Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Microbiology & Fermentation Technology Regular Papers
Heterologous Expression and Functional Characterization of a Novel Chitinase from the Chitinolytic Bacterium Chitiniphilus shinanonensis
Lanxiang HUANGArisa SHIZUMEMasahiro NOGAWAGoro TAGUCHIMakoto SHIMOSAKA
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2012 年 76 巻 3 号 p. 517-522

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Chitiniphilus shinanonensis strain SAY3T is a chitinolytic bacterium isolated from moat water of Ueda Castle in Nagano Prefecture, Japan. Fifteen genes encoding putative chitinolytic enzymes (chiA-chiO) have been isolated from this bacterium. Five of these constitute a single operon (chiCDEFG). The open reading frames of chiC, chiD, chiE, and chiG show sequence similarity to family 18 chitinases, while chiF encodes a polypeptide with two chitin-binding domains but no catalytic domain. Each of the five genes was successfully expressed in Escherichia coli, and the resulting recombinant proteins were characterized. Four of the recombinant proteins (ChiC, ChiD, ChiE, and ChiG) exhibited endo-type chitinase activity toward chitinous substrates, while ChiF showed no chitinolytic activity. In contrast to most endo-type chitinases, which mainly produce a dimer of N-acetyl-D-glucosamine (GlcNAc) as final product, ChiG completely split the GlcNAc dimer into GlcNAc monomers, indicating that it is a novel chitinase.
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© 2012 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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