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Studies on Transglycosidation to Vitamin B6 by Microorganisms
Authors:Kawai Fusako  Yamada Hideaki  Ogata Koichi
Institution:1. Department of Agricultural Chemistry, Kyoto University, Kyoto;2. Research Institute for Food Science, Kyoto University, Kyoto
Abstract:Some properties of pyridoxine glucoside-synthesizing enzyme were studied using the partially and highly purified enzyme preparations from Micrococcus sp. No. 431.

The enzyme was stable at pH 7.0 and between 0°C and 30°C. The maximal activity was obtained at pH 8.0 and 37°C. Besides sucrose, phenyl-α-d-glucoside and maltose served as glucosyl donor. Of vitamin B6 compounds tested, only pyridoxine served as glucosyl acceptor. The enzyme activity was inhibited by PCMB and heavy metal ions, and the inhibition was prevented by 2-mercaptoethanol, indicating the enzyme would be a sulfhydryl enzyme. The activity was not affected by chelating agents and not activated by metal ions.
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