Abstract
Tyrosinase from Agaricus bisporus was immobilised covalently on mesostructured siliceous foam (MCF) and three mesoporous silicas of SBA-15 type of different pore sizes, regarded as the reference, to reveal that MCF was the superior enzyme support. All the carriers were functionalised using 3-aminopropyltrimethoxysilane and the enzyme was attached covalently via glutaraldehyde or by simple adsorption and it was also cross-linked with glutaraldehyde in selected samples. The experiments indicated that only tyrosinase attached covalently was highly active and that postimmobilisation cross-linking slightly reduced its activity with no improvement in stability. MCFbound tyrosinase was the best biocatalyst with monophenolase and diphenolase activities of 3627 U mL−1 and 53040 U mL−1 of carrier sediment, respectively. Inactivation studies at 55°C showed that MCF-bound tyrosinase was 20 times more stable than the native enzyme, whereas for typical SBA-15 it was only 12 times. A comparative study with other, non-siliceous enzyme supports indicated that aminated MCF appeared to be the carrier of choice for the covalent attachment of tyrosinase.
References
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