Transglycosylating Action of Cyclomaltodextrin Glucanotransferase from Bacillus stearothermophilus SE-4

The purified cyclomaltodextrin glucanotransferase (EC 2. 4. 1. 19 (CGT-ase)) from Bacillus stearothermophilus SE-4 produced α-, β- and γ-cyclodextrins from potato starch in the proportion of 1.0: 1.7: 0.6 throughout the reaction at 80°C. In the presence of stevioside, rebaudioside-A or rebaudio side-C as the acceptor of transglycosylation, SE-4 CGT-ase catalyzed the synthesis of the corresponding glycosylated derivatives without the formation of cyclodextrins and glucose. On the other hand, CGT-ase from B. macerans showed a weak transglycosylation activity on rebaudioside-A and rebaudioside-C.