Characterization of the third chitinase Chi18C of Clostridium paraputrificum M-21 |
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Authors: | Kenji Morimoto Michiko Yoshimoto Shuichi Karita Tetsuya Kimura Kunio Ohmiya Kazuo Sakka |
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Affiliation: | (1) Rare Sugar Research Center, Kagawa University, 2393 Ikenobe, Miki-cho, Kita-gun Kagawa, 761-0795, Japan;(2) Faculty of Bioresources, Mie University, Tsu 514-8507, Japan |
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Abstract: | A novel chitinase gene chiC of Clostridium paraputrificum M-21, a chitinolytic and hydrogen-gas-producing bacterium, was characterized along with its translated product. The chi18C gene encodes 683 amino acids (signal peptide included) with a deduced molecular weight of 74,651. Chi18C is a modular enzyme composed of a family-18 catalytic module of glycoside hydrolases, two reiterated modules of unknown function, and a family-12 carbohydrate-binding module. Recombinant Chi18C was active toward soluble and insoluble chitin preparations, and synthetic substrates such as 4-methylumbelliferyl-β-d-N-N′-N″-triacetylchitotriose, but not active toward 4-MU-N-acetylglucosamine or 4-MU-β-d-N-N′-diacetylchitobioside. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and immunological analyses suggested that the expression of chi18C was inducible with chitinous substrates and that Chi18C was secreted into the culture medium. A possible role of Chi18C in the chitinolytic system of C. paraputrificum M-21 is discussed. |
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Keywords: | Chitinase Clostridium Paraputrificum |
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