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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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 |
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Wiley Online Library |
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crwiley |
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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 |
container_start_page |
2870 |
op_container_end_page |
2880 |
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1800741645651542016 |