Isolation of Vinblastine in Callus Culture with Differentiated Roots of Catharanthus roseus (L). G. Don |
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Authors: | Yoshiharu Miura Kazumasa Hirata Norihide Kurano |
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Institution: | Department of Biochemical Engineering, Faculty of Pharmaceutical Sciences, Osaka University, Suita, Osaka 565, Japan |
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Abstract: | 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. |
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Keywords: | Bacillus subtilis NADH:DCIP oxidoreductase azoreductase diaphorase |
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