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Immobilization of Candida antarctica Lipase B on Silicone Nanofilaments


Naef, Noah U; Seeger, Stefan (2021). Immobilization of Candida antarctica Lipase B on Silicone Nanofilaments. Journal of Nanomaterials, 2021:8812240.

Abstract

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.

Abstract

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.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Scopus Subject Areas:Physical Sciences > General Materials Science
Uncontrolled Keywords:General Materials Science
Language:English
Date:5 February 2021
Deposited On:21 Oct 2021 13:22
Last Modified:22 Oct 2021 20:01
Publisher:Hindawi Publishing Corporation
ISSN:1687-4110
OA Status:Gold
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1155/2021/8812240

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