Sorption-assisted surface conjugation: a way to stabilize laccase enzyme |
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Authors: | Zimmermann Yannick-Serge Shahgaldian Patrick Corvini Philippe F X Hommes Gregor |
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Institution: | (1) Institute for Ecopreneurship, School of Life Sciences, University of Applied Sciences Northwestern Switzerland, Gr?ndenstrasse 40, Muttenz, CH-4132, Switzerland;(2) Institute for Chemistry and Bioanalytics, School of Life Sciences, University of Applied Sciences Northwestern Switzerland, Gr?ndenstrasse 40, Muttenz, CH-4132, Switzerland;(3) School of the Environment, Nanjing University, Hankou Road 22, 210093 Nanjing, China; |
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Abstract: | Enyzme immobilization on solid surfaces is one of the most relevant methods to improve enzyme activity and stability under
harsh conditions over extended periods. A typically interesting application is the immobilization of laccases, multicopper
enzymes oxidizing aromatic compounds, to solid surfaces in order to develop valuable tools for the elimination of micropollutants
in wastewater. Laccase of the white-rot fungus Coriolopsis polyzona has been successfully immobilized on fumed silica nanoparticles using a novel method. It consists in the sorption of the
enzyme to amino-modified silica nanoparticles and the subsequent covalent cross-linking using glutaraldehyde as a homobifunctional
linker. The so-produced nanoparticulate material has been characterized by means of scanning electron microscopy and Brunauer–Emmett–Teller
surface area analysis revealing modifications of the surface structure and area during the coupling procedure. Laccase immobilization
on spherical nanoparticles produced according to the method of St?ber has been shown to be much less efficient than on fumed
silica nanoparticles. Long-term stability assays revealed that the novel developed method allows a drastic stabilization of
the enzyme. In real wastewater, 77% of the laccase activity remained on the nanoparticles over 1 month, whereas the activity
of free laccase dropped to 2.5%. The activity loss on the nanoparticles resulted from partial inactivation of the immobilized
enzymes and additional release into the surrounding solution with subsequent fast inactivation of the free enzymes, since
almost no activity was found in the supernatants. |
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