| Autor: |
UEDA, Mitsuhiro, KOTANI, Yukiko, SUTRISNO, Aji, NAKAZAWA, Masami, MIYATAKE, Kazutaka |
| Zdroj: |
Bioscience, Biotechnology, and Biochemistry; January 2005, Vol. 69 Issue: 4 p842-844, 3p |
| Abstrakt: |
Chitinase B was purified from a culture medium of Ralstoniasp. A-471 by precipitation with (NH4)2SO4and column chromatography with DEAE-Toyopearl 650M 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 β-anomer of (GlcNAc)2from the substrate (GlcNAc)6, whereas (GlcNAc)4produced almost at equilibrium, indicating that the enzyme predominantly hydrolyzes the second glycosidic linkage from the nonreducing end of (GlcNAc)6. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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