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

@article{Tomme1996CharacterizationOC,
  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},
  year={1996},
  volume={178 14},
  pages={4216-23}
}
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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