Production of laccase using a submerged culture of Trametes versicolor sdu-4 was optimized using a central composite design of the Response Surface Methodology. Optimized conditions gave a laccase yield of 4,213 U/L which was approximately three times of that in basal medium. The laccase was purified to homogeneity using a three-step process. The overall yield of the purification was 58%, with a purification fold of 11.4 and a specific activity of 1320.7 U/mg protein. The molecular mass of the laccase was 60 kDa. The optimum pH values of the enzyme were 2.2, 3.7, and 7 for the oxidations of ABTS, DMP, and syringaldazine, respectively. The enzyme had adaptability to a broad pH range and high temperature and was stable at pH 3.0 ~ 10.0. The half-life of this laccase at $70^{circ}C$ was 2.2 h. Methyl red, 2-bromophenol, and 4-bromophenol were oxidized by the purified laccase in the absence of mediators. Purified laccase was effective in the decolorization of several dyes and was not inhibited by $Cu^{2+}$, $Mn^{2+}$, $Zn^{2+}$, $Na^+$, $K^+$, $Mg^{2+}$, $Ba^{2+}$, and $Ca^{2+}$ at 5 mM. These excellent characteristics made it a highly attractive candidate for industrial use.