expression characterization and 246trichlorophenol degradation of laccase from monilinia fructigena a novel laccase gene from monilinia fructigena was synthesized chemically according to the yeast bias codon and integrated into the genome of pichia pastoris gs115 by electroporation the expressed enzyme was recovered from the culture supernatant and purified the result of enzyme activity assay and sdspage demonstrated that the recombinant laccase was induced and extracellularly expressed in p pastoris main biochemical properties of this laccase such as thermodependence and thermostability optimal ph and ph stability and the effect of metal ions and inhibitors were characterized with 22azinobis3ethylbenzothiazoline6sulfonate abts as the substrate mflcc had its optimal ph at 35 and optimal temperature at 45c the km values of the abts guaiacol were 0012 and 0016 mm respectively and the corresponding v max values are 2439 and 1055 um min1 mg1 respectively the recombinant laccase degraded 80 246trichlorophenol after 8 h under the optimal conditions the recombinant strain and its laccase can be considered as candidate for treating waste water polluted with trichlorophenols