Purification and characterization of chitinase B from moderately thermophilic bacterium Ralstonia sp. A-471 |
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Authors: | Ueda Mitsuhiro Kotani Yukiko Sutrisno Aji Nakazawa Masami Miyatake Kazutaka |
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Affiliation: | Laboratory of Biocycle Engineering, Department of Applied Biological Chemistry, Osaka Prefecture University, Osaka 599-8531, Japan. mueda@biochem.osakafu-u.ac.jp |
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Abstract: | 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, indicating that the enzyme predominantly hydrolyzes the second glycosidic linkage from the nonreducing end of (GlcNAc)6. |
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