ABSTRACT
A laccase has been isolated from Fusarium sp. FW2PhC1 and characterized. The highest extracellular laccase production from the fungus was observed as 43.41 U/ml using sodium acetate buffer (100 mM, pH-5.0) on day 14 in static condition. The pH and temperature optima of the enzyme were 5.0 and 30°C, respectively. The enzyme was stable in the pH range from 4.0 to 10.0 and at temperatures below 40ºC. Protein concentration of the enzyme was estimated to be 0.31 mg/ml by using Lowry method. The laccase showed the highest substrate specificity for DMP (2,6-dimethoxyphenol) as a substrate. The Km and Vmax of the laccase were 3.27 mM and 196.07 U/mg, respectively for the substrate DMP. About 20 U/ml of the crude laccase, efficiently decolorized three industrial dyes neutral red (67%), indigo carmine (63%) and methyl green (58%) at a concentration of 50 µM after 24 h of incubation at 30°C.
