Lipase B of Candida antarctica co‐adsorbed with polyols onto TiO 2 nanoparticles for improved biocatalytic performance

Abstract BACKGROUND The immobilization of the lipase B of Candida antarctica CALB over TiO 2 nanoparticles was thoroughly investigated with the isotherms of adsorption at various temperatures with and without the addition of sorbitol and glycerol. The surface composition, secondary structure and the...

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Published in:Journal of Chemical Technology & Biotechnology
Main Authors: Llerena Suster, Carlos R, Toledo, María Victoria, Fittipaldi, Antonela S, Morcelle, Susana R, Briand, Laura E
Other Authors: Consejo Nacional de Investigaciones Científicas y Técnicas, Universidad Nacional de La Plata
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2017
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Online Access:http://dx.doi.org/10.1002/jctb.5305
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spelling crwiley:10.1002/jctb.5305 2024-06-02T07:58:20+00:00 Lipase B of Candida antarctica co‐adsorbed with polyols onto TiO 2 nanoparticles for improved biocatalytic performance Llerena Suster, Carlos R Toledo, María Victoria Fittipaldi, Antonela S Morcelle, Susana R Briand, Laura E Consejo Nacional de Investigaciones Científicas y Técnicas Universidad Nacional de La Plata 2017 http://dx.doi.org/10.1002/jctb.5305 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fjctb.5305 https://onlinelibrary.wiley.com/doi/pdf/10.1002/jctb.5305 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Journal of Chemical Technology & Biotechnology volume 92, issue 11, page 2870-2880 ISSN 0268-2575 1097-4660 journal-article 2017 crwiley https://doi.org/10.1002/jctb.5305 2024-05-03T11:19:29Z Abstract BACKGROUND The immobilization of the lipase B of Candida antarctica CALB over TiO 2 nanoparticles was thoroughly investigated with the isotherms of adsorption at various temperatures with and without the addition of sorbitol and glycerol. The surface composition, secondary structure and the effect of the addition of the polyols was addressed. RESULTS The maximum dispersion limit of protein on TiO 2 nanoparticles (NPs) is 0.073 ± 0.007 µmol m −2 . Glycerol and sorbitol co‐adsorb on the TiO 2 NPs reaching 45% of the surface composition of the biocatalyst. The optimized material was able to catalyze the esterification of 52% of R/S‐ibuprofen with ethanol (0.31 ± 0.01 µmol min −1 mg −1 ) with 41% of enantiomeric excess towards S(+)‐ibuprofen in 24 h reaction. Under similar reaction conditions, the commercial counterpart Novozym® 435 showed 34% conversion (0.091 ± 0.003 µmol min −1 mg −1 ) and 16% of enantiomeric excess. CONCLUSIONS The molecular association between the protein and the polyols exerts a positive cooperativism which prevents aggregation of the protein and protects its active conformation. The residual esterase activity of the immobilized CALB compared with the free lipase depends directly on the amount of co‐adsorbed polyols. Moreover, polyols boost the catalytic performance in the kinetic resolution of racemic ibuprofen showing an optimum at the maximum coverage of polyols on the biocatalysts. © 2017 Society of Chemical Industry Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library Journal of Chemical Technology & Biotechnology 92 11 2870 2880
institution Open Polar
collection Wiley Online Library
op_collection_id crwiley
language English
description Abstract BACKGROUND The immobilization of the lipase B of Candida antarctica CALB over TiO 2 nanoparticles was thoroughly investigated with the isotherms of adsorption at various temperatures with and without the addition of sorbitol and glycerol. The surface composition, secondary structure and the effect of the addition of the polyols was addressed. RESULTS The maximum dispersion limit of protein on TiO 2 nanoparticles (NPs) is 0.073 ± 0.007 µmol m −2 . Glycerol and sorbitol co‐adsorb on the TiO 2 NPs reaching 45% of the surface composition of the biocatalyst. The optimized material was able to catalyze the esterification of 52% of R/S‐ibuprofen with ethanol (0.31 ± 0.01 µmol min −1 mg −1 ) with 41% of enantiomeric excess towards S(+)‐ibuprofen in 24 h reaction. Under similar reaction conditions, the commercial counterpart Novozym® 435 showed 34% conversion (0.091 ± 0.003 µmol min −1 mg −1 ) and 16% of enantiomeric excess. CONCLUSIONS The molecular association between the protein and the polyols exerts a positive cooperativism which prevents aggregation of the protein and protects its active conformation. The residual esterase activity of the immobilized CALB compared with the free lipase depends directly on the amount of co‐adsorbed polyols. Moreover, polyols boost the catalytic performance in the kinetic resolution of racemic ibuprofen showing an optimum at the maximum coverage of polyols on the biocatalysts. © 2017 Society of Chemical Industry
author2 Consejo Nacional de Investigaciones Científicas y Técnicas
Universidad Nacional de La Plata
format Article in Journal/Newspaper
author Llerena Suster, Carlos R
Toledo, María Victoria
Fittipaldi, Antonela S
Morcelle, Susana R
Briand, Laura E
spellingShingle Llerena Suster, Carlos R
Toledo, María Victoria
Fittipaldi, Antonela S
Morcelle, Susana R
Briand, Laura E
Lipase B of Candida antarctica co‐adsorbed with polyols onto TiO 2 nanoparticles for improved biocatalytic performance
author_facet Llerena Suster, Carlos R
Toledo, María Victoria
Fittipaldi, Antonela S
Morcelle, Susana R
Briand, Laura E
author_sort Llerena Suster, Carlos R
title Lipase B of Candida antarctica co‐adsorbed with polyols onto TiO 2 nanoparticles for improved biocatalytic performance
title_short Lipase B of Candida antarctica co‐adsorbed with polyols onto TiO 2 nanoparticles for improved biocatalytic performance
title_full Lipase B of Candida antarctica co‐adsorbed with polyols onto TiO 2 nanoparticles for improved biocatalytic performance
title_fullStr Lipase B of Candida antarctica co‐adsorbed with polyols onto TiO 2 nanoparticles for improved biocatalytic performance
title_full_unstemmed Lipase B of Candida antarctica co‐adsorbed with polyols onto TiO 2 nanoparticles for improved biocatalytic performance
title_sort lipase b of candida antarctica co‐adsorbed with polyols onto tio 2 nanoparticles for improved biocatalytic performance
publisher Wiley
publishDate 2017
url http://dx.doi.org/10.1002/jctb.5305
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fjctb.5305
https://onlinelibrary.wiley.com/doi/pdf/10.1002/jctb.5305
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source Journal of Chemical Technology & Biotechnology
volume 92, issue 11, page 2870-2880
ISSN 0268-2575 1097-4660
op_rights http://onlinelibrary.wiley.com/termsAndConditions#vor
op_doi https://doi.org/10.1002/jctb.5305
container_title Journal of Chemical Technology & Biotechnology
container_volume 92
container_issue 11
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