Purification and SomeProperties of Cyclodextrinase from Bacillus coagulans

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A gram positive bacterium (strain No. 109) isolated from soil as a producer of cyclodextrinase was identified as Bacillus coagulans. The cyclodextrinase from B. coagulans was purified to a homogeneous state by disc-electrophoresis after Streptomycin treatment, DEAE-Sephadex column chromatography, Ultrogel AcA44gel filtration and hydroxyapatite column chromatography.The molecular weight of the enzymewas determined to be 6.2 × 104 by sodium dodecylsulfate gel electrophoresis. The isoelectric point of the enzymewas pH5.0. The enzymewas most active at pH 6.2 and 50°C, and stable up to 45°C at pH 7.0 and in the range of pH 6.0-7.3 at 40°C on 2 hr incubation. This enzyme hydrolyzed linear maltooligosaccharides (such as maltotetraose (G4), maltopentaose (G5) and maltohexaose (G6)) and α-, β- and γ-cyclodextrins (CDs) faster than maltotriose (G3) and short chain amylose (DP 18), but did not hydrolyze maltose. The rates of hydrolysis for polysaccharides (such as starch, amylose and amylopectin) were below 1 %as compared to that for β-CD. The Kmvalues for G3, G4, G5, G6, shortchainamylose(DP 18) and α-, β-and-γ-CD were4.5, 4.0, 2.3, 1.5, 1.5, 10, 2.8 and0.47 mil, respectively. The products with this enzymehad the α-configulation.
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