Purification and characterization of thermostable chitinase from Bacillus licheniformis SK-1.

@article{Kudan2009PurificationAC,
  title={Purification and characterization of thermostable chitinase from Bacillus licheniformis SK-1.},
  author={Sanya Kudan and Rath Pichyangkura},
  journal={Applied biochemistry and biotechnology},
  year={2009},
  volume={157 1},
  pages={23-35}
}
Chitinase was purified from the culture medium of Bacillus licheniformis SK-1 by colloidal chitin affinity adsorption followed by diethylamino ethanol-cellulose column chromatography. The purified enzyme showed a single band on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The molecular size and pI of chitinase 72 (Chi72) were 72 kDa and 4.62 (Chi72) kDa, respectively. The purified chitinase revealed two activity optima at pH 6 and 8 when colloidal chitin was used as substrate. The… CONTINUE READING