Display options
Cite
Oikawa T, Nakai J, Tsukagawa Y, et al. A Novel Type of D-Mannitol Dehydrogenase from Acetobacter xylinum: Occurrence, Purification, and Basic Properties. Biosci Biotechnol Biochem. 1997;61(10):1778-82doi: 10.1271/bbb.61.1778.
Oikawa, T., Nakai, J., Tsukagawa, Y., & Soda, K. (1997). A Novel Type of D-Mannitol Dehydrogenase from Acetobacter xylinum: Occurrence, Purification, and Basic Properties. Bioscience, biotechnology, and biochemistry, 61(10), 1778-82. https://doi.org/10.1271/bbb.61.1778
Oikawa, T, et al. "A Novel Type of D-Mannitol Dehydrogenase from Acetobacter xylinum: Occurrence, Purification, and Basic Properties." Bioscience, biotechnology, and biochemistry vol. 61,10 (1997): 1778-82. doi: https://doi.org/10.1271/bbb.61.1778
Oikawa T, Nakai J, Tsukagawa Y, Soda K. A Novel Type of D-Mannitol Dehydrogenase from Acetobacter xylinum: Occurrence, Purification, and Basic Properties. Biosci Biotechnol Biochem. 1997 Jan;61(10):1778-82. doi: 10.1271/bbb.61.1778. PMID: 27393178.
Copy Download .nbib Format: NLM
Share it on

Biosci Biotechnol Biochem. 1997 Jan;61(10):1778-82. doi: 10.1271/bbb.61.1778.

A Novel Type of D-Mannitol Dehydrogenase from Acetobacter xylinum: Occurrence, Purification, and Basic Properties.

Bioscience, biotechnology, and biochemistry

T Oikawa, J Nakai, Y Tsukagawa, K Soda

Affiliations

  1. a Department of Biotechnology, Faculty of Engineering , Kansai University.
  2. b Kansai University High Technology Research Center , Suita-shi, Osaka 564 , Japan.

PMID: 27393178 DOI: 10.1271/bbb.61.1778

Abstract

We purified a novel type of D-mannitol dehydrogenase, which contains a c-type cytochrome and an unknown chromophore in the soluble fraction of an acetic acid bacterium, Acetobacter xylinum KU-1, to homogeneity. The enzyme showed the maximum activity at pH 5 and 40°C. It was stable up to 60°C at pH 6, and was inhibited by Hg(2+) and p-quinone (Ki = 0.18 mm). The molecular weight of the enzyme was about 140,000, and those of the subunits were 69,000, 51,000, and 20,000; the enzyme is hetero-trimeric and contained 8 g-atoms of Fe per mole. The α-helix content was estimated to be about 52.9%. The enzyme catalyzed phenazine methosulfate dependent oxidation of d-mannitol with an apparent Km of 98 μm (for d-mannitol) and Vmax of 213 μmol/min/mg. The reduced form of the enzyme showed the absorption maxima at 386, 416, 480, 518, 550, and 586 nm, which are attributable to a c-type cytochrome in the enzyme.

Keywords: Acetobacter xylinum; D-mannitol dehydrogenase; c-type cytochrome

Publication Types