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Applied Microbiology and Biotechnology

, Volume 42, Issue 4, pp 555–562 | Cite as

Purification, characterization and regulation of the synthesis of an Aspergillus nidulans acidic xylanase

  • M. Fernández-Espinar
  • F. Piñaga
  • L. de Graaff
  • J. Visser
  • D. Ramón
  • S. Vallés
Biochemical Engineering Original Paper

Abstract

An acidic xylanase from a culture filtrate of Aspergillus nidulans grown on oat-spelt xylan was purified to apparent homogeneity. The purified enzyme showed a single band on sodium dodecyl sulphate-polyacrylamide gel electrophoresis with a molecular mass of 34,000 Da and had an isoelectric point of approximately 3.4. The enzyme was a non-debranching endoxylanase highly specific for xylans. The xylanase showed an optimal activity at pH 6.0 and 56° C and had a Michaelis constant Km of 0.97 mg oat-spelt xylan (soluble fraction) ml and a maximed reaction velocity (Vmax) of 1,091 μmol min−1 (mg−1protein)−1. Using polyclonal antibodies raised against the purified enzyme, the regulation of its synthesis has been studied. The xylanase production is repressed by glucose and induced by oat-spelt xylan, arabinoxylan, 4-O-methylglucurono-xylan, birchwood xylan and xylose.

Keywords

Enzyme Molecular Mass Xylose Aspergillus Isoelectric Point 
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 1994

Authors and Affiliations

  • M. Fernández-Espinar
    • 1
  • F. Piñaga
    • 1
  • L. de Graaff
    • 2
  • J. Visser
    • 2
  • D. Ramón
    • 1
  • S. Vallés
    • 1
  1. 1.Departamento de Biotechnología. Instituto de Agroquímica y Technología de AlimentosCSICValenciaSpain
  2. 2.Section Molecular Genetics of Industrial MicroorganismsWageningen Agricultural UniversityWageningenThe Netherlands

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