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Molecular Cloning and Characterization of CMCase gene (celC) from Salmonella typhimurium UR
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HOME > J. Microbiol > Volume 42(3); 2004 > Article
Research Support, Non-U.S. Gov't
Molecular Cloning and Characterization of CMCase gene (celC) from Salmonella typhimurium UR
Ju-Soon Yoo 1, Youn-Ju Jung 1, Soo-Yeol Chung 2, Young-Choon Lee 1, Yong-Lark Choi 1
Journal of Microbiology 2004;42(3):205-210
DOI: https://doi.org/2088 [pii]
1 Division of Biotechnology, Faculty of Natural Resources and Life Science, Dong-A University, Busan, 604-714 ; 2Department of Food Science and Nutrition, Dongju College, Busan, Korea1 Division of Biotechnology, Faculty of Natural Resources and Life Science, Dong-A University, Busan, 604-714 ; 2Department of Food Science and Nutrition, Dongju College, Busan, Korea
Corresponding author:  Yong-Lark Choi , Tel: 82-51-200-7585, 
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Abstract

The sequence coding for carboxymethylcellulase (CMCase, CelC) was isolated from the DNA of Salmonella typhimurium UR1. 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^oC and pH 6.5, respectively.

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    Molecular Cloning and Characterization of CMCase gene (celC) from Salmonella typhimurium UR
    J. Microbiol. 2004;42(3):205-210.
    DOI: https://doi.org/2088 [pii]
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