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Issue 12, 2014
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Mesoporous titania thin films as efficient enzyme carriers for paraoxon determination/detoxification: effects of enzyme binding and pore hierarchy on the biocatalyst activity and reusability

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Abstract

In this work we demonstrate the efficient immobilization of histidine 6-tagged organophosphate hydrolase (His6–OPH), an organophosphate-degrading enzyme, on mesoporous titania thin films. This permits the use of the biocatalyst films as efficient tools in the detection/detoxification of paraoxon. His6–OPH was immobilized on mesoporous thin films with uniform (9 nm) and bimodal (13–38 nm) pore size distribution, through covalent attachment and physical adsorption. The biocatalyst films show good activity, and enhanced stability with respect to the free enzyme at extreme conditions of pH and temperature, especially around neutral pH and room temperature. In addition, the bioactive films can be easily separated from the reaction media and reused multiple times without significant loss of activity.

Graphical abstract: Mesoporous titania thin films as efficient enzyme carriers for paraoxon determination/detoxification: effects of enzyme binding and pore hierarchy on the biocatalyst activity and reusability

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Article information


Submitted
21 Jan 2014
Accepted
22 Jan 2014
First published
29 Jan 2014

Analyst, 2014,139, 3127-3136
Article type
Paper

Mesoporous titania thin films as efficient enzyme carriers for paraoxon determination/detoxification: effects of enzyme binding and pore hierarchy on the biocatalyst activity and reusability

N. Frančič, M. G. Bellino, G. J. A. A. Soler-Illia and A. Lobnik, Analyst, 2014, 139, 3127
DOI: 10.1039/C4AN00152D

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