Oriented Immobilization of a Fully Active Monolayer of Histidine‐Tagged Recombinant Laccase on Modified Gold Electrodes
2008; Wiley; Volume: 14; Issue: 24 Linguagem: Inglês
10.1002/chem.200800368
ISSN1521-3765
AutoresVéronique Balland, Christelle Hureau, Angela Maria Cusano, Yingli Liu, Thierry Tron, Benoı̂t Limoges,
Tópico(s)Advanced biosensing and bioanalysis techniques
ResumoAbstract 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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