Kinetic Analysis of a Chitinase from Red Sea Bream,<i>Pagrus major</i>

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  • KARASUDA Shuji
    Laboratory of Biochemistry, Department of Biological Science, Faculty of Agriculture, Yamaguchi University
  • YAMAMOTO Kosuke
    Laboratory of Biochemistry, Department of Biological Science, Faculty of Agriculture, Yamaguchi University
  • KONO Michiko
    Fisheries Research Laboratory, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Maisaka
  • SAKUDA Shohei
    Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo
  • KOGA Daizo
    Laboratory of Biochemistry, Department of Biological Science, Faculty of Agriculture, Yamaguchi University

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  • Kinetic Analysis of a Chitinase from Red Sea Bream, Pagrus major

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Kinetic analysis was done on the 46-kDa chitinase (EC 3.2.1.14) purified from the stomach of red sea bream, Pagrus major, using glycolchitin and N-acetylchitooligosaccharides (GlcNAcn, n=2–6) as substrates. High activity was observed at two pHs, such as 2.5 and 9.0, toward glycolchitin as seen in other insect chitinases, and also at both pH 2.5 and 5.0 even toward a short substrate, N-acetylchitopentasaccharide. Allosamidin competitively inhibited chitinase with Ki value of 0.0214 μM at pH 2.5 and 0.0024 μM at pH 9.0 in the reaction of glycolchitin. Substrate inhibition was observed in the reaction of N-acetylchitopentasaccharide. The anomeric forms of the products from N-acetylchitooligosaccharides were analyzed to be β anomer by the high pressure liquid chromatography (HPLC) method. The data for both β-anomer formation and allosamidin inhibition suggest that red sea bream chitinase belongs to family 18 of glycosyl hydrolases. This suggestion is also supported by the results for the N-terminal amino acid sequence.

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