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《Journal of Chemical Industry and Engineering(China)》 2005-04
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Purification and properties of chitinase from Metarhizium anisopliae

YANG Ge,CHEN Hongzhang,LI Zuohu (State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100080,China)  
A fungium-producing chitinase was isolated from the dead body of Anisopliae. A chitinase was isolated from the culture of Metarhizium anisopliae and purified to electrophoretic homogeneity by the steps of ammonium sulfate precipitation,DEAE-cellulose and hydrophobic interaction column chromatography. Its molecular mass was estimated to be about 61.5 kD by SDS-PAGE,and 57.14 kD by mass spectroscopy.The isoelectric temperature and pH of the enzyme activity were 55 ℃ and 6.0 respectively.The isoelectric point was 4.02.Its N-terminal sequence was VIGPAAPL. The carbohydrate content was 56.2% by the phenol-sulfuric acid method. Michaelis constant of the enzyme was 14.5 μmol·L -1.The enzyme activity was stable under 45 ℃ and in the pH range of 3.0—9.5. The activity was enhanced by Zn 2+、Ca 2+、Ba 2+ and Mn 2+,and was strongly inhibited by Hg 2+、Co 2+ and Fe 2+.EDTA also inhibited the activity.Ser was the possible essential residue for enzyme activity.
【Fund】: 国家重点基础研究发展计划项目 ( 973 计划)(2004CB719700);; 中国科学院知识创新工程重要方向项目(KSCXZ SW 301).~~
【CateGory Index】: Q936
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