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The enzymatic properties of purified CGTase from alkalophilic Bacillus sp. YC-335 have been examined. Apparent Vmax values of the enzyme in transferring glycosy: residues α-, β- and γ-cyclodextrin (CD) to sucrose were 16.13, 21.8 and 9.8 μmoles/min/mg protein, respectively and Km values of the corresponding CD were 1.68, 0.33 and 0.37 mM, respectively. A number of saccharides, specially starch hydrolyzates such as glucose and maltose, could activate the dextrinizing activity of the enzym. However, the dextrinizing activity was inhibited by β-CD. It was found from Lineweaver-Burk plot that the inhibition of CGTase by β-CD was noncompetitive. High performance liquid chromatographic analysis showed that the enzyme has three kinds of activity ; transglycosylation and disproportionation as well as cyclization
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