Purification and Properties of NAD^+-dependent Sorbitol Dehydrogenase from Bacillus fructosus
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概要
- 論文の詳細を見る
Sorbitol dehydrogenase (EC 1.1.1.14), which catalyzes the NAD^+-linked interconversion of D-sorbitol and D-fructose, was purified and crystallized from cell-free extracts of Bacillus fructosus grown on D-sorbitol as a sole carbon source. The crystalline enzyme was homogeneous on disc electrophoresis and ultracentrifugation. The molecular weight was 102,000 by the sedimentation equilibrium method. The enzyme acted specifically on D-sorbitol, and showed an optimum pH at 9.0. The K_m values for D-sorbitol and NAD^+ were 1.1×10^-2M and 2.2×10^-4M, respectively. The enzyme activity was inhibited by p-chloromercuribenzoate, Ag^+, Hg^<2+>, and Cu^<2+>.
- 社団法人日本農芸化学会の論文
- 1999-03-23
著者
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UWAJIMA TAKAYUKI
Faculty of Engineering, Fukui University
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Uwajima T
Faculty Of Engineering Fukui University
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Uwajima Takayuki
Tokyo Research Laboratories Kyowa Hakko Kogyo Co. Ltd.
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