Purification and Characterization of Constitutive Polyethylene Glycol (PEG) Dehydrogenase of a PEC 4000-Utilizing Flavobacterium sp. No. 203

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概要

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• Polyethylene glycol (PEG) 4000-utilizing bacterium no. 203 was identified as a Flavobacterium species. 2,6- Dichlorophenol-indophenol (DCIP)-dependent PEG dehydrogenase was constitutively formed in nutrient broth, glucose and PEG media. However, the enzyme formation was repressed in the presence of an excess amount (over 0.25%) of PEG 400 of 1000. PEG dehydrogenase was purified approximately 34 fold by precipitation with ammonium sulfate, solubilization with benzalkonium chloride, chromatography with DEAE-Toyopearl 650 M and hydroxylapatite and gel filtration on Toyopearl HW-55. The molecular weight of the purified PEG dehydrogenase was calculated to be approximately 2.20×10^5,a value which seemed to consist of four subunits with the same molecular weight of 5.70×10^4. The enzyme was stable below 40℃ and in the pH range of 7.0 and 8.0. The optimum pH and temperature of the activity were around 8.0 and 40℃, respectively. The enzyme reduced DCIP and coenzyme Q_1 and Q_2. PEG dehydrogenase showed activity toward various PEG molecules (dimer-PEG 20,000). The apparent K_m values for PEG 400,1000,4000 and 6000 were about 1.0,1.7,2.8 and 5.9 mM, respectively. The enzyme oxidized primary aliphatic alcohols of C_3-C_<12>, the corresponding aldehydes of C_3-C_7,aromatic alcohols and aldehydes, diols, etc. The enzyme was inactive on ethylene glycol, glycerol, secondary alcohols and sugar alcohols. THe enzyme activity was strongly inhibited by sulfhydryl agents or heavy metals and 1,4-benzoquinone. THe purified enzyme showed absorption apectrum similar to that of PEG 6000 dehydrogenase which was already been reported to be a quinoprotein. The prosthetic group of the enzyme was extracted with methanol and identified as PQQ from its prosthetic group capability for glucose dehydrogenase and the fluorescence spectrum.

• 公益社団法人日本生物工学会の論文
• 1989-05-25

著者

• Kawai Fusako

  Department Of Agricultural Chemistry College Of Agriculture Kyoto University

• Kawai Fusako

  Department Of Biology Kobe University

• YAMANAKA HIROSHI

  (Present address)Research Laboratories, Hakutsuru Brewing Co., Ltd.

• Yamanaka Hiroshi

  (present Address)research Laboratories Hakutsuru Brewing Co. Ltd.

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