Comparison of cell-bound and extracellular isopullulanase from Aspergillus niger.

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  • SAKANO Yoshiyuki
    Laboratory of Biochemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
  • TAGUCHI Ayako
    Laboratory of Biochemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
  • HISAMATSU Reiko
    National Food Research Institute
  • KOBAYASHI Shoichi
    National Food Research Institute
  • FUJIMOTO Daisaburo
    Laboratory of Biochemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology
  • KOBAYASHI Tsuneo
    Laboratory of Biochemistry, Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo University of Agriculture and Technology

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Other Title
  • Ａｓｐｅｒｇｉｌｌｕｓ　ｎｉｇｅｒ菌体結合型と細胞外イソプルラナーゼの比較

Abstract

Cell-bound isopullulanase of Aspergillus niger was purified from the mycelia in a sub-merged culture through 1) solubilization of the enzyme with Novozyme 234, 2) P-cellulose (pH 3.8) and DEAF-cellulose (pH 5.5) chromatography, 3) displacement chromatography (changing pH from 6.2 to 4.0) and gel filtration on Bio-Gel P-100 (pH 5.5). Purified enzyme showed a single glycoprotein band, stained with Coomassie Brilliant blue and Na104-Schiff's reagent, on PAGE and a single peak on HPLC using TSK-gel G-3000 Swxz. Substrate specificity of cell-bound and extracellular isopullulanase was the same on pullulan, panose (GlcP(α1→6)Glcp(α1→4)Glc), and 62-a-maltosylmaltose (GlcP (α1→44) Glcp (α1→6) GlcP (α1→4) Glc) . Their optimum pH and temperature were almost similar, but pH and thermal stability of extracellular enzyme were better than those of cell-bound enzyme. Their molecular weight and isoelectric point were different, i, e., 62, 000 and 4.8 (cell-bound enzyme), and 74, 000 and 4.65 (extracellular enzyme).

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