Tsugawa W, Horiuchi S, Tanaka M, Wake H, Sode K
Department of Biotechnology, Tokyo University of Agriculture and Technology, Japan.
Appl Biochem Biotechnol. 1996 Mar;56(3):301-10. doi: 10.1007/BF02786960.
A novel glucose dehydrogenase (GDH) from a marine bacterium Cytophaga 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-1 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 typical property of marine bacterial enzymes. Using this novel enzyme, and enzymatic determination of 1,5-anhydro-D-glucitol (1,5AG) utilizing 2,6-dichrolophenolindophenol (DCIP) and phenazine methosulfate (PMS) as electron mediators was carried out. A good linear correlation was observed from 0.5 mM to 4 mM of 1,5AG.
从海洋细菌食纤维菌属海洋黄杆菌IFO 14170的膜组分中分离出一种新型葡萄糖脱氢酶（GDH）。这种GDH催化葡萄糖羟基的氧化，但不在其C-1位发生反应。该酶由一条分子量为67000的单肽组成。GDH能在高盐度条件下反应。最适pH约为8.0，显示出海洋细菌酶的典型特性。利用这种新型酶，以2,6-二氯酚靛酚（DCIP）和硫酸吩嗪甲酯（PMS）作为电子介质，对1,5-脱水-D-葡萄糖醇（1,5AG）进行了酶法测定。在1,5AG浓度为0.5 mM至4 mM时观察到良好的线性相关性。
