PURIFICATION AND PROPERTIES OF CYCLODEXTRIN GLUCANOTRANSFERASE FROM BREVIBACTERIUM SP NO-9605

Cyclodextrin glucanotransferase (EC 2.4.1.19) from Brevibacterium sp. No. 9605 was purified to homogeneity by chromatography on butyl-Toyope arl 650M, gamma-cyclodextrin-Sepharose 4B, and Toyopearl HW-55S. The m olecular weight of the purified enzyme was estimated to be 75,000 by s odium dodecyl sulfate-polyacrylamide gel electrophoresis. The isoelect ric point of the purified enzyme was 2.8. The optimum pH and temperatu re were pH 10 and 45 degrees C, respectively. The enzyme was stable at the range of pH 6-8 and at temperatures 50 degrees C or less in the p resence of CaCl2. The enzyme produced mainly gamma-cyclodextrin from s tarch in the initial stage of reaction, but later, the proportion of b eta-cyclodextrin was increased.