%0 Journal Article
%T Purification and properties of manganese peroxidase from Trametes versicolor<br>变色栓菌锰过氧化物酶同工酶的纯化及其性质研究
%A ZHANG Lian-hui
%A YANG Xiu-qing
%A GE Ke-shan
%A QIAN Shi-jun
%A <br>张连慧
%A 杨秀清
%A 葛克山
%A 钱世钧
%J 微生物学报
%D 2005
%I 
%X Two manganese peroxidase (MnP) active fractions D1 and D2 were got from the extracellular culture of Trametes versicolor by using ammonium sulfate precipitation, DEAE-cellulose DE52 chromatography. MnP1 was purified to electrophoretic homogeneity from the D2 by Phenyl Sepharose 6 Fast Flow chromatography and MnP2 was purified to electrophoretic homogeneity from the D1 by Sephacryl S-200HR chromatography and Phenyl Sepharose 6 Fast Flow chromatography. The specific activities of two MnP isozymes are 579.1U/mg and 425.0U/mg; purification folds are 17.51 and 12.85 and the yields are 6.17% and 2.47%, respectively. MnP1 and MnP2 have approximate molecular masses of 46.3kD and 43.0kD respectively, as determined by SDS-PAGE. The isoenzymes differed in optimum temperature (60degreesC and 65degreesC) and optimum pH(5.8 and 6.2) for oxidation of DMP (2,6-dimethoxyphenol). MnP1 and MnP2 are stable below 45degreesC and ranging from pH4.0 to pH7.0. DMP is the best substrate, the Km values of MnP1 and MnP2 for DMP are 13.43micromol/L and 12.45micromol/L respectively. Catalysis doesn't occur in the complete absence of Mn. EDTA inhibites the activities of MnP1 and MnP2 at the higher concentration and DTT inhibites the enzyme activities completely.
%K Trametes versicolor
%K Manganese peroxidase
%K Purification
%K Properties<br>变色栓菌
%K 锰过氧化物酶
%K 纯化
%K 性质
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=EF62F89276D52493&yid=2DD7160C83D0ACED&vid=94E7F66E6C42FA23&iid=94C357A881DFC066&sid=FD6137FFCE59D193&eid=EB8E83807F36F05B&journal_id=0001-6209&journal_name=微生物学报&referenced_num=0&reference_num=17