Applied Microbiology and Biotechnology

, Volume 28, Issue 4–5, pp 425–432

Characteristics of Trichoderma reeseiβ-xylosidase and its use in the hydrolysis of solubilized xylans

  • Kaisa Poutanen
  • Jürgen Puls
Biotechnology

DOI: 10.1007/BF00268208

Cite this article as:
Poutanen, K. & Puls, J. Appl Microbiol Biotechnol (1988) 28: 425. doi:10.1007/BF00268208
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Summary

The β-xylosidase (EC 3.2.1.37) of Trichoderma reesei was purified and its characteristics and use in the hydrolysis of steamed birch xylan were studied. The enzyme was a glycoprotein with a molecular weight of 100000 as determined by SDS-gel electrophoresis and its isoelectric point was 4.7. The pH optimum was 4.0 and temperature optimum 60°C. β-Xylosidase was competitively inhibited by xylose and the inhibition constant was 2.3 mM. The purified enzyme also showed α-arabinofuranosidase activity.

Copyright information

© Springer-Verlag 1988

Authors and Affiliations

  • Kaisa Poutanen
    • 1
  • Jürgen Puls
    • 2
  1. 1.Biotechnical LaboratoryVTTEspooFinland
  2. 2.Bundesforschungsanstalt für Forst- und HolzwirtschaftInstitut für HolzchemieHamburg 80Federal Republic of Germany

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