A modular xylanase from mesophilic Cellulomonas fimi contains the same cellulose-binding and thermostabilizing domains as xylanases from thermophilic bacteria

  1. Jonathan H. Clarke1,
  2. Keith Davidson1,
  3. Harry J. Gilbert2,
  4. Carlos M.G.A. Fontes2,
  5. Geoffrey P. Hazlewood1,*

Article first published online: 17 JAN 2006

DOI: 10.1111/j.1574-6968.1996.tb08175.x

Issue

FEMS Microbiology Letters

FEMS Microbiology Letters

Volume 139, Issue 1, pages 27–35, May 1996

Additional Information

How to Cite

Clarke, J. H., Davidson, K., Gilbert, H. J., Fontes, C. M. and Hazlewood, G. P. (1996), A modular xylanase from mesophilic Cellulomonas fimi contains the same cellulose-binding and thermostabilizing domains as xylanases from thermophilic bacteria. FEMS Microbiology Letters, 139: 27–35. doi: 10.1111/j.1574-6968.1996.tb08175.x

Author Information

  1. 1

    Department of Cellular Physiology, The Babraham Institute, Babraham Hall, Babraham, Cambridge CB2 4AT, UK

  2. 2

    Department of Biological and Nutritional Sciences, Faculty of Agriculture and Biological Sciences, The University, Newcastle upon Tyne NE1 7RU, UK

* *Corresponding author. Tel.: +44 (1223) 832 312; Fax; +44 (1223) 837 912.

Publication History

  1. Issue published online: 17 JAN 2006
  2. Article first published online: 17 JAN 2006
  3. (Received 3 February 1996, Revised 14 March 1996, Accepted 14 March 1996)

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Keywords:

  • Cellulomonas fimi;
  • Xylanase gene;
  • Xylanase structure;
  • Cellulose-binding domain;
  • NodB domain;
  • Therrnostabilizing domain

Abstract The xynC gene from mesophilic Cellulomonas fimi encodes a large 125 kDa modular xylanase (XYLC), consisting of six distinct functional domains. In addition to a single Family 10 catalytic domain, XYLC contains a domain homologous with the nodulation protein, NodB, from nitrogen-fixing bacteria and therrnostabilizing and cellulose-binding domains found previously only in xylanases from thermophilic bacteria.

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