Purification and Properties of<i>Bacillus acidopullulyticus</i>Pullulanase

DOI DOI 被引用文献1件 オープンアクセス
  • KUSANO Shuichi
    Laboratory of Biological Chemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
  • NAGAHATA Naokazu
    Laboratory of Biological Chemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
  • TAKAHASHI Shin-Ichiro
    Laboratory of Biological Chemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
  • FUJIMOTO Daisaburo
    Laboratory of Biological Chemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
  • SAKANO Yoshiyuki
    Laboratory of Biological Chemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology

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  • Purification and properties of Bacillus acidopullulyticus pullulanase.

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Two active forms (F1 and F2) of Bacillus acidopullulyticus pullulanase (EC 3.2.1.41 pullulan 6-glucanohydrolase) from Promozyme 200L (Novo Industri A/S) were purified using 50% (v/v) acetone precipitation and chromatographies on CM-Toyopearl 650S, Toyopearl HW-55S, and Butyl-Toyopearl 650S columns. The F1 and F2 forms showed single bands in polyacrylamide gel electrophoresis with or without sodium dodecyl sulfate. The optimum pHs and specific activities of F1 and F2 were about 5.0 and 200 - 220 units/mg, respectively. The molecular weights of F1 and F2 were estimated as 115, 000 and 116, 000, and their isoelectric points were 5.0 and 5.2. The Km values of F1 and F2 for pullulan were the same, 2.5mM glucose equivalents, and their k0 values were calculated as 2.9 × 103 and 3.6× 103s-1, respectively, from the Lineweaver-Burk plots. These K0 values of F1 and F2 for pullulan are larger than that (2.9 × 102sec-1) of Klebsiella pneumoniae pullulanase. The activities of F1 and F2 on glycogen β-limit dextrins were 26-46% of those on pullulan, but the activity of K. pneumoniae pullulanase on glycogen β-limit dextrins was 3 -6% of that on pullulan.

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