This review concerns copper-containing oxidases--laccases. Principal biochemical and electrochemical properties of laccases isolated from different sources are described, as well as their structure and mechanism of catalysis. Possible applications of laccases in different fields of biotechnology are discussed.

No abstract

No abstract

No abstract

We report on the assembly and characterisation of a high potential, stable, mediator‐less and cofactor free biocathode based on a fungal laccase (Lc), adsorbed on highly dispersed carbonaceous materials. First, the stability and activity of Trametes hirsuta Lc immobilised on different carbon particles were studied and compared to the solubilised enzyme. Based on the experimental results and a literature analysis, the carbonaceous material BM‐4 was chosen to design efficient and stable biocatalysts for the production of a ‘floating' air diffusion Lc‐based biocathode. Voltammetric characteristics and operational stability of the biocathode were investigated. The current density of oxygen reduction at the motionless biocathode in a quiet, air saturated citrate buffer (100 mM, pH 4.5, 23 °C) reached values as high as 0.3 mA cm–2 already at 0.7 V versus NHE. The operational stability of the biocathode depended on the current density of the device. For example, at low current density (20 μA cm–2), the biocathode lost only 5× of its initial power after 1 month of continuous operation. However, when the device was polarised at 150 mV it lost more than 32× of its initial power in just 10 min. We also found that co‐immobilisation of Lc and peroxidase on highly dispersed carbon materials could protect the biocatalyst from rapid inactivation by hydrogen peroxide produced during electrocatalytic reactions at high‐current densities.