Extracellular alkaline proteinase of Colletotrichum gloesosporsioides
Extracellular alkaline proteinase of Colletotrichum gloesosporsioides
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DOI：
10.1134/s0006297907030145
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发表时间：
2007-03-01
影响因子：
2.8
通讯作者：
Belozersky, M. A.
中科院分区：
文献类型：
--
作者：
Dunasevsky, Ya. E.;Matveeva, A. R.;Belozersky, M. A.
炭疽病病原菌胶孢炭疽菌（Colletotrichum gloeosporioides）的主要蛋白酶分子量为57 kD，纯化倍数超过200倍，得率为5%。该蛋白酶在pH9.0 -10.0范围内具有最大活性，在pH6.0 -11.5范围内酶活力稳定（残活不低于70%）。所研究的酶在55 ℃下完全保持其活性。最佳温度为45摄氏度纯化的C.胶孢霉蛋白酶在碱性pH值下稳定，但在pH值低于5.0时迅速失去活性。加入牛血清白蛋白可使酶在酸性条件下稳定.抑制剂分析和底物特异性的酶的数据允许其分类为枯草杆菌蛋白酶家族的丝氨酸蛋白酶。结果表明，C. gloeosporioides特异性地影响植物细胞壁蛋白。有人提出，所研究的蛋白酶-通过水解细胞壁-提供了真菌渗透到宿主植物的组织。
The main proteinase of the filamentous fungus Colletotrichum gloeosporioides causing anthracnoses and serious problems for production and storage of agricultural products has molecular mass of 57 kD and was purified more than 200-fold to homogeneity with the yield of 5%. Maximal activity of the proteinase is at pH 9.0-10.0, and the enzyme is stable at pH 6.0-11.5 (residual activity not less than 70%). The studied enzyme completely kept its activity to 55 degrees C. with a temperature optimum of 45 degrees C. The purified C. gloeosporioides proteinase is stable at alkaline pH values, but rapidly loses its activity at pH Values lower than 5.0. Addition of bovine serum albumin stabilizes the enzyme Under acidic conditions. Data on inhibitor analysis and substrate specificity of the enzyme allow its classification as a serine proteinase of subtilisin family. It is demonstrated that the extracellular proteinase of C. gloeosporioides specifically effects plant cell wall proteins. It is proposed that the studied proteinase - via hydrolysis of cell wall - provides for penetration of the fungus into the tissues of the host plant.