Purification and Characterization of a Novel Isozyme of Chitinase from Bombyx mori
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- KABIR Khondkar Ehteshamul
- Department of Biological Science, Faculty of Agriculture, Yamaguchi University
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- HIROWATARI Daizo
- Department of Biological Science, Faculty of Agriculture, Yamaguchi University
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- WATANABE Katsuhiro
- Department of Biological Science, Faculty of Agriculture, Yamaguchi University
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- KOGA Daizo
- Department of Biological Science, Faculty of Agriculture, Yamaguchi University
Bibliographic Information
- Other Title
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- Purification and Characterization of a Novel Isozyme of Chitinase from<i>Bombyx mori</i>
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Abstract
75-kDa chitinase, which showed potential as a biocontrol agent against Japanese pine sawyer, was characterized after purification from the integument of the fifth instar larvae of Bombyx mori by chromatography on diethylaminoethyl (DEAE)-Toyoperal 650 (M), hydroxylapatite, and Fractogel EMD DEAE 650 (M) columns. The optimum pH was 6.0 toward N-acetylchitopentaose (GlcNAc5) and 10 toward glycolchitin. The optimum temperature was 60 °C toward GlcNAc5 and 25 °C toward glycolchitn. The enzyme was stable at pH 7–10 and below 40 °C. Kinetic analysis and reaction-pattern analysis using glycolchitin and N-acetylchitooligosacchraides as substrates indicated that 75-kDa chitinase is an endo- or random-type hydrolytic enzyme to produce the β anomeric product and that it prefers the longer N-acetylchitooligosaccharides, suggesting, together with the N-terminal amino acid sequence, that the 75-kDa chitinase belongs to family 18 of glycosyl hydrolases.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 70 (1), 252-262, 2006
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Details 詳細情報について
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- CRID
- 1390282681452269056
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- NII Article ID
- 10018535676
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- NII Book ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 7791791
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed