Abstract
Cyclodextrin glucanotransferases (EC 2.4.1.19) (CGTase) are industrially important enzymes for production of cyclodextrin (CD) from starch. γ-CD yield of CGTase from alkalophilic Bacillus species is usually much lower than β-CD, while from alkalophilic Bacillus sp. 7-12. γ-CD yield is close to β-CD. A CGTase from alkalophilic Bacillus sp. 7-12 was purified and characterized. When purified by ammonium sulfate fractionation, DEAE-cellulose column chromatography and Sepharose CL-6B column chromatography, the enzyme obtained consisted of a single band that did not dissociate into subunits by SDS polyacrylamide gel electrophoresis. Molecular weight of the purified enzyme was determined to be 69,000 Da by SDS-PAGE. The enzyme showed a K m of 1.24 mg/mL and V max 0.101 μM/min when potato starch was used as substrate. The enzyme was stable below 70C with an optimum activity at 60C, and stable at pH range 6-10 with an optimum pH at 8.5. The enzyme activity was strongly inhibited by Ag + , Cu 2+ , Mg 2+ , Al 3+ , Co 2+ , Zn 2+ , Fe 2+ and slightly inhibited by Sn 2+ , Mn 2+ , The ions Ca 2+ and K + , EDTA and DTT had no influence on the enzyme activity.
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