Thermal stabilization of Bacillus subtilis family-11 xylanase by directed evolution.

@article{Miyazaki2006ThermalSO,
  title={Thermal stabilization of Bacillus subtilis family-11 xylanase by directed evolution.},
  author={Kentaro Miyazaki and Misa Takenouchi and Hidemasa Kondo and Natsuko Noro and Mamoru Suzuki and Sakae Tsuda},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 15},
  pages={10236-42}
}
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, Xyl(st), was identified which contained three amino acid substitutions: Q7H, N8F, and S179C. The half-inactivation temperature (the midpoint of the melting curves) for the Xyl(st) variant compared with the wild-type enzyme after incubation for 10 min was elevated from… CONTINUE READING
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