Purification and characterization of chitinase from Paenibacillus sp. D1.

@article{Singh2011PurificationAC,
  title={Purification and characterization of chitinase from Paenibacillus sp. D1.},
  author={Anil Kumar Singh and Hari S. Chhatpar},
  journal={Applied biochemistry and biotechnology},
  year={2011},
  volume={164 1},
  pages={77-88}
}
A 56.56-kDa extracellular chitinase from Paenibacillus sp. D1 was purified to 52.3-fold by ion exchange chromatography using SP Sepharose. Maximum enzyme activity was recorded at pH 5.0 and 50 °C. MALDI-LC-MS/MS analysis identified the purified enzyme as chitinase with 60% similarity to chitinase Chi55 of Paenibacillus ehimensis. The activation energy (E (a)) for chitin hydrolysis and temperature quotient (Q (10)) at optimum temperature was found to be 19.14 kJ/mol and 1.25, respectively… CONTINUE READING