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KMID : 0380619940260040375
Korean Journal of Food Science and Technology
1994 Volume.26 No. 4 p.375 ~ p.381
Purification and Properties of Cyclodextrin glycosyltransferase from Bacillus stearothermophilus KY - 126


Abstract
A bacterial strain No. KY-126, which produced extracellular cyclodextrin glycosyltransferase(CGTase), was isolated from soil and identified as Bacillus stearothermophilus KY-126. The enzyme was purified by the treatments of ammonium sulfate precipitation, DEAF-Sephadex, Sephadex G-100 column chromatography. The optimal pH and temperature for the enzyme activity were pH 5.5 and 65¡É, respectively. And the enzyme was stable at pH values from 6.0 to 11.0 at 55¡É for 30 min and stable up to 60¡É for 30 min.. The enzyme was inhibited by HgClz. The molecular weight of the enzyme was estimated to be 67,000 by using SDS-PAGE. The maximum conversion from starch to cyclodextrin (CD) by CGTase was 43%r and obtained at 6 hr reaction and the ratio of ¥á-, ¥á-, ¥ã-, CD prodyction at this time was 2.9 : 2.1 : 1.0.
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