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The ability of such a common redox mediator as 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonate) (ABTS) to undergo sorption on carbon surfaces is explored here to convert multiwalled carbon nanotubes (CNTs) into a stable colloidal solution of ABTS-modified carbon nanostructures, the diameters of which are approximately 10 nm (as determined by transmission electron microscopy). Subsequently, inks composed of fungal laccase (Cerrena unicolor) mixed with the dispersion of ABTS-modified CNTs and stabilized with Nafion, were deposited on glassy carbon and successfully employed to the reduction of oxygen in McIlvain buffer at pH 5.2. For comparison, the systems utilizing only ABTS-free CNTs and laccase as well as ABTS-modified CNTs did not show appreciable activity toward the oxygen reduction. The three-dimensionally distributed ABTS-modified CNTs are expected to improve the film's overall conductivity and to facilitate electrical connection between the electrode and the enzyme. The network film of ABTS-modified CNTs is rigid, and it is characterized by charge propagation capabilities comparable to the conventional redox polymers. The whole concept of utilization of CNTs modified with ultrathin films of redox mediators in the preparation of efficient bioelectrocatalytic films seems to be of general importance to electroanalytical chemistry and to the development of biosensors.

A membrane‐free biofuel cell (BFC) is reported based on enzymes wired to graphite electrodes by means of Os‐complex modified redox polymers. For the anode cellobiose dehydrogenase (CDH) is used as a biocatalyst whereas for the cathode a laccase was applied. This laccase is a high‐potential laccase and hence able to reduce O2 to H2O at a formal potential higher than +500 mV versus Ag/AgCl. In order to establish efficient electrochemical contact between the enzymes and graphite electrodes electrodeposition polymers containing Os‐complex with specifically designed monomer compositions and formal potentials of the coordinatively bound Os‐complex were synthesised and used to wire the enzymes to the electrodes. The newly designed CDH/Os‐redox polymer anode was characterised at different pH values and optimised with respect to the nature of the polymer and the enzyme‐to‐polymer ratio. The resulting BFC was evaluated running on β‐lactose as a fuel and air/O2 as an oxidising agent. The power output, the maximum current density and the electromotor force (Eemf) were found to be affected by the pH value, resulting in a maximum power output of 1.9 μW cm–2 reached at pH 4.3, a maximum current density of about 13 μA cm–2 at pH 3.5, and the highest Eemf approaching 600 mV at pH 4.0.

The wood-degrading basidiomycete Cerrena unicolor C-139 has been suggested as a potential producer of the industrially important enzyme laccase. Basic culture parameters influencing the enzyme synthesis in shakenflask and aerated bioreactor cultures were evaluated to improve the yields of the process. Production of extracellular laccase was considerably enhanced by the addition of Cu 2+ in the micromolar range to a carbon-sufficient and nitrogen-sufficient culture medium (C/N = 16.69). When an optimised medium containing glucose (10 g/L) and L-asparagine (1.5 g/L) was used, and enzyme synthesis was stimulated by addition of 10 lM Cu 2+ to the culture medium on days 3, 6 and 9, maximal laccase productivity obtained after 17 days' cultivation in shaken flask cultures was above 100,000 nkat/L. In fermenter fungal cultures, the influence of stabilisation of medium pH on laccase activity was additionally studied. The use of a bioreactor with an automatic pH control set at pH 6.5 after 48-h incubation resulted in the enzyme activity of 65,000 nkat/L after 8 days' cultivation.

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