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Applied Microbiology and Biotechnology

, Volume 50, Issue 2, pp 284–287 | Cite as

Application of the affinity binding of xylanases to oat-spelt xylan in the purification of endoxylanase CM-2 from Streptomyces chattanoogensis CECT 3336

  • C. L. López-Fernández
  • J. Rodríguez
  • A. S. Ball
  • J. L. Copa-Patiño
  • M. I. Pérez-Leblic
  • M. E. Arias
SHORT CONTRIBUTION

bstract

The use of the insoluble polysaccharides Avicel and oat-spelt xylan for the binding and subsequent purification of active xylanases from Streptomyces chattanoogensis was investigated. Maximum recovery of xylanases was achieved with oat-spelt xylan, using NaCl (2 M) to remove active protein. The application of this technique to the purification of xylanases resulted in the purification of an endoxylanase (CM-2) with high specific activity (729.5 U mg−1). The properties of the purified enzyme, exhibiting activity and stability between 40 °C and 60 °C and between pH 5 and 8, suggest a potential role for both the enzyme and the rapid purification protocol in the removal of hemicelluloses from kraft pulp prior to bleaching.

Keywords

Enzyme Purification Polysaccharide Streptomyces Potential Role 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1998

Authors and Affiliations

  • C. L. López-Fernández
    • 1
  • J. Rodríguez
    • 1
  • A. S. Ball
    • 2
  • J. L. Copa-Patiño
    • 1
  • M. I. Pérez-Leblic
    • 1
  • M. E. Arias
    • 1
  1. 1.Departamento de Microbiología y Parasitología, Universidad de Alcalá, 28871 Alcalá de Henares, Madrid, Spain e-mail: MPMAF@ MICROB.ALCALA.ES Tel.: +34-1-8854633 Fax: +34-1-8854623ES
  2. 2.Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester, CO43SQ, UKGB

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