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KMID : 0545119980080030251
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Journal of Microbiology and Biotechnology
1998 Volume.8 No. 3 p.251 ~ p.257
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Purification and Characterization of Cycloinulooligosaccharide Frudctanotransferase from Bacillus macersns CFC1
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Kim Hwa-Young
Choi Yong-Jin
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Abstract
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Cycloinulooligosaccharide fructanotransferase (CFTase) which produces cyclofructan from inulin was purified 332-fold from a culture broth of Bacillus macerans CFC1. The molecular mass of the CFTase was estimated to be 110 kDa by SDS-polyacrylamide gel electrophoresis and gel filtration, indicating that the enzyme has a monomer structure. The maximal level of enzyme activity was observed at pH 7.5 and 45℃. The enzyme was stable in the pH range 6.0 to 9.5, and at temperatures up to 45℃ for 1 h. The enzyme activity was completely inhibited in the presence of 0.5 mM Ag^+ or Cu^2+ ion. None of sucrose (GF), 1-kestose (GF2), or nystose (GF3) were found to be substrates for the CFTase, but inulooligosaccharides larger than nystose were attacked by the enzyme. The CFTase catalyzes not only the cyclization as the major reaction, but also disproportionation and coupling reactions involving intermolecular transfructosylation in the same manner as cyclodextrin glucanotransferase (CGTase) (EC 2.4.1.19).
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