Characterization of a NADH : Dichloroindophenol Oxidoreductase from Bacillus subtilis
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概要
- 論文の詳細を見る
We expressed and purified an azoreductase homolog, YvaB, from Bacillus subtilis. YvaB was found to have NADH:2,6-dichloroindophenol oxidoreductase activity, as well as azoreductase activity. Purified YvaB was active without FMN, unlike Escherichia coli azoreductase. YvaB was most active at pH 7.5 and 40 °C, and was stable up to 55 °C after incubation for 30 min. Remarkably, it was stable in the presence of Ag+, and was activated by the addition of non-ionic detergents. Other enzymatic properties of YvaB were also investigated.
- 社団法人 日本農芸化学会の論文
- 2007-02-23
著者
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Nishiya Yoshiaki
Tsuruga Institute Of Biotechnology Toyobo Co. Ltd.
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Yamamoto Yoshihiro
Industrial Technology Center Kyoto Municipal Industrial Research Institute
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