Purification and Some Properties of Aspergillus aculeatus β-Xylosidase

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  • OOI Toshihiko
    Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
  • FUJIMOTO Hiroaki
    Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
  • WANG Sang-lang
    Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
  • TAKIZAWA Toshio
    Bioscience Laboratory, Meiji Seika Kaisha Ltd.
  • HIDAKA Hidemasa
    Bioscience Laboratory, Meiji Seika Kaisha Ltd.
  • OGURA Sei
    Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
  • MURAO Sawao
    Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture
  • ARAI Motoo
    Department of Applied Biological Chemistry, College of Agriculture, University of Osaka Prefecture

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Other Title
  • Aspeygillus　aculeatus由来β-キシロシダーゼの精製と諸性質
  • Aspergillus aculeatus ユライ ベータ キシロシダーゼ ノ

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Abstract

Extracellular β-xylosidase ([EC 3.2.1.37]: xylan 1, 4-β-xylosidase) was purified from a culture filtrate of Aspergillus aculeatus No. F-50 by column chromatography using DEAE-Sephadex A-50, Sephacry 5-200, and DEAE-Toyopearl 650M columns, and preparative isoelectric focusing. The purified enzyme was homogeneous on SDS-polyacrylamide gel electrophoresis . The molecular weight was about 105, 000 by SDS-PAGE and its p1 value was 4.3. The optimum pH and temperature for the /3 -xylosidase activities were 2.0 and 70°C, respectively. The β-xylosidase was stable for 30 min at 50°C and stable between pH 3 and 7. The enzyme activity was strongly inhibited by Cu2+, Mn2+, and Hg2+. The enzyme hydrolyzed xylooligosaccharides, xylobiose through xylopentaose, to form xylose. The β-xylosidase showed potent activity towards larchwood xylan .

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