Thermal Stabilization of Bacillus subtilis Family-11 Xylanase by Directed Evolution

We used directed evolution to enhance the thermostability of glycosyl hydrolase family-11 xylanase from Bacillus subtilis. By combining random point mutagenesis, saturation mutagenesis, and DNA shuffling, a thermostable variant, Xylst, was identified which contained three amino acid substitutions: Q...

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Veröffentlicht in:	The Journal of biological chemistry 2006-04, Vol.281 (15), p.10236-10242
Hauptverfasser:	Miyazaki, Kentaro, Takenouchi, Misa, Kondo, Hidemasa, Noro, Natsuko, Suzuki, Mamoru, Tsuda, Sakae
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacillus subtilis Bacillus subtilis - metabolism Binding Sites Crystallography, X-Ray Cysteine - chemistry Disulfides - chemistry DNA - metabolism DNA Primers - chemistry Electrophoresis, Polyacrylamide Gel Endo-1,4-beta Xylanases - chemistry Endo-1,4-beta Xylanases - genetics Escherichia coli - metabolism Evolution, Molecular Gene Library Hot Temperature Hydrogen - chemistry Models, Molecular Mutagenesis Mutagenesis, Site-Directed Mutation Point Mutation Polymerase Chain Reaction Protein Conformation Temperature Time Factors
Online-Zugang:	Volltext
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