Lignin peroxidase (EC 1.11.1.14) is a potent, heme-containing enzyme that catalyzes oxidative reactions in the presence of hydrogen peroxide. Its wide-ranging capabilities stem from its effectiveness in degrading xenobiotics and various compounds with both phenolic and non-phenolic structures. The enzyme was isolated and purified from Emericella nidulans using ammonium sulfate precipitation, DEAE-cellulose and Sephadex G200. The specific activity was 416.7 units mg-1 protein, and the purification fold was 148.6 from Sephadex G-200. The Km and Vmax values were determined to be 0.93 mM and 93.3 units mg-1 protein, respectively. The enzyme showed optimal activity at 45°C and pH 5.0. It demonstrated thermostability at 60°C, which was further enhanced by the presence of trehalose (a disaccharide) or sorbitol (a polyol). Additionally, the enzyme maintained good storage stability at 25°C. These results indicate that the fungal lignin peroxidase was purified with appreciable specific activity and thermostability. This offers the enzyme the advantage to be applied in decolorization of synthetic dyes.