Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 425-432 |
| Journal | Applied Microbiology and Biotechnology |
| Volume | 28 |
| Issue number | 4-5 |
| DOIs | |
| Publication status | Published - 1988 |
| MoE publication type | A1 Journal article-refereed |