抄録
1. B2G synthesized from maltose and B2 by E. coli, compared with those obtained by the enzyme of rat liver and of Asp. oryzae. The chemical properties of these B2G are found to be quite identical.
2. For the formation of B2G, the optimum temperature and pH were found to be 30° and 6.9, respectively, and maltose was chosen as most suitable glucosyl donor among various saccharides.
3. The formation of B2G was inhibited by both inorganic and organic phosphates, and the latter is attributed to the competitive effect on glucosyl-donating substances. Powerful inhibition revealed by the mild oxidizing reagents and SH reagents is due to the direct action on the enzyme itself.
4. The isoalloxazine ring of B2 was found to play an important role in this kind of transglucosidation, and the glucosidation was inhibited profoundly by lumiflavin. The redox potential of B2 is suitable for the glucosidation. The authors have postulated the mechanism of this transglucosidation and discussed on its significant role.
