Purification and Characterization of Laccase from Monodictys asperospera (Cooke & Massee) Ellis
- VernacularTitle:丝孢菌Monodictys asperospera(Cooke & Massee)Ellis漆酶的分离纯化及其酶学性质
- Author:
Yi-Ning WANG
;
Guo-Zhu ZHAO
;
Yue-Ming ZHAO
;
Xiao-Liang DI
;
Xiang-Ming XIE
;
- Publication Type:Journal Article
- Keywords:
Hyphomycete,Laccase,Fermentation,Enzymatic characteristics
- From:
Microbiology
2008;0(11):-
- CountryChina
- Language:Chinese
-
Abstract:
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 lac-case 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 carbo-hydrate content was 18.14%.In addition,it was found that laccase activity was significantly inhibited by Cu2+.
