Recombinant .ALPHA.-Glucosidase from Aspergillus niger. Overexpression by Emericella nidulans, Purification and Characterization

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  • Ogawa Masahiro
    Department of Biological Chemistry, College of Bioresource Sciences, Nihon University
  • Nishio Toshiyuki
    Department of Biological Chemistry, College of Bioresource Sciences, Nihon University
  • Minoura Kayo
    Department of Biological Chemistry, College of Bioresource Sciences, Nihon University
  • Uozumi Takeshi
    Department of Life Sciences, School of Agriculture, Meiji Univercity
  • Wada Masato
    Department of Biological Chemistry, College of Bioresource Sciences, Nihon University
  • Hashimoto Noriko
    Department of Biological Chemistry, College of Bioresource Sciences, Nihon University
  • Kawachi Ryu
    Department of Biological Chemistry, College of Bioresource Sciences, Nihon University
  • Oku Tadatake
    Department of Biological Chemistry, College of Bioresource Sciences, Nihon University

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Other Title
  • <b><i>Aspergillus niger</i> 由来組換え α-グルコシダーゼの<i>Emericella nidulans</i> での過剰発現，精製および諸性質</b>
  • Recombinant α-Glucosidase from Aspergillus niger. Overexpression by Emericella nidulans, Purification and Characterization
  • Recombinant アルファ Glucosidase from Aspergillus niger Overexpression by Emericella nidulans Purification and Characterization

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Abstract

An expression plasmid containing the aglA gene encoding Aspergillus niger GN-3 α-glucosidase was constructed and inserted into Emericella nidulans JCM10259. The transformant secreted about 61 mg/L of the recombinant α-glucosidase into its culture medium. The recombinant enzyme was purified from the culture filtrate through ammonium sulfate precipitation and three chromatographic steps. It was confirmed that, like wild-type A. niger GN-3 α-glucosidase, the purified recombinant enzyme consisted of two subunits. Although the molecular mass of the recombinant enzyme was slightly smaller than that of wild-type A. niger α-glucosidase (attributed to differences in glycosylation), the pH optima and substrate specificities of the wild-type and recombinant enzymes were comparable.

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