Isolation and Characterization of a Serine Protease from the Nematophagous Fungus, Lecanicillium psalliotae, Displaying Nematicidal Activity
Isolation and Characterization of a Serine Protease from the Nematophagous Fungus, Lecanicillium psalliotae, Displaying Nematicidal Activity
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DOI：
10.1007/s10529-005-8461-0
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发表时间：
2005-08
影响因子：
2.7
通讯作者：
Jinkui Yang;Xiaowei Huang;B. Tian;Miao Wang;Qiuhong Niu;Keqin Zhang
中科院分区：
文献类型：
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作者：
Jinkui Yang;Xiaowei Huang;B. Tian;Miao Wang;Qiuhong Niu;Keqin Zhang
PsalliotaeLecanicillium产生一种胞外蛋白酶（Ver 112），经纯化后在SDS-PAGE上显示单一条带，分子量为32 kDa。Ver 112的最佳活性为pH 10和70 °C（超过5分钟）。纯化的蛋白酶降解广泛的底物，包括酪蛋白，明胶，和线虫角质层与81%的线虫（Panagrellus redivus）处理后12小时被降解。该蛋白酶对PMSF（ImM）高度敏感，表明它是丝氨酸蛋白酶。Ver 112的N-末端氨基酸残基与其他食虫真菌表皮降解蛋白酶具有高度的相似性，这表明Ver 112在线虫感染中起作用。
Lecanicillium psalliotaeproduced an extracellular protease (Ver112) which was purified to apparent homogeneity giving a single band on SDS-PAGE with a molecular mass of 32 kDa. The optimum activity of Ver112 was at pH 10 and 70 °C (over 5 min). The purified protease degraded a broad range of substrates including casein, gelatin, and nematode cuticle with 81% of a nematode (Panagrellus redivivus) being degraded after treating with Ver112 for 12 h. The protease was highly sensitive to PMSF (1 mM) indicating it to be a serine protease. TheN-terminal amino acid residues of Ver112 shared a high degree of similarity with other cuticle-degrading proteases from nematophagous fungi which suggests a role in nematode infection.