| Autor: |
Ohishi, Kazuo, Yamagishi, Masaaki, Ohta, Toshiya, Motosugi, Masayoshi, Izumida, Hitoshi, Sano, Hiroshi, Adachi, Kyoko, Miwa, Tan |
| Zdroj: |
Bioscience, Biotechnology, and Biochemistry; January 1997, Vol. 61 Issue: 7 p1113-1117, 5p |
| Abstrakt: |
The Chitinase-producing bacterium Vibrio alginolyticusH-8 isolated from mud of Hamana Lake also produced two deacetylases for (GlcNAc)2extracellularly. Deacetylases DA1 and DA2 were purified from crude enzyme by column chromatography on Q-Sepharose FF, Phenyl Sepharose HP, Gigapite, and Superdex 200 HR. The final preparation was homogeneous in SDS-PAGE. The molecular weights were 48,000 and 46,000 for deacetylases DA1 and DA2, respectively. The pIs, optimum pHs, and optimum temperatures for deacetylases DA1 and DA2 were as follows; DA1, pI3.3, optimum pH 8.5–9.0, optimum temperature 45°C, DA2, pI3.5, optimum pH 8.0–8.5, optimum temperature 40°C. Both deacetylases were stable at pHs between 7.0 and 11.0 and at temperatures below 40°C. The activities of both enzymes were inhibited by Ag+and Hg2+. 1H-NMR of the reaction product by deacetylase DA1 for (GlcNAc)2showed that the purified deacetylase selectively hydrolyzed the 2-acetamide group at the reducing end of (GlcNAc)2. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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