Purification and characterization of laccase from curvularia trifol

Electrophoretic pure lacquer enzymes were obtained from the thick enzyme of Gladiolus Curvularia trifol with grading precipitation and DEAE2-Cellulose ion exchange chromatography. The overall recycling rate of enzyme activity was 14.97% and the purification reached 2.96 times. The relative molecular mass of enzyme was 92.3Kda. The optimal temperature and pH were 40 degrees C and 3.5, respectively. The K-m of ABTS catalyzed by laccase was 1.11x 10(-5) mol L-1. Alizarin red and Congo red could be degradated by purified laccase effectively without the participation of small molecule amboceptor. Alizarin red could be degradated by 80% with its being affected by 1000U/L of enzyme activity for 70h, which revealed the huge potentiality of Gladiolus Curvularia trifol and laccase in the degradation of dye.