Molecular Cloning and Characterization of an Enzyme Hydrolyzing p-Nitrophenyl α-D-Glucoside from Bacillus stearothermophilus SA0301

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  • KOBAYASHI Atsushi
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology
  • 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
  • SUYAMA Mikita
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology
  • SASAKI Jun
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology
  • NYAMDAWAA Batbold
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology
  • SAKAGUCHI Masayoshi
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology
  • SAKANO Yoshiyuki
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology

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タイトル別名
  • Molecular Cloning and Characterization of an Enzyme Hydrolyzing p-Nitrophenyl .ALPHA.-D-Glucoside from Bacillus stearothermophilus SA0301
  • Molecular Cloning and Characterization of an Enzyme Hydrolyzing p Nitrophenyl アルファ D Glucoside from Bacillus stearothermophilus SA0301
  • Molecular Cloning and Characterization of an Enzyme Hydrolyzing<i>p</i>-Nitrophenyl α-<scp>D</scp>-Glucoside from<i>Bacillus stearothermophilus</i>SA0301

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Bacillus stearothermophilus SA0301 produces an extracellular oligo-1,6-glucosidase (bsO16G) that also hydrolyzes p-nitrophenyl α-D-glucoside (Tonozuka et al., J. Appl. Glycosci., 45, 397–400 (1998)). We cloned a gene for an enzyme hydrolyzing p-nitrophenyl α-D-glucoside, which was different from the one mentioned above, from B. stearothermophilus SA0301. The k0⁄Km values of bsO16G for isomaltotriose and isomaltose were 13.2 and 1.39 s−1·mM−1 respectively, while the newly cloned enzyme did not hydrolyze isomaltotriose, and the k0⁄Km value for isomaltose was 0.81 s−1·mM−1. The primary structure of the cloned enzyme more closely resembled those of trehalose-6-phosphate hydrolases than those of oligo-1,6-glucosidases, and the cloned enzyme hydrolyzed trehalose 6-phosphate. An open reading frame encoding a protein homologous to the trehalose-specific IIBC component of the phopshotransferase system was also found upstream of the gene for this enzyme.

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