Participation of bacterial α-1,3-glucanases on fungal cell-wall degradation

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  • Yano Shigekazu
    Department of Biochemical Engineering, Graduate School of Science and Technology, Yamagata University
  • Wakayama Mamoru
    Department of Biotechnology, Faculty of Life Sciences, Ritsumeikan University

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Other Title
  • 真菌細胞壁を分解する細菌型α-1,3-グルカナーゼの特性
  • プロシーディング 真菌細胞壁を分解する細菌型α-1,3-グルカナーゼの特性
  • プロシーディング シンキン サイボウヘキ オ ブンカイ スル サイキンガタa-1,3-グルカナーゼ ノ トクセイ

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Abstract

The fungal cell-wall is a complex structure composed of cross-linked polysaccharides and glycoproteins. Chitin and β-1,3-glucan are the main skeletal polysaccharides of most fungi. On the other hands, α-1,3-glucan has been found in various fungal species and has an important role in some fungi. For example, α-1,3-glucan acts as a virulence factor in some pathogenic fungi. Considering this background, α-1,3-glucanase (EC3.2.1.59) has been studied as a biological control agent of pathogenic fungi. α-1,3-Glucanases are classified into two families, 71 and 87, of glycoside hydrolases (GH) based on their amino acid sequences. Type 71 α-1,3-glucanase have been found in fungi, and type 87 enzymes have been found in bacteria. We isolated type 87 α-1,3-glucanase (Agl-KA) from culture filtrate of Bacillus circulans KA-304. Agl-KA hydrolyzed the fungal cell-wall α-1,3-glucan and released the protoplasts from Schizophyllum commune mycelia in cooperation with GH family type 19 chitinase. Here, we report that domain structure and function of Agl-KA. Furthermore, we briefly discuss potential future applications of bacterial α-1,3-glucanases.

Journal

  • JSM Mycotoxins

    JSM Mycotoxins 66 (1), 37-43, 2016

    Japanese Society of Mycotoxicology

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