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Purification and properties of cyclodextrin glucanotransferase from an alkalophilic Bacillus sp. 7-12


Purification and properties of cyclodextrin glucanotransferase from an alkalophilic Bacillus sp. 7-12



Journal of food biochemistry 8(6): 463-475



ISSN/ISBN: 0145-8884

DOI: 10.1111/j.1745-4514.2004.04603.x

Cyclodextrin glucanotransferases (EC 2.4.1.19) (CGTase) are industrially important enzymes for production of cyclodextrin (CD) from starch. gamma-CD yield of CGTase from alkalophilic Bacillus species is usually much lower than beta-CD, while from alkalophilic Bacillus sp. 7-12. gamma-CD yield is close to beta-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 micromolar/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+, Cu2+, Mg2+, Al3+, Co2+, Zn2+, Fe2+ and slightly inhibited by Sn2+, Mn2+. The ions Ca2+ and K+, EDTA and DTT had no influence on the enzyme activity.

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