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Updated: Jul 3, 2026

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Published on: December 8, 2020
Oriented immobilization of a fully active monolayer of histidine-tagged recombinant laccase on modified gold
Véronique Balland1, Christelle Hureau, Angela Maria Cusano
1Laboratoire d'Electrochimie Moléculaire, UMR CNRS 7591, Université Paris Diderot, 2 place Jussieu, Paris Cedex 05, France. veronique.balland@univ-paris-diderot.fr
Abstract:
The formation of a dense monolayer of histidine-tagged recombinant laccase on gold electrodes by using a short thiol-NTA linker is described, as well as a kinetic analysis of the process by cyclic voltammetry. From a detailed analysis of the catalytic reduction of dioxygen by laccase in the presence of a one-electron redox mediator it can be concluded that the immobilized enzyme remains as active as in homogeneous solution.
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