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Laccases (EC 1.10.3.2) are a class of multi-copper oxidases with important industrial values. A basidiomycete strain  Cerrena  sp. HYB07 with high laccase yield was identified. After cultivation in the shaking flask for 4 days, a maximal activity of 210.8 U mL −1  was attained. A 58.6-kDa laccase (LacA) with 7.2% carbohydrate and a specific activity of 1952.4 U mg −1  was purified. 2,2′-Azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) was the optimal substrate, with  K   m  and  k   cat  being 93.4 µM and 2468.0 s −1 , respectively. LacA was stable at 60°C, pH 5.0 and above, and in organic solvents. Metal ions Na + , K + , Ca 2+ , Mg 2+ , Mn 2+ , Zn 2+  enhanced LacA activity, while Fe 2+  and Li +  inhibited LacA activity. LacA decolorized structurally different dyes and a real textile effluent. Its gene and cDNA sequences were obtained. Putative  cis -acting transcriptional response elements were identified in the promoter region. The high production yield and activity, robustness and dye decolorizing capacity make LacA and  Cerrena  sp. HYB07 potentially useful for industrial and environmental applications such as textile finishing and wastewater treatment.

Purification and Characterization of a Novel Laccase from Cerrena sp. HYB07 with Dye Decolorizing Ability