In this study, the production, partial purification and characterization of a laccase from Botrytis cinerea strain (DSMZ No. 877) was studied. The production of laccase was induced using copper sulphate and Gallic acid as inducers. The maximum laccase activity observed during B. cinerea growth in the presence of 0.1% Gallic acid was 2600 UL−1. Laccase purification was performed by precipitated the enzyme with 90% ammonium sulphate followed by gel filtration chromatography. The optimum pH for the laccase activity was observed at acidic pH values (close to pH 3.5 - 4.6), while the optimum temperature was 70 °C. The ability of the produced laccase as well as the laccase from T. versicolor to catalyse the decolorization of a phenolic dye (phenol red) was also investigated using natural and synthetic mediators. The higher decolorization activity was observed with 1–hydroxybenzotriazole (HBT) as mediator at pH 4.5 and temperature 30° C.