PURIFICATION AND SOME PROPERTIES OF CYCLOINULO-OLIGOSACCHARIDE FRUCTANOTRANSFERASE FROM BACILLUS-CIRCULANS OKUMZ 31B

Cycloinulo-oligosaccharide fructanotransferase was purified from the cultured medium of Bacillus circulans OKUMZ 31B, to electrophoretic homogeneity, by anion-exchange column chromatography on DEAE-Toyopearl 650M, hydrophobic column chromatography on Butyl-Toyopearl 650M, gel-filtration column chromatography on Sephacryl S-200HR and anion-exchenge column chromatography on SuperQ-Toyopearl 650M. The enzyme has a molecular weight of 132000 and a pI of 4.1. The enzyme was most active at pH 7.5 and 40 degrees C, and was stable at pH 6.0-9.0 and below 40 degrees C. The enzyme catalyses the conversion of inulin into cycloinulohexaose and cycloinuloheptaose in the ratio of ca. 4:1, and a small amount of cycloinulo-octaose, The enzyme has an isoform which may be a proteolyticaly modified species of the CFTase because of its reduced molecular weight, 126000.