T Kobayashi, H Tamura, R Taguchi, S Udaka, H Ikezawa
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引用次数: 4
摘要
我们利用短芽孢杆菌47表达系统成功高产出苏云金芽孢杆菌磷脂酰肌醇特异性磷脂酶C (PIPLC)。在短芽孢杆菌表达载体pNU211中，在中间壁蛋白基因启动子的控制下，表达了重组苏云金芽孢杆菌PIPLC。将大量重组PIPLC (0.4 g / l培养物)作为成熟酶分泌到培养基中，纯化后的重组PIPLC酶学性质与野生型苏云金芽孢杆菌酶学性质相似。该系统为研究PIPLC的三维结构-功能关系提供了一种有用的方法。
High-level expression of Bacillus thuringiensis phosphatidylinositol-specific phospholipase C by the Bacillus brevis host-vector system.
We succeeded in hyperproduction of Bacillus thuringiensis phosphatidylinositol-specific phospholipase C (PIPLC), using a Bacillus brevis 47 expression system. The recombinant B. thuringiensis PIPLC was expressed under the control of the middle wall protein gene promoter in B. brevis expression vector pNU211. A large amount of recombinant PIPLC (0.4 g per liter culture) was secreted into the medium as a mature enzyme, and the enzymatic properties of purified recombinant PIPLC were similar to those of the enzyme from wild-type B. thuringiensis. This system provides a useful approach to the three-dimensional structure-function relationship of PIPLC.
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