Extracellular laccase (Tplac) from Trametes pubescens was purified to homogeneity by a three-step method, which resulted in a high specific activity of 18.543Umg⁻¹, 16.016-fold greater than that of crude enzyme at the same level. Tplac is a monomeric protein that has a molecular mass of 68kDa. The enzyme demonstrated high activity toward 1.0mM ABTS at an optimum pH of 5.0 and temperature of 50°C, and under these conditions, the catalytic efficiency (k_cat/K_m) is 8.34s⁻¹μM⁻¹. Tplac is highly stable and resistant under alkaline conditions, with pH values ranging from 7.0 to 10.0. Interestingly, above 88% of initial enzyme activity was maintained in the presence of metal ions at 25.0mM, leading to an increase in substrate affinity, which indicated that the laccase is highly metal-tolerant. These unusual properties demonstrated that the new fungal laccase Tplac has potentials for the specific industrial or environmental applications.