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).

The paper presents a spectral formulation of surface profile irregularity in a wideband frequency range for roughness, waviness and shape components along the measured length. A unique distribution of roughness and waviness components is proposed, according to the nature of their origination in the course of machining with tools of defined cutting edge, as distinct from standard filtration in measurements of surface irregularities. Differences resulting from both formulations are outlined as well as the method of determining the frequency of component separation for surface roughness and waviness.