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

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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.

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Authors and Affiliations

  1. Biotechnical Laboratory, VTT, Tietotie 2, SF-02150, Espoo, Finland

    Kaisa Poutanen

  2. Bundesforschungsanstalt für Forst- und Holzwirtschaft, Institut für Holzchemie, Leuschnerstraße 91, D-2050, Hamburg 80, Federal Republic of Germany

    Jürgen Puls

Authors
  1. Kaisa Poutanen
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  2. Jürgen Puls
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Poutanen, K., Puls, J. Characteristics of Trichoderma reesei β-xylosidase and its use in the hydrolysis of solubilized xylans. Appl Microbiol Biotechnol 28, 425–432 (1988). https://doi.org/10.1007/BF00268208

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  • DOI: https://doi.org/10.1007/BF00268208

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