Current Genetics

, Volume 26, Issue 3, pp 228–232

Isolation and characterization of a 1,4-β-endoxylanase gene of A. awamori

Authors

  • Johanna G. M. Hessing
    • TNO Nutrition and Food Research
  • Co van Rotterdam
    • TNO Nutrition and Food Research
  • John M. A. Verbakel
    • Unilever Research Laboratories
  • Martinus Roza
    • Unilever Research Laboratories
  • Jan Maat
    • Unilever Research Laboratories
  • Robert F. M. van Gorcom
    • TNO Nutrition and Food Research
  • Cees A. M. J. J. van den Hondel
    • TNO Nutrition and Food Research
Original Articles

DOI: 10.1007/BF00309552

Cite this article as:
Hessing, J.G.M., van Rotterdam, C., Verbakel, J.M.A. et al. Curr Genet (1994) 26: 228. doi:10.1007/BF00309552

Abstract

An enzyme with a particular 1,4-β-xylanase activity was identified and purified from wheat-bran culture medium of an Aspergillus awamori strain. With oligonucleotides based on the N-terminal amino-acid sequence of the enzyme, the exlA gene of A. awamori, encoding 1,4-β-xylanase A, has been cloned. Based on the deduced amino-acid sequence, 1,4-β-xylanase A is produced as a 211 amino-acid-residue-long precursor, which is converted post-translationally into a 184-aa-residue-long mature protein. Transformation of the original A. awamori strain with multiple copies of the exlA gene resulted in a 40-fold overproduction of 1,4-β-xylanase A. The overproduced enzyme has the same biochemical and enzymological properties as the wild-type enzyme.

Key words

Aspergillus awamoriEnzyme (1,4-β-D-xylanohydrolase E.C. 3.2.1.8) purificationexlA gene isolationMulticopy transformantOverexpression
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Copyright information

© Springer-Verlag 1994