Extracellular laccase produced by the wood-rotting fungus Cerrena unicolor was immobilised covalently on the mesostructured siliceous foam (MCF) and three hexagonally ordered mesoporous silicas (SBA-15) with different pore sizes. The enzyme was attached covalently via glutaraldehyde (GLA) or by simple adsorption and additionally crosslinked with GLA. The experiments indicated that laccase bound by covalent attachment remains very active and stable. The best biocatalysts were MCF and SBA-15 with Si-F moieties on their surface. Thermal inactivation of immobilised and native laccase at 80°C showed a biphasic-type activity decay, that could be modelled with 3- parameter isoenzyme model. It appeared that immobilisation did not significantly change the mechanism of activity loss but stabilised a fraction of a stable isoform. Examination of time needed for 90% initial activity loss revealed that immobilisation prolonged that time from 8 min (native enzyme) up to 155 min (SBA-15SF).