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Wakako Tsugawa Shuichi Horiuchi Mitsuharu Tanaka Hitoshi Wake Koji Sode 《Applied biochemistry and biotechnology》1996,56(3):301-310
A novel glucose dehydrogenase (GDH) from a marine bacteriumCytophaga marinoflava IFO 14170 was isolated from its membrane fraction. This GDH catalyzes the oxidation of a hydroxy group of glucose, but does
not react in its C-l position. This enzyme is composed of a single peptide with a mol wt of 67,000. The GDH can react under
high salinity. The optimum pH is around 8.0, showing a typical property of marine bacterial enzymes. Using this novel enzyme,
an enzymatic determination of 1,5-anhydro-D-glucitol (1,5AG) utilizing 2,6-dichrolophenolindophenol (DCIP) and phenazine methosulfate
(PMS) as electron mediators was caried out. A good linear correlation was observed from 0.5 mM to 4 mM of 1,5AG. 相似文献
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