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淡紫拟青霉几丁质酶的纯化和活性影响因子
引用本文:肖炎农,王明祖.淡紫拟青霉几丁质酶的纯化和活性影响因子[J].植物病理学报,1998,28(3):275-280.
作者姓名:肖炎农  王明祖
作者单位:华中农业大学植保系, 武汉 430070
摘    要: 淡紫拟青霉(Paecilomyces lilacinus)是一种重要的植物线虫卵寄生真菌。采用DEAE-22离子交换层析和SephcrylS-300凝胶过滤层析分离纯化到一种淡紫拟青霉胞外几丁质酶,经7.5%聚丙烯酰胺凝胶电脉检测为单一条酶带,Rf值等于0.43。淡紫拟青霉几丁质酶的最适温度为45℃。热稳定性测定表明它在40℃下放置10min可保持原有活力,60℃下10min,完全失活。该酶的最适pH值为5。其pH值稳定性与温度和反应时间有关。20℃、20min,在pH3~9范围内稳定;37℃、1h,则只在pH5~7范围内较稳定。金属离子如Mg2+、Ca2+、Zn2+、Li+和Fe2+对酶有一定的激活作用,其中Mg2+的激活作用最强。相反,Cu2+对酶有强烈抑制作用。

关 键 词:淡紫拟青霉  几丁质酶  分离纯化  活性影响因子  

PURIFICATION OF EXTRACELLULAR CHITINASE PRODUCED BY PAECILOMYCES LILACINUS AND ITS ACTIVITY INFLUENCING FACTORS
Xiao Yannong,Wang Mingzu,Wang,Daoben,Hu Xiaohui.PURIFICATION OF EXTRACELLULAR CHITINASE PRODUCED BY PAECILOMYCES LILACINUS AND ITS ACTIVITY INFLUENCING FACTORS[J].Acta Phytopathologica Sinica,1998,28(3):275-280.
Authors:Xiao Yannong  Wang Mingzu  Wang  Daoben  Hu Xiaohui
Institution:Department of Plant Protection, Huazhong Agricultural University, Wuhan 430070
Abstract:A chitinase from culture filtrate of Paecilomyces lilacinus, an important parasite of plant nematode eggs, was purified by preciptation with ammonium sulfate followed by ion exchange chromatography on DEAE-22 and gel filtration on Sephcryl S-300. The optimum pH for the enzyme was pH 5, and maximum activity was obtained at 45℃. for 10 minutes and denatured at 60℃ for 10 minutes. It was comparatively stable within pH 3~9 at 20℃ for 20 minutes and within pH 5~7 at 37℃ for one hour, Metallic ions such as Mg2+, Ca2+, Fe2+,Zn2+ and Li+ could activate the enzyme.
Keywords:Chitinase    Paecilomyces lilacilus          Activity variation  Purification  Extraction  
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