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丝孢菌Monodictys asperospera (Cooke & Massee) Ellis漆酶的分离纯化及其酶学性质
引用本文:王祎宁,赵国柱,赵悦茗,邸晓亮,谢响明. 丝孢菌Monodictys asperospera (Cooke & Massee) Ellis漆酶的分离纯化及其酶学性质[J]. 微生物学通报, 2009, 36(11): 1710-1715
作者姓名:王祎宁  赵国柱  赵悦茗  邸晓亮  谢响明
作者单位:北京林业大学生物科学与技术学院,北京,100083
基金项目:国家自然科学基金项目(No. 30700647)
摘    要:本研究首次发现Monodictyx asperospera(Cooke&Massee)Ellis具有较好的产漆酶能力.粗酶液经硫酸铵盐析、DEAE-纤维素层析及丙烯葡聚糖凝胶S-300层析纯化,纯化倍数为8.1,回收率为5.7%.漆酶分子量约为77kD,最适反应温度为55℃,最适反应pH6.0,以丁香醛连氮为底物时Km为0.163mm0l/L,Vmax为0.194 mmol(L·min),含糖量为18.14%,Cu2+对漆酶有明显抑制作用.

关 键 词:丝孢菌  漆酶  发酵  酶学性质

Purification and Characterization of Laccase from Monodictys asperospera (Cooke & Massee) Ellis
WANG Yi-Ning,ZHAO Guo-Zhu,ZHAO Yue-Ming,DI Xiao-Liang and XIE Xiang-Ming. Purification and Characterization of Laccase from Monodictys asperospera (Cooke & Massee) Ellis[J]. Microbiology China, 2009, 36(11): 1710-1715
Authors:WANG Yi-Ning  ZHAO Guo-Zhu  ZHAO Yue-Ming  DI Xiao-Liang  XIE Xiang-Ming
Affiliation:College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, China;College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, China;College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, China;College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, China;College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, China
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 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+.
Keywords:Hyphomycete   Laccase   Fermentation   Enzymatic characteristics
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