Sol-gel Entrapped Candida antarctica lipase B — A Biocatalyst with Excellent Stability for Kinetic Resolution of Secondary Alcohols
Sol-gel entrapment is an efficient immobilization technique that allows preparation of robust and highly stable biocatalysts. Lipase from Candida antarctica B was immobilized by sol-gel entrapment and by sol-gel entrapment combined with adsorption on Celite 545, using a ternary silane precursor syst...
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ftmdpi:oai:mdpi.com:/1420-3049/17/11/13045/ 2023-08-20T04:01:30+02:00 Sol-gel Entrapped Candida antarctica lipase B — A Biocatalyst with Excellent Stability for Kinetic Resolution of Secondary Alcohols Anca Ursoiu Cristina Paul Tibor Kurtán Francisc Péter agris 2012-11-02 application/pdf https://doi.org/10.3390/molecules171113045 EN eng Multidisciplinary Digital Publishing Institute https://dx.doi.org/10.3390/molecules171113045 https://creativecommons.org/licenses/by/3.0/ Molecules; Volume 17; Issue 11; Pages: 13045-13061 lipase sol-gel immobilization ionic liquids additive reusability stability kinetic resolution Text 2012 ftmdpi https://doi.org/10.3390/molecules171113045 2023-07-31T20:30:30Z Sol-gel entrapment is an efficient immobilization technique that allows preparation of robust and highly stable biocatalysts. Lipase from Candida antarctica B was immobilized by sol-gel entrapment and by sol-gel entrapment combined with adsorption on Celite 545, using a ternary silane precursor system. After optimization of the immobilization protocol, the best enzyme loading was 17.4 mg/g support for sol-gel entrapped lipase and 10.7 mg/g support for samples obtained by entrapment and adsorption. Sol-gel immobilized enzymes showed excellent values of enantiomeric ratio E and activity when ionic liquid 1-octyl-3-methyl-imidazolium tetrafluoroborate was used as additive. Immobilization increased the stability of the obtained biocatalysts in several organic solvents. Excellent operational stability was obtained for the immobilized lipase, maintaining unaltered catalytic activity and enantioselectivity during 15 reuse cycles. The biocatalysts were characterized using scanning electron microscopy (SEM) and fluorescence microscopy. The improved catalytic efficiency of entrapped lipases recommends their application for large-scale kinetic resolution of optically active secondary alcohols. Text Antarc* Antarctica MDPI Open Access Publishing Molecules 17 11 13045 13061 |
institution |
Open Polar |
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MDPI Open Access Publishing |
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English |
topic |
lipase sol-gel immobilization ionic liquids additive reusability stability kinetic resolution |
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lipase sol-gel immobilization ionic liquids additive reusability stability kinetic resolution Anca Ursoiu Cristina Paul Tibor Kurtán Francisc Péter Sol-gel Entrapped Candida antarctica lipase B — A Biocatalyst with Excellent Stability for Kinetic Resolution of Secondary Alcohols |
topic_facet |
lipase sol-gel immobilization ionic liquids additive reusability stability kinetic resolution |
description |
Sol-gel entrapment is an efficient immobilization technique that allows preparation of robust and highly stable biocatalysts. Lipase from Candida antarctica B was immobilized by sol-gel entrapment and by sol-gel entrapment combined with adsorption on Celite 545, using a ternary silane precursor system. After optimization of the immobilization protocol, the best enzyme loading was 17.4 mg/g support for sol-gel entrapped lipase and 10.7 mg/g support for samples obtained by entrapment and adsorption. Sol-gel immobilized enzymes showed excellent values of enantiomeric ratio E and activity when ionic liquid 1-octyl-3-methyl-imidazolium tetrafluoroborate was used as additive. Immobilization increased the stability of the obtained biocatalysts in several organic solvents. Excellent operational stability was obtained for the immobilized lipase, maintaining unaltered catalytic activity and enantioselectivity during 15 reuse cycles. The biocatalysts were characterized using scanning electron microscopy (SEM) and fluorescence microscopy. The improved catalytic efficiency of entrapped lipases recommends their application for large-scale kinetic resolution of optically active secondary alcohols. |
format |
Text |
author |
Anca Ursoiu Cristina Paul Tibor Kurtán Francisc Péter |
author_facet |
Anca Ursoiu Cristina Paul Tibor Kurtán Francisc Péter |
author_sort |
Anca Ursoiu |
title |
Sol-gel Entrapped Candida antarctica lipase B — A Biocatalyst with Excellent Stability for Kinetic Resolution of Secondary Alcohols |
title_short |
Sol-gel Entrapped Candida antarctica lipase B — A Biocatalyst with Excellent Stability for Kinetic Resolution of Secondary Alcohols |
title_full |
Sol-gel Entrapped Candida antarctica lipase B — A Biocatalyst with Excellent Stability for Kinetic Resolution of Secondary Alcohols |
title_fullStr |
Sol-gel Entrapped Candida antarctica lipase B — A Biocatalyst with Excellent Stability for Kinetic Resolution of Secondary Alcohols |
title_full_unstemmed |
Sol-gel Entrapped Candida antarctica lipase B — A Biocatalyst with Excellent Stability for Kinetic Resolution of Secondary Alcohols |
title_sort |
sol-gel entrapped candida antarctica lipase b — a biocatalyst with excellent stability for kinetic resolution of secondary alcohols |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2012 |
url |
https://doi.org/10.3390/molecules171113045 |
op_coverage |
agris |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Molecules; Volume 17; Issue 11; Pages: 13045-13061 |
op_relation |
https://dx.doi.org/10.3390/molecules171113045 |
op_rights |
https://creativecommons.org/licenses/by/3.0/ |
op_doi |
https://doi.org/10.3390/molecules171113045 |
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Molecules |
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17 |
container_issue |
11 |
container_start_page |
13045 |
op_container_end_page |
13061 |
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1774724765956702208 |