Journal
CURRENT MICROBIOLOGY
Volume 66, Issue 4, Pages 374-378Publisher
SPRINGER
DOI: 10.1007/s00284-012-0283-4
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Funding
- National Science Funds Committee [31272659, 30971817]
- National twelfth five-year science and technology support program [2011BAD14B05]
- Sichuan Science and Technology Bureau [2010GZ0290, 2012GZ0008, 2010GZ0065, 2011GZ0027]
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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 A degrees 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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