http://dx.doi.org/10.1039/d1re00342a http://pubs.rsc.org/en/content/articlepdf/2021/RE/D1RE00342A en eng Royal Society of Chemistry (RSC) http://rsc.li/journals-terms-of-use Reaction Chemistry & Engineering volume 6, issue 12, page 2391-2399 ISSN 2058-9883 journal-article 2021 crroyalschem https://doi.org/10.1039/d1re00342a 2024-08-12T04:29:25Z An efficient biocatalyst was obtained by covalent immobilization of lipase B from C. antarctica on functionalized SwCNTs for the kinetic resolution of some aryl-ethanols in batch and continuous-flow modes. Article in Journal/Newspaper Antarc* Antarctica Royal Society of Chemistry Reaction Chemistry & Engineering
institution Open Polar
collection Royal Society of Chemistry
op_collection_id crroyalschem
language English
description An efficient biocatalyst was obtained by covalent immobilization of lipase B from C. antarctica on functionalized SwCNTs for the kinetic resolution of some aryl-ethanols in batch and continuous-flow modes.
author2 European Social Fund
Nemzeti Kutatási Fejlesztési és Innovációs Hivatal
format Article in Journal/Newspaper
author Gal, Cristian Andrei
Barabás, Laura Edit
Bartha Vári, Judith-Hajnal
Moisă, Mădălina Elena
Balogh-Weiser, Diana
Bencze, László Csaba
Poppe, László
Paizs, Csaba
Toșa, Monica Ioana
spellingShingle Gal, Cristian Andrei
Barabás, Laura Edit
Bartha Vári, Judith-Hajnal
Moisă, Mădălina Elena
Balogh-Weiser, Diana
Bencze, László Csaba
Poppe, László
Paizs, Csaba
Toșa, Monica Ioana
Lipase on carbon nanotubes – an active, selective, stable and easy-to-optimize nanobiocatalyst for kinetic resolutions
author_facet Gal, Cristian Andrei
Barabás, Laura Edit
Bartha Vári, Judith-Hajnal
Moisă, Mădălina Elena
Balogh-Weiser, Diana
Bencze, László Csaba
Poppe, László
Paizs, Csaba
Toșa, Monica Ioana
author_sort Gal, Cristian Andrei
title Lipase on carbon nanotubes – an active, selective, stable and easy-to-optimize nanobiocatalyst for kinetic resolutions
title_short Lipase on carbon nanotubes – an active, selective, stable and easy-to-optimize nanobiocatalyst for kinetic resolutions
title_full Lipase on carbon nanotubes – an active, selective, stable and easy-to-optimize nanobiocatalyst for kinetic resolutions
title_fullStr Lipase on carbon nanotubes – an active, selective, stable and easy-to-optimize nanobiocatalyst for kinetic resolutions
title_full_unstemmed Lipase on carbon nanotubes – an active, selective, stable and easy-to-optimize nanobiocatalyst for kinetic resolutions
title_sort lipase on carbon nanotubes – an active, selective, stable and easy-to-optimize nanobiocatalyst for kinetic resolutions
publisher Royal Society of Chemistry (RSC)
publishDate 2021
url http://dx.doi.org/10.1039/d1re00342a
http://pubs.rsc.org/en/content/articlepdf/2021/RE/D1RE00342A
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source Reaction Chemistry & Engineering
volume 6, issue 12, page 2391-2399
ISSN 2058-9883
op_rights http://rsc.li/journals-terms-of-use
op_doi https://doi.org/10.1039/d1re00342a
container_title Reaction Chemistry & Engineering
_version_ 1810489810206326784

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