Literature DB >> 23238954

AppA C-terminal plays an important role in its thermostability in Escherichia coli.

Baojin Fei1, Yu Cao, Hui Xu, Xinran Li, Tao Song, Zhongan Fei, Dairong Qiao, Yi Cao.   

Abstract

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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Year:  2012        PMID: 23238954     DOI: 10.1007/s00284-012-0283-4

Source DB:  PubMed          Journal:  Curr Microbiol        ISSN: 0343-8651            Impact factor:   2.188


  18 in total

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Review 4.  Biotechnological production and applications of phytases.

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Journal:  Appl Environ Microbiol       Date:  2004-05       Impact factor: 4.792

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Journal:  Appl Environ Microbiol       Date:  1999-02       Impact factor: 4.792

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Journal:  Curr Microbiol       Date:  2007-07-25       Impact factor: 2.343

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  2 in total

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2.  Insights into the unfolding pathway and identification of thermally sensitive regions of phytase from Aspergillus niger by molecular dynamics simulations.

Authors:  Kapil Kumar; Krunal Patel; D C Agrawal; J M Khire
Journal:  J Mol Model       Date:  2015-06-04       Impact factor: 1.810

  2 in total

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