Laccase produced by the white rot fungus Trametes sanguinea M85-2 was purified and crystallized. Purification of the enzyme was performed by chromatographies on DEAE- and phenyl-Troyopearl at room temperature. The enzyme was purified to an almost homogeneous state about 6-fold with a yield of 73% from the culture filtrate. The molecular mass of the enzyme was determined to be 62 kDa by SDS-PAGE and the enzyme to be a monomeric glycoprotein containing 9.1% carbohydrate. The purified laccase had 3.3 atoms of copper per enzyme molecule and an isoelectric point of 3.5. The optimum pH and temperature for maximum enzyme activity were 5.0 and 60 degrees C, respectively, The enzyme was stable in a PH range from 5 to 10 and at pH 6.0 for 2 weeks at 25 degrees C. The substrate specificity was broad and the enzyme activity was potently inhibited by compounds such as azide and cyanide.