Characteristics of Trichoderma reeseiβ-xylosidase and its use in the hydrolysis of solubilized xylans
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- Poutanen, K. & Puls, J. Appl Microbiol Biotechnol (1988) 28: 425. doi:10.1007/BF00268208
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The β-xylosidase (EC 184.108.40.206) 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.