Characterization of CenC, an enzyme from Cellulomonas fimi with both endo- and exoglucanase activities.

  title={Characterization of CenC, an enzyme from Cellulomonas fimi with both endo- and exoglucanase activities.},
  author={Peter Tomme and Emily M. Kwan and Neil R. Gilkes and Douglas G. Kilburn and Richard A. Warren},
  journal={Journal of bacteriology},
  volume={178 14},
The cenC gene, encoding beta-1,4-glucanase C (CenC) from Cellulomonas fimi, was overexpressed in Escherichia coli with a tac-based expression vector. The resulting polypeptide, with an apparent molecular mass of 130 kDa, was purified from the cell extracts by affinity chromatography on cellulose followed by anion-exchange chromatography. N-terminal sequence analysis showed the enzyme to be properly processed. Mature CenC was optimally active at pH 5.0 and 45 degrees C. The enzyme was extremely… CONTINUE READING
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Molecular cloning: a laboratory manual, 2nd ed

  • J. Sambrook, E. F. Fritsch, T. Maniatis
  • 1989
Highly Influential
4 Excerpts

Cellobiohydrolase B ( CbhB ) , a second cellobiohydrolase from the cellulolytic bacterium Cellulomonas fimi

  • H. Shen, M. Schmuck, +4 authors R. A. J. Warren
  • Biochem . J .
  • 1995

Cellulose-binding domains: classification and properties, p. 142–161

  • P. Tomme, R.A.J. Warren, R. C. Miller, Jr., D. G. Kilburn, N. R. Gilkes
  • 1995
1 Excerpt

Purification and characterization of a less randomly acting endo-1,4b-D-glucanase from the culture filtrate of Fusarium oxysporum

  • P. Christakopoulos, D. Kekos, B. J. Marcis, M. Claeyssens, M. K. Bhat
  • 1995
1 Excerpt

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