Expression of thermostable alkaline protease gene from Thermoactinomyces sp. E79 in E. coli and heat activation of the gene product

被引：0
|
作者：
Jung-Kee Lee
Young-Ok Kim
K. Sunitha
Tae-Kwang Oh
机构：
[1] Korea Research Institute of Bioscience & Biotechnology (KRIBB),Microbial Enzyme RU
来源：
Biotechnology Letters | 1998年 / 20卷
关键词：
Enzyme; Purification; Organic Chemistry; Thermal Stability; CaCl2;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
The expression of Thermoactinomyces sp. E79 protease gene cloned into E. coli was highly host-dependent and the levels of protease expression was most stable in E. coli RR1 and E. coli HB101. Heating the intracellular extract at 70°C for 15 min converted the inactive recombinant E79 protease to its active mature form and also resulted in purification of the enzyme in a single step. Addition of 10 mM CaCl2 to the E79 protease decreased its autolysis and increased its thermal stability. © Rapid Science Ltd. 1998
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页码：837 / 840
页数：3
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