Purification and Characterization of a Xyloglucan-specific Glycosyl Hydrolase from Aspergillus oryzae RIB40

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  • Hakamada Yoshihiro
    Department of Applied Bioscience, College of Bioscience and Chemistry, Kanazawa Institute of Technology Genome Biotechnology Laboratory, Kanazawa Institute of Technology
  • Arata Shoukan
    Department of Applied Bioscience, College of Bioscience and Chemistry, Kanazawa Institute of Technology
  • Ohashi Shinichi
    Genome Biotechnology Laboratory, Kanazawa Institute of Technology

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A xyloglucanase (xyloglucan-specific endo-β-1,4-glucanase [EC 3.2.1.151]), AoXEG29, was purified from Aspergillus oryzae RIB40 to 75.5-fold of its apparent homogeneity with 1.2% recovery. It was a monomeric protein with a molecular mass of approximately 29 kDa estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, gel filtration and zymogram analysis. Sugar-chain staining showed a sugar chain in the purified enzyme. AoXEG29 hydrolyzed detectable amounts of xyloglucan and AZCL-xyloglucan, but not CMC, H3PO4-swollen cellulose, oat-spelt xylan, low-melting-point agarose, glucomannan, colloidal chitin, or AZCL-xylan. The optimum pH at 40°C and optimum temperature at pH 5.0 were 4.5-5.5 and 60°C, respectively. AoXEG29 was stable at pH 3-8 at 40°C for 30 min and up to 50°C at pH 5 for 20 min. The kinetic parameters Km and Vmax for the hydrolysis of tamarind xyloglucan were 2.4 mg/mL and 1,250 U/mg, respectively.

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