Classification of Chitosanases by Hydrolytic Specificity toward N¹,N⁴-Diacetylchitohexaose

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  • HIRANO Katsuaki
    Department of Applied Biochemistry and Food Science, Faculty of Agriculture, Saga University Department of Applied Biochemistry and Food Science, Faculty of Agriculture, Saga University
  • WATANABE Masamichi
    Department of Applied Biochemistry and Food Science, Faculty of Agriculture, Saga University Department of Applied Biochemistry and Food Science, Faculty of Agriculture, Saga University
  • SEKI Kiyohiko
    Department of Applied Biochemistry and Food Science, Faculty of Agriculture, Saga University Department of Applied Biochemistry and Food Science, Faculty of Agriculture, Saga University
  • ANDO Akikazu
    Department of Nanobiology, Graduate School of Advanced Integration Science, Chiba University Department of Nanobiology, Graduate School of Advanced Integration Science, Chiba University
  • SAITO Akihiro
    Department of Materials and Life Sciences, Faculty of Science and Technology, Shizuoka Institute of Science and Technology Department of Materials and Life Sciences, Faculty of Science and Technology, Shizuoka Institute of Science and Technology
  • MITSUTOMI Masaru
    Department of Applied Biochemistry and Food Science, Faculty of Agriculture, Saga University Department of Applied Biochemistry and Food Science, Faculty of Agriculture, Saga University

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  • Classification of Chitosanases by Hydrolytic Specificity toward <i>N</i><sup>1</sup>,<i>N</i><sup>4</sup>-Diacetylchitohexaose

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The hydrolytic specificities of chitosanases were determined using N1,N4-diacetylchitohexaose [(GlcN)2-GlcNAc-(GlcN)2-GlcNAc]. The results for the hydrolytic specificities of chitosanases belonging to subclasses I, II, and III toward chitohexaose and N1,N4-diacetylchitohexaose agreed with previous results obtained by analysis of the hydrolysis products of partially N-acetylated chitosan. N1,N4-Diacetylchitohexaose is a useful substrate to determine the hydrolytic specificity of chitosanase. On the other hand, chitosanases from Amycolatopsis sp. CsO-2 and Pseudomonas sp. A-01 showed broad cleavage specificity. They cleaved both the GlcNAc-GlcN and the GlcN-GlcNAc bonds in addition to the GlcN-GlcN bond in the substrate. Thus, both enzymes were new chitosanases. The chitosanases were divided into four subclasses according to their specificity for hydrolysis of the β-glycosidic linkages in partially N-acetylated chitosan.

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