Characterization of Clostridium paraputrificum chitinase A from a recombinant Escherichia coli.

@article{Morimoto2001CharacterizationOC,
  title={Characterization of Clostridium paraputrificum chitinase A from a recombinant Escherichia coli.},
  author={Kenji Morimoto and Shuichi Karita and Tetsuya Kimura and Kazuo Sakka and Kunio Ohmiya},
  journal={Journal of bioscience and bioengineering},
  year={2001},
  volume={92 5},
  pages={466-8}
}
Clostridium paraputrificum chitinase A (ChiA) was purified from a recombinant Escherichia coli. ChiA was active toward chitin from crab shells, colloidal chitin, glycol chitin, and 4-methylumbelliferyl beta-D-N,N'-diacetylchitobioside [4-MU-(GlcNAc)2]. ChiA showed maximum activity at pH 6.0 and its optimum temperature was 45 degrees C. ChiA was stable between pH 6.0 and 9.0 and at temperatures up to 40 degrees C. The K(m) and V(max) values of ChiA for 4-MU-(GlcNAc)2 were estimated to be 6.9… CONTINUE READING