Purification and Characterization of Cycloinulooligosaccharide Fructanotransferase (CFTase) from Bacillus circulans MCI-2554

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Cycloinulooligosaccharide fructanotransferase (CFTase) that produces cyclofructan from inulin was purified about 69-fold from a culture broth of Bacillus circulans MCI-2554 by column chromatographies on DEAE-Toyopearl, QAE-Toyopearl, hydroxyapatite, and phenyl-Sepharose. The molecular mass of the enzyme was estimated to be 115 kDa by SDS-polyacrylamide gel electrophoresis and gel filtration, indicating a monomer structure. Maximal activity was observed at pH 7. 5 and 45℃. The enzyme was active from pH 5. 5 to pH 9. 5, and at temperatures up to 45℃. The enzyme activity was inhibited by Fe^<2+> and Cu^<2+>. A part of the amino acid sequence was identical with that of β-fructofuranosidases of Zymomonas mobilis, carrot, Salmonella typhimurium, and mung bean.
社団法人日本農芸化学会の論文
1995-01-23