Improvement of thermostability of fungal xylanase by using site-directed mutagenesis.

@article{Sriprang2006ImprovementOT,
  title={Improvement of thermostability of fungal xylanase by using site-directed mutagenesis.},
  author={Rutchadaporn Sriprang and Krisana Asano and Jarupan Gobsuk and Sutipa Tanapongpipat and Verawat Champreda and Lily Eurwilaichitr},
  journal={Journal of biotechnology},
  year={2006},
  volume={126 4},
  pages={454-62}
}
Replacing several serine and threonine residues on the Ser/Thr surface of the xylanase from Aspergillus niger BCC14405 with four and five arginines effectively increases the thermostability of the enzyme. The modified enzymes showed 80% of maximal activity after incubating in xylan substrate for 2h at 50 degrees C compared to only 15% activity for wild-type enzyme. The half-life of the mutated enzymes increased to 257+/-16 and 285+/-10 min for the four- and five-arginine mutants, respectively… CONTINUE READING