Characterization and Antifungal Activity of Gazyumaru (Ficus microcarpa) Latex Chitinases: Both the Chitin-Binding and the Antifungal Activities of Class I Chitinase Are Reinforced with Increasing Ionic Strength

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  • TAIRA Toki
    Department of Bioscience and Biotechnology, Faculty of Agriculture, Ryukyu University
  • OHDOMARI Atsuko
    Department of Bioscience and Biotechnology, Faculty of Agriculture, Ryukyu University
  • NAKAMA Naoya
    Department of Bioscience and Biotechnology, Faculty of Agriculture, Ryukyu University
  • SHIMOJI Makiko
    Department of Bioscience and Biotechnology, Faculty of Agriculture, Ryukyu University
  • ISHIHARA Masanobu
    Department of Bioscience and Biotechnology, Faculty of Agriculture, Ryukyu University

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  • Characterization and Antifungal Activity of Gazyumaru (Ficus microcarpa) Latex Chitinases: Both the Chitin-Binding and the Antifungal Activities of Class 1 Chitinase Are Reinforced with Increasing Ionic Strength
  • Characterization and Antifungal Activity of Gazyumaru (<i>Ficus microcarpa</i>) Latex Chitinases: Both the Chitin-Binding and the Antifungal Activities of Class I Chitinase Are Reinforced with Increasing Ionic Strength

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Three chitinases, designated gazyumaru latex chitinase (GLx Chi)-A, -B, and -C, were purified from the latex of gazyumaru (Ficus microcarpa). GLx Chi-A,-B, and -C are an acidic class III (33 kDa, pI 4.0), a basic class I (32 kDa, pI 9.3), and a basic class II chitinase (27 kDa, pI>10) respectively. GLx Chi-A did not exhibit any antifungal activity. At low ionic strength, GLx Chi-C exhibited strong antifungal activity, to a similar extent as GLx Chi-B. The antifungal activity of GLx Chi-C became weaker with increasing ionic strength, whereas that of GLx Chi-B became slightly stronger. GLx Chi-B and -C bound to the fungal cell-walls at low ionic strength, and then GLx Chi-C was dissociated from them by an escalation of ionic strength, but this was not the case for GLx Chi-B. The chitin-binding activity of GLx Chi-B was enhanced by increasing ionic strength. These results suggest that the chitin-binding domain of basic class I chitinase binds to the chitin in fungal cell walls by hydrophobic interaction and assists the antifungal action of the chitinase.

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