Immobilization of Candida antarctica Lipase B on Silicone Nanofilaments
Candida antarctica lipase B was immobilized on a series of silicone nanofilament-coated matrices of different porosities. In addition to creating a more open surface, SNF’s hydrophobicity allows for a simple immobilization pathway via adsorption. In order to study the impact of the nanostructure, th...
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2021
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ftunivzuerich:oai:www.zora.uzh.ch:207943 2024-06-23T07:45:56+00:00 Immobilization of Candida antarctica Lipase B on Silicone Nanofilaments Naef, Noah U Seeger, Stefan Karimi-Maleh, Hassan Karimi-Maleh, H ( Hassan ) 2021-02-05 application/pdf https://www.zora.uzh.ch/id/eprint/207943/ https://www.zora.uzh.ch/id/eprint/207943/8/8812240.pdf https://www.zora.uzh.ch/id/eprint/207943/1/Journal_of_Nanomaterials_SNF_Enzyme_catalysis_revised_version.pdf https://doi.org/10.5167/uzh-207943 https://doi.org/10.1155/2021/8812240 eng eng Hindawi Publishing Corporation https://www.zora.uzh.ch/id/eprint/207943/8/8812240.pdf https://www.zora.uzh.ch/id/eprint/207943/1/Journal_of_Nanomaterials_SNF_Enzyme_catalysis_revised_version.pdf doi:10.5167/uzh-207943 doi:10.1155/2021/8812240 urn:issn:1687-4110 info:eu-repo/semantics/openAccess Creative Commons: Attribution 4.0 International (CC BY 4.0) http://creativecommons.org/licenses/by/4.0/ Naef, Noah U; Seeger, Stefan (2021). Immobilization of Candida antarctica Lipase B on Silicone Nanofilaments. Journal of Nanomaterials, 2021:8812240. Department of Chemistry 540 Chemistry General Materials Science Journal Article PeerReviewed info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/acceptedVersion 2021 ftunivzuerich https://doi.org/10.5167/uzh-20794310.1155/2021/8812240 2024-05-29T01:11:17Z Candida antarctica lipase B was immobilized on a series of silicone nanofilament-coated matrices of different porosities. In addition to creating a more open surface, SNF’s hydrophobicity allows for a simple immobilization pathway via adsorption. In order to study the impact of the nanostructure, the performance was compared with control samples lacking SNFs. For all materials, the surface was characterized with BET measurements, and the immobilized enzyme was measured as well as the catalytic activity. Enzyme loads ranged between 3.85% and 2.53% and decreased with the decreasing surface area of the carrier material from 200 m2/g to 0.04 m2/g, while the activity per enzyme increases from 824 U to 2040 U. The data suggest that the coating seals off inner surfaces, forcing the enzyme to be immobilized at more accessible positions allowing for higher activity per enzyme. Optimization of the immobilization conditions allowed us to create a thinner enzyme layer which further improved the activity per enzyme to 3129 U. While this activity is comparable to the commercial Novozyme 435 with 3073 U, the SNF-based system performs the catalysis in a thin surface layer of around 13 μm. A favorite area of application is, for example, the creation of enzyme-based detection systems, where the high activity per surface area of up to 89622 Umg/m2 would lead to high signal strength. Article in Journal/Newspaper Antarc* Antarctica University of Zurich (UZH): ZORA (Zurich Open Repository and Archive |
institution |
Open Polar |
collection |
University of Zurich (UZH): ZORA (Zurich Open Repository and Archive |
op_collection_id |
ftunivzuerich |
language |
English |
topic |
Department of Chemistry 540 Chemistry General Materials Science |
spellingShingle |
Department of Chemistry 540 Chemistry General Materials Science Naef, Noah U Seeger, Stefan Immobilization of Candida antarctica Lipase B on Silicone Nanofilaments |
topic_facet |
Department of Chemistry 540 Chemistry General Materials Science |
description |
Candida antarctica lipase B was immobilized on a series of silicone nanofilament-coated matrices of different porosities. In addition to creating a more open surface, SNF’s hydrophobicity allows for a simple immobilization pathway via adsorption. In order to study the impact of the nanostructure, the performance was compared with control samples lacking SNFs. For all materials, the surface was characterized with BET measurements, and the immobilized enzyme was measured as well as the catalytic activity. Enzyme loads ranged between 3.85% and 2.53% and decreased with the decreasing surface area of the carrier material from 200 m2/g to 0.04 m2/g, while the activity per enzyme increases from 824 U to 2040 U. The data suggest that the coating seals off inner surfaces, forcing the enzyme to be immobilized at more accessible positions allowing for higher activity per enzyme. Optimization of the immobilization conditions allowed us to create a thinner enzyme layer which further improved the activity per enzyme to 3129 U. While this activity is comparable to the commercial Novozyme 435 with 3073 U, the SNF-based system performs the catalysis in a thin surface layer of around 13 μm. A favorite area of application is, for example, the creation of enzyme-based detection systems, where the high activity per surface area of up to 89622 Umg/m2 would lead to high signal strength. |
author2 |
Karimi-Maleh, Hassan Karimi-Maleh, H ( Hassan ) |
format |
Article in Journal/Newspaper |
author |
Naef, Noah U Seeger, Stefan |
author_facet |
Naef, Noah U Seeger, Stefan |
author_sort |
Naef, Noah U |
title |
Immobilization of Candida antarctica Lipase B on Silicone Nanofilaments |
title_short |
Immobilization of Candida antarctica Lipase B on Silicone Nanofilaments |
title_full |
Immobilization of Candida antarctica Lipase B on Silicone Nanofilaments |
title_fullStr |
Immobilization of Candida antarctica Lipase B on Silicone Nanofilaments |
title_full_unstemmed |
Immobilization of Candida antarctica Lipase B on Silicone Nanofilaments |
title_sort |
immobilization of candida antarctica lipase b on silicone nanofilaments |
publisher |
Hindawi Publishing Corporation |
publishDate |
2021 |
url |
https://www.zora.uzh.ch/id/eprint/207943/ https://www.zora.uzh.ch/id/eprint/207943/8/8812240.pdf https://www.zora.uzh.ch/id/eprint/207943/1/Journal_of_Nanomaterials_SNF_Enzyme_catalysis_revised_version.pdf https://doi.org/10.5167/uzh-207943 https://doi.org/10.1155/2021/8812240 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Naef, Noah U; Seeger, Stefan (2021). Immobilization of Candida antarctica Lipase B on Silicone Nanofilaments. Journal of Nanomaterials, 2021:8812240. |
op_relation |
https://www.zora.uzh.ch/id/eprint/207943/8/8812240.pdf https://www.zora.uzh.ch/id/eprint/207943/1/Journal_of_Nanomaterials_SNF_Enzyme_catalysis_revised_version.pdf doi:10.5167/uzh-207943 doi:10.1155/2021/8812240 urn:issn:1687-4110 |
op_rights |
info:eu-repo/semantics/openAccess Creative Commons: Attribution 4.0 International (CC BY 4.0) http://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.5167/uzh-20794310.1155/2021/8812240 |
_version_ |
1802643043339206656 |