Seven N-terminal Residues of a Thermophilic Xylanase Are Sufficient to Confer Hyperthermostability on Its Mesophilic Counterpart

Open Access

Peer-reviewed

Research Article

Shan Zhang,

Affiliation State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, P. R. China
⨯
Yongzhi He,

Affiliation State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, P. R. China
⨯
Haiying Yu,

Affiliation State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, P. R. China
⨯
Zhiyang Dong

* E-mail: dongzy@sun.im.ac.cn

Affiliation State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, P. R. China
⨯

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Directed evolution
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Sequence alignment
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Escherichia coli
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Hydrolysis
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Plasmid construction
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Polymerase chain reaction
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Substitution mutation
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Transformation associated recombination
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