The adsorption of a bacterial cellulase and its two isolated domains to crystalline cellulose.

@article{Gilkes1992TheAO,
  title={The adsorption of a bacterial cellulase and its two isolated domains to crystalline cellulose.},
  author={Neil R. Gilkes and Eric Jervis and Bernard Henrissat and Bahar Tekant and Robert C. Miller and Richard A. Warren and Douglas G. Kilburn},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 10},
  pages={6743-9}
}
CenA is a bacterial cellulase (beta-1,4-glucanase) comprised of a globular catalytic domain joined to an extended cellulose-binding domain (CBD) by a short linker peptide. The adsorption of CenA and its two isolated domains to crystalline cellulose was analyzed. CenA and CBD.PTCenA' (the CBD plus linker) adsorbed rapidly to cellulose at 30 degrees C, and no net desorption of protein was observed during the following 16.7 h. There was no detectable adsorption of the catalytic domain. Scatchard… CONTINUE READING

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