Properties of cellulosomal family 9 cellulases from Clostridium cellulovorans

Applied Microbiology and Biotechnology
Takamitsu AraiRoy H Doi

Abstract

The cellulosomal family 9 cellulase genes engH, engK, engL, engM, and engY of Clostridium cellulovorans have been cloned and sequenced. We compared the enzyme activity of family 9 cellulosomal cellulases from C. cellulovorans and their derivatives. EngH has the highest activity toward soluble cellulose derivatives such as carboxymethylcellulose (CMC) as well as insoluble cellulose such as acid-swollen cellulose (ASC). EngK has high activity toward insoluble cellulose such as ASC and Avicel. The results of thin-layer chromatography showed that the cleavage products of family 9 cellulases were varied. These results indicated that family 9 endoglucanases possess different modes of attacking substrates and produce varied products. To investigate the functions of the carbohydrate-binding module (CBM) and the catalytic module, truncated derivatives of EngK, EngH, and EngY were constructed and characterized. EngHDeltaCBM and EngYDeltaCBM devoid of the CBM lost activity toward all substrates including CMC. EngKDeltaCBM and EngMDeltaCBM did not lose activity toward CMC but lost activity toward Avicel. These observations suggest that the CBM is extremely important not only because it mediates the binding of the enzyme to the substrates b...Continue Reading

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Citations

Jul 24, 2007·Journal of Bacteriology·Nicholas D Gold, Vincent J J Martin
May 6, 2014·Journal of Industrial Microbiology & Biotechnology·Minh Tuan NguyenHiroaki I Ogawa
Jul 5, 2016·International Journal of Biological Macromolecules·Su-Jung KimSung Ok Han
Aug 21, 2013·Applied and Environmental Microbiology·Kazuma MatsuiMitsuyoshi Ueda
May 30, 2017·Applied Microbiology and Biotechnology·Cheng-Jie DuanJia-Xun Feng

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