Purification and Characterization of Acid-stable Protopectinase Produced by<i>Aspergillus awamori</i>in Solid-state Fermentation

  • NAGAI Masaru
    Department of Food Science and Nutrition, Faculty of Agriculture, Kinki University
  • OZAWA Akira
    Department of Applied Biological Chemistry, College of Agriculture, Osaka Prefecture University
  • KATSURAGI Tohoru
    Graduate School of Biological Sciences, Nara Institute of Science and Technology
  • SAKAI Takuo
    Department of Food Science and Nutrition, Faculty of Agriculture, Kinki University

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  • Purification and Characterization of Acid-stable Protopectinase Produced by Aspergillus awamori in Solid-state Fermentation.

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  Aspergillus awamori IFO 4033 produced an acid-stable protopectinase in solid-state fermentation using wheat bran as the medium. The enzyme was purified to a homogeneous preparation with anion-exchange, hydrophobic, and size-exclusion chromatography. The enzyme was a monomeric protein of 52 kDa, by SDS-PAGE analysis, with an isoelectric point of pH 3.7. The optimum pH for enzyme activity was 2.0, and it was most active at 50°C (at pH 2.0) and was stable up to 50°C (at pH 2.0). The enzyme showed pectin-releasing activity toward protopectins from various origins, especially on lemon protopectin. An outstanding characteristic of the enzyme was its extreme stability in acidic conditions: the enzyme activity was not lost after incubating at pH 2.0 and 37°C for 24 h.<br>

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