Laccase (EC 126.96.36.199) is an extracellular enzymes that is widely used in the decolorization process of textile dye wastewater. The aims of this study was to isolate, purify, and characterize the laccase produced by Trametes pavonia EDN 134 and to explore the laccase ability to decolorize azo textile dyes. Laccase purification process was carried out by fractionation using ammonium sulfate and continued with Hi Trap desalting column chromatography method. The results revealed that the highest laccase specific activity was 8268 U/g and detected in the ammonium sulfate fraction 40-60%. The purification using AKTA-Prime showed that the laccase specific activity enhanced to 98976.61 U/g. The purified laccase activity was optimum at pH 4 and temperature 27°C. The addition of heavy metal ions Hg2+ and Zn2+ reduced the activity of laccase, while Cu2+ and Mn2+ enhanced the activity. In addition, the purified laccase decolorized 200 ppm of Methyl Red (MR), Reactive Black 5 (RB5), and Reactive Red 120 (RR 120) of azo dyes as much as 50.7%, 21.9%, and 35.5%, respectively. This study proposes the potency of the laccase from T. pavonia EDN 134 for decolorization of textile dye wastewater.