SUMMARY: Extracellular laccase (EC of the cultivated mushroom was produced constitutively in defined or complex media. No enzyme induction was found after treatment with cycloheximide or with other potential inducers such as toluidine or xylidine. The enzyme was purified to homogeneity by ammonium sulphate precipitation, ion-exchange chromatography, gel filtration and affinity chromatography. It eluted as a single peak from ion-exchange, gel filtration and affinity columns and sedimented as a single band on centrifugation. It showed four enzymically active bands on electrophoresis and a diffuse band on isoelectric focusing. Its molecular weight was estimated to be about 100000 and the enzyme contained 15% carbohydrate and two atoms of copper per molecule. The substrate specificity was similar to that of other fungal laccases. Antiserum prepared against the purified enzyme gave one major precipitin band.


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