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KMID : 1134819970260020351
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Journal of the Korean Society of Food Science and Nutrition
1997 Volume.26 No. 2 p.351 ~ p.357
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Purification and Characterization of Cyclodextrin Glycosyltransferase from Bacillus firmus
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Sohn Cheon-Bae
Kim Seong-Ai
Park Young-A
Kim Myung-Hee
Moon Sook-Kyung
Jang Sun-Ae
Lee Myung-Sun
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Abstract
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The cyclodextrin glycosyltransferase(EC 3.2.1.19) from Bacillus firmus was purified by precipitating with ammonium sulfate followed by, DEAE-Sephadex A-50 column chromatography and Sephadex G-100 column chromatography. In this way, we were able to obtain the single band protein on SDS-PAGE with a yield of 12%, whose purity was 49 fold. The purified CGTase was identified as a protein having molecular weight of approximately 80,000 dalton and isoelectric point of 9.6. The optimum pH and temperature for the enzyme activity were 8.0 and 65℃, respectively. The enzyme was stable at between pH 5.5 and 9.0 and up to 50℃. After 24hr of enzyme reaction using soluble starch as substrate, the ratio of α-, β- and γ-cyclodextrin production was 0.01 : 2.90 : 1.00, respectively. And this CGTase pro-duced mainly β- and γ-cyclodextrin.
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KEYWORD
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Bacillus firmus, cyclodextrin glycosyltransferase, cyclodextrin
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