AppA C-terminal Plays an Important Role in its Thermostability in Escherichia coli

被引:0
|
作者
Baojin Fei
Yu Cao
Hui Xu
Xinran Li
Tao Song
Zhongan Fei
Dairong Qiao
Yi Cao
机构
[1] College of Life Science,Microbiology and Metabolic Engineering Key Laboratory of Sichuan Province
[2] Sichuan University,undefined
来源
Current Microbiology | 2013年 / 66卷
关键词
Phytic Acid; AppA; Phytase Activity; Protein Thermostability; Sodium Phytate;
D O I
暂无
中图分类号
学科分类号
摘要
Due to our previous research, mainly the thermostable mutants Q307D, Y311K, and I427L, we conjectured that Escherichia coli AppA phytase’s C-terminal plays an important role in its thermostability, and AppA begins to collapse from the C-terminal when at a higher temperature. So here we constructed C-lose mutant to prove it. The residual activities of the wild-type AppA phytase and C-lose were 31.42 and 70.49 %, respectively, after being heated at 80 °C for 10 min. The C-terminal deletion mutant C-lose showed 39.07 % thermostability enhancement than the wild-type both without the pH and temperature optimum changed. It proved the C-lose plays a key role in E. coli AppA phytase’s thermostability.
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页码:374 / 378
页数:4
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