Purification and characterization of chitinase B from moderately thermophilic bacterium Ralstonia sp. A-471.

@article{Ueda2005PurificationAC,
  title={Purification and characterization of chitinase B from moderately thermophilic bacterium Ralstonia sp. A-471.},
  author={Mitsuhiro Ueda and Yukiko Kotani and Aji Sutrisno and Masami Nakazawa and Kazutaka Miyatake},
  journal={Bioscience, biotechnology, and biochemistry},
  year={2005},
  volume={69 4},
  pages={842-4}
}
Chitinase B was purified from a culture medium of Ralstonia sp. A-471 by precipitation with (NH4)2SO4 and column chromatography with DEAE-Toyopearl 650 M and Sephacryl S-200. The purified enzyme was homogeneous on SDS-PAGE. The molecular weight was 45,000 by SDS-PAGE. The optimum pH was 5.0 and stable pH was from 5.0 to 10.0. In the early stage of the reaction, chitinase B produced beta-anomer of (GlcNAc)2 from the substrate (GlcNAc)6, whereas (GlcNAc)4 produced almost at equilibrium… CONTINUE READING