Laccases comprise a class of multi-copper containing oxidases that are environmentally friendly and industrially important.Laccases have low substrate specificity and can oxidize a wide range of substrates such as phenolic lignin compounds,recalcitrant dyestuffs and other environment pollutants,accompanied by concomitant reduction of molecular oxygen to water.We have previously isolated a white-rot fungus Cerrena sp.strain HYB07,which produced laccase with high yields,high activity and wide substrate range.The HYB07 laccase gene family contained at least eight isozymes,among which,Lac7 was the major laccase expressed.Indeed,transcription levels of Lac7 correlated with fungal laccase yields.Cerrena laccase showed strong potentials in biodegradation;it could oxidize various organic contaminants including polycyclic aromatic hydrocarbons,phthalate esters,antimicrobials and dyestuffs including malachite green and Coomassie Brilliant Blue.Degradation products of malachite green were identified with LC-TOF MS,and laccase appeared to transform malachite green via two simultaneous pathways.Laccase was also used to detain polyacrylamide gels stained with Coomassie Brilliant Blue R-250.The method did not require organic solvents or changing the destaining solution.Due to simultaneous gel destaining and dye decolorization,the colorless destaining solution can be disposed of directly.Laccase destaining of polyacrylamide gels was simple,efficient,and environmentally friendly.Immobilization of Cerrena laccase displayed enhanced thermo-stability and tolerance to organic solvents,metal ions and NaCl.Laccase CLEAs also displayed greater velocity and efficiency in Remazol Brilliant Blue Reactive decolorization in the presence of NaCl than free laccase.The research findings served to facilitate understanding and industrial applications of laccase.