Formation, topography and reactivity ofCandida antarcticalipase B immobilized on silicon surface
Candida antarctica lipase B (CaLB) was immobilized on silicon wafers previously modified with aminopropyltriethoxysilane (APTES) and activated with glutaraldehyde (GLA). The various steps of immobilization were characterized using transmission FTIR, AFM, contact angle measurements and XPS. Furthermo...
Published in: | Biocatalysis and Biotransformation |
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2010
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ftunivkragujevac:oai:https://scidar.kg.ac.rs:123456789/19847 2024-09-15T17:46:25+00:00 Formation, topography and reactivity ofCandida antarcticalipase B immobilized on silicon surface Miletic Nemanja, Nemanja Fahriansyah, null Nguyen, Le-Thu T. Loos, Katja 2010 application/pdf https://scidar.kg.ac.rs/handle/123456789/19847 https://doi.org/10.3109/10242422.2010.531712 unknown Informa Healthcare, London, England, UK Miletić, N., Fahriansyah, L.T.T. Nguyen, K. Loos. (2010): Formation, topography and reactivity of Candida antarctica lipase B immobilized on silicon surface. Biocatalysis and Biotransformations, 28(5-6), 357-369. 1024-2422 https://scidar.kg.ac.rs/handle/123456789/19847 doi:10.3109/10242422.2010.531712 000285554000008 info:eu-repo/semantics/openAccess Biocatalysis and Biotransformation Enzyme immobilization Candida antarctica lipase B Silanization Glutaraldehyde activation Silicon surface article PublishedVersion 2010 ftunivkragujevac https://doi.org/10.3109/10242422.2010.531712 2024-07-11T23:30:40Z Candida antarctica lipase B (CaLB) was immobilized on silicon wafers previously modified with aminopropyltriethoxysilane (APTES) and activated with glutaraldehyde (GLA). The various steps of immobilization were characterized using transmission FTIR, AFM, contact angle measurements and XPS. Furthermore, the formation of APTES films during the initial immobilization step was additionally analyzed by ellipsometry and an ‘ island ’ monolayer film formation was revealed. When the concentration of APTES was increased, the amount of immobilized lipase also increased. On the other hand, while the activity of immobilized enzyme in lipase-catalyzed transesterification of 6,8-difluoro-4-methylumbelliferyl octanoate initially increased, showing the highest value when 0.00050% w/v APTES solution was used for the initial immobilization step, it subsequently decreased. Comparison of enzyme activity and surface filling results indicate that there has to be multilayer formation in the enzyme layer, as revealed by AFM images and determination of enzyme loading. Published Article in Journal/Newspaper Antarc* Antarctica SCIDAR - A Digital Archive of the University of Kragujevac Biocatalysis and Biotransformation 28 5-6 357 369 |
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SCIDAR - A Digital Archive of the University of Kragujevac |
op_collection_id |
ftunivkragujevac |
language |
unknown |
topic |
Enzyme immobilization Candida antarctica lipase B Silanization Glutaraldehyde activation Silicon surface |
spellingShingle |
Enzyme immobilization Candida antarctica lipase B Silanization Glutaraldehyde activation Silicon surface Miletic Nemanja, Nemanja Fahriansyah, null Nguyen, Le-Thu T. Loos, Katja Formation, topography and reactivity ofCandida antarcticalipase B immobilized on silicon surface |
topic_facet |
Enzyme immobilization Candida antarctica lipase B Silanization Glutaraldehyde activation Silicon surface |
description |
Candida antarctica lipase B (CaLB) was immobilized on silicon wafers previously modified with aminopropyltriethoxysilane (APTES) and activated with glutaraldehyde (GLA). The various steps of immobilization were characterized using transmission FTIR, AFM, contact angle measurements and XPS. Furthermore, the formation of APTES films during the initial immobilization step was additionally analyzed by ellipsometry and an ‘ island ’ monolayer film formation was revealed. When the concentration of APTES was increased, the amount of immobilized lipase also increased. On the other hand, while the activity of immobilized enzyme in lipase-catalyzed transesterification of 6,8-difluoro-4-methylumbelliferyl octanoate initially increased, showing the highest value when 0.00050% w/v APTES solution was used for the initial immobilization step, it subsequently decreased. Comparison of enzyme activity and surface filling results indicate that there has to be multilayer formation in the enzyme layer, as revealed by AFM images and determination of enzyme loading. Published |
format |
Article in Journal/Newspaper |
author |
Miletic Nemanja, Nemanja Fahriansyah, null Nguyen, Le-Thu T. Loos, Katja |
author_facet |
Miletic Nemanja, Nemanja Fahriansyah, null Nguyen, Le-Thu T. Loos, Katja |
author_sort |
Miletic Nemanja, Nemanja |
title |
Formation, topography and reactivity ofCandida antarcticalipase B immobilized on silicon surface |
title_short |
Formation, topography and reactivity ofCandida antarcticalipase B immobilized on silicon surface |
title_full |
Formation, topography and reactivity ofCandida antarcticalipase B immobilized on silicon surface |
title_fullStr |
Formation, topography and reactivity ofCandida antarcticalipase B immobilized on silicon surface |
title_full_unstemmed |
Formation, topography and reactivity ofCandida antarcticalipase B immobilized on silicon surface |
title_sort |
formation, topography and reactivity ofcandida antarcticalipase b immobilized on silicon surface |
publisher |
Informa Healthcare, London, England, UK |
publishDate |
2010 |
url |
https://scidar.kg.ac.rs/handle/123456789/19847 https://doi.org/10.3109/10242422.2010.531712 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Biocatalysis and Biotransformation |
op_relation |
Miletić, N., Fahriansyah, L.T.T. Nguyen, K. Loos. (2010): Formation, topography and reactivity of Candida antarctica lipase B immobilized on silicon surface. Biocatalysis and Biotransformations, 28(5-6), 357-369. 1024-2422 https://scidar.kg.ac.rs/handle/123456789/19847 doi:10.3109/10242422.2010.531712 000285554000008 |
op_rights |
info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.3109/10242422.2010.531712 |
container_title |
Biocatalysis and Biotransformation |
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28 |
container_issue |
5-6 |
container_start_page |
357 |
op_container_end_page |
369 |
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1810494545824055296 |