The laccase induction in submerged culture of basidiomycete Cerrena unicolor VKM F-3196 was investigated. Cu(2+) at concentration 0.1 mM was an optimum inducer of C. unicolor laccase. Two isoforms of laccase, namely LacC1 and LacC2, were isolated and characterized. The isoforms were shown to have different physical-chemical and catalytic properties. On the basis of the MALDI TOF MS analysis of tryptic cleavage products of both the proteins and N-terminal amino-acid sequences analysis two isoforms of laccase (LacC1 and LacC2) were classified as products of two different genes.