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Molecular Cloning and Characterization of CM Case gene (celC) from Salmonella typhimurium UR  

Yoo, Ju-Soon (Division of Biotechnology, Faculty of Natural Resources and Life Science, Dong-A University)
Jung, Youn-Ju (Division of Biotechnology, Faculty of Natural Resources and Life Science, Dong-A University)
Chung, Soo-Yeol (Department of Food Science and Nutrition, Dongju College)
Lee, Young-Choon (Division of Biotechnology, Faculty of Natural Resources and Life Science, Dong-A University)
Choi, Yong-Lark (Division of Biotechnology, Faculty of Natural Resources and Life Science, Dong-A University)
Publication Information
Journal of Microbiology / v.42, no.3, 2004 , pp. 205-210 More about this Journal
Abstract
The sequence coding for carboxymethylcellulase (CMCase, CelC) was isolated from the DNA of Salmonella typhimurium URl. Comparison between the deduced amino acid sequence of CelC (368 amino acid residues, Molecular mass 41 kDa) and that of the previously published CMCase revealed that this enzyme belongs to the cellulase family 8 and D. The protein was overproduced in Escherichia coli using T7 expression system, and its activity was confirmed by CMC-SDS-PAGE. When the overexpressed CelC protein was tested on cellulose-type substrates, the recombinant protein is able to degrade cellulose-type substrates, such as CM-cellulose, xylan, avicel, lichenan, and laminarin. Optimal temperature and pH for enzyme activity were found to be 50$^{\circ}C$ and pH 6.5, respectively.
Keywords
Salmonella typhimurium; CMCase; celC; CMC-SDS-PAGE;
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