Improving the thermostability and catalytic efficiency of Bacillus deramificans pullulanase by site-directed mutagenesis.

@article{Duan2013ImprovingTT,
  title={Improving the thermostability and catalytic efficiency of Bacillus deramificans pullulanase by site-directed mutagenesis.},
  author={Xuguo Duan and Jian Chen and Jing Wu},
  journal={Applied and environmental microbiology},
  year={2013},
  volume={79 13},
  pages={4072-7}
}
Pullulanase (EC 3.2.1.41) is a well-known starch-debranching enzyme. Its instability and low catalytic efficiency are the major factors preventing its widespread application. To address these issues, Asp437 and Asp503 of the pullulanase from Bacillus deramificans were selected in this study as targets for site-directed mutagenesis based on a structure-guided consensus approach. Four mutants (carrying the mutations D503F, D437H, D503Y, and D437H/D503Y) were generated and characterized in detail… CONTINUE READING