Purification and Some Properties of an Extracellular Oligo-1, 6 Glucosidase from Bacillus stearotheymaphilus SA0301

DOI
  • TONOZUKA Takashi
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology
  • SATO Kimihiko
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology
  • SAKAGUCHI Masayoshi
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology
  • SUYAMA Mikita
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology
  • SEKINE Kyoichi
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology
  • SAKANO Yoshiyuki
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology

Bibliographic Information

Other Title
  • Bacillus stearothermophilus SA 0301株の菌体外オリゴ1,6-グルコシダーゼの精製と諸性質

Abstract

Bacillus stearothermophilus designated strain SA0301 produces extracellular oligo-1, 6-glucosidases during the stationary phase of growth. The enzyme was purified to an electrophoretically homogeneous form. Its molecular mass was estimated to be 63 kDa by SDS-PAGE, and its N-terminal amino acid sequence was MERKWWKEAVVYQIYP-. The enzyme was shown to hydrolyze isomaltose, isomaltotriose, and panose, but not trehalose, sucrose, or maltose.

Journal

Details 詳細情報について

  • CRID
    1390282680147089920
  • NII Article ID
    130004257560
  • DOI
    10.11541/jag1994.45.397
  • COI
    1:CAS:528:DyaK1MXos1ynuw%3D%3D
  • ISSN
    18844898
    13403494
  • Data Source
    • JaLC
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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