The laccase gene lacB3 and its corresponding full-length cDNA were cloned and characterized from the endophytic fungus Phomopsis liquidambari.The cloned lacB3 is 1867 bp in length, harboring the full-length cDNA sequence as well as two short introns of 58 and 78 bp.The 173 i bp full-length lacB3 cDNA encoded a mature laccase protein containing 576 amino acids preceded by a signal peptide of 20 amino acids.This protein sequence showed a 59% match to other known fungal laccases.The recombinant laccase (rLACB3) is active over a broad pH (2-6)and temperature (20-80 ℃) range, with optima at pH 2.5 and 50 ℃.rLACB3 is stimulated by Mg2+, methanol, ethanol, acetonitrile; and inhibited by Fe2+ and NaN3.Furthermore, rLACB3 could catalyze a 79.2-94.9% decolorization of selected dyes.These results laid a solid foundation for the use of the Phomnopsis liquidambari laccase in industrial and/or environmental applications.