Purification and Characterization of Laccase from Monodictys asperospera (Cooke & Massee) Ellis
丝孢菌Monodictys asperospera (Cooke & Massee) Ellis漆酶的分离纯化及其酶学性质

A new wood-degrading fungus Monodictys asperospera (Cooke & Massee) Ellis with a high level of laccase production was chosen to study. This laccase was purified by ammonium sulfate precipitation, DEAE-cellulose and sephacryl S-300. Purification of about 8.1 fold was achieved with an overall yield of 5.7%. Its molecular weight was estimated to be about 77 kD. The optimum temperature and pH of the laccase activity were 55°C and 6.0, respectively. Kinetic studies of the laccase showed that the Km and the Vmax for using syringaldazine as substrate was 0.163 mmol/L and 0.194 mmol/(L·min), respectively. The carbohydrate content was 18.14%. In addition, it was found that laccase activity was significantly inhibited by Cu2+.