Purification and some properties of cycloinulo-oligosaccharide fructanotransferase from Bacillus circulans OKUMZ 31B

✍ Scribed by Mishio Kawamura; Takao Uchiyama

• Book ID: 102997645
• Publisher: Elsevier Science
• Year: 1994
• Tongue: English
• Weight: 428 KB
• Volume: 260
• Category: Article
• ISSN: 0008-6215
• DOI: 10.1016/0008-6215(94)84047-4

✦ Synopsis

Cycloinulo-oligosaccharide fructanotransferase was purified from the cultured medium of BuciUus circdum OKUMZ 31B, to electrophoretic homogeneity, by anion-exchange column chromatography on DEAR-Toyopearl 65Oh4, hydrophobic column chromatography on Butyl-Toyopearl65OM, gel-filtration column chromatography on Sephacryl S-200HR and anion-exchenge column chromatography on SuperQ-Toyopearl 650M. The enzyme has a molecular weight of 132ooO and a p1 of 4.1. The enzyme was most active at pH 7.5 and 4O"C, and was stable at pH 6-O-9.0 and below 40°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 CFIase because of its reduced molecular weight, 126009.