Cyclodextrin glucanotransferase (CGTase, EC 2.4.1.19) from Bacillus circulans ATCC 21783 was purified by ultrafiltration and a consecutive starch adsorption. Total enzyme yield of 75.5% and purification factor of 13.7 were achieved. CGTase was most active at 65 ºC, possessed two clearly revealed pH-optima at 6.0 and 8.6 and retained from 75 to 100% of its initial activity in a wide range of pH, between 5.0 and 11.0. The cyclising activity was enhanced by 1 mM CaCl 2 or 4 mM CoCl 2 . The enzyme was thermostable up to 70 ºC, and 64% of the original activity remained at 70 ºC after 30 min heat treatment. Up to 41% conversion into cyclodextrins was obtained from 40 g l -1 starch without using any additives. This CGTase produced two types of cyclodextrins, beta and gamma, in a ratio 73:27 after 4 h reaction time at 65 ºC. This feature of the enzyme could be of interest for industrial cyclodextrin production.