Preparation of High-Purity Cyclodextrin Glucanotransferase from Bacillussp. 1070

Two schedules have been developed for chromatographic purification of cyclodextrin glucanotransferase (CGTase) from a culture of Bacillussp. 1070. The purification on butyl-Toyopearl and on Cu(II)-iminodiacetic (IDA) agarose resulted in a 9.5-fold purification of the enzyme. The second schedule for purification (chromatography on butyl-Toyopearl and on DEAE-Sephacel) resulted in a 13.5-fold increase in the specific activity of CGTase. By electrophoresis under denaturing conditions, the enzyme purity was shown to be no less than 90%. According to preliminary data, CGTase consists of two isoenzymes with pI 5.1 and 5.3.