Abstract
An α-L-arabinofuranosidase (EC 3.2.1.55) of Trichoderma reesei was purified to homogeneity by cation- and anion-exchange chromatography. The enzyme had a molecular weight of 53 kDa as estimated by SDS electrophoresis.
The isoelectric point of the enzyme was 7.5 and its pH optimum was 4.0. The enzyme hydrolyzed beet arabinan and released arabinose from wheat straw arabinoxylan.
The isoelectric point of the enzyme was 7.5 and its pH optimum was 4.0. The enzyme hydrolyzed beet arabinan and released arabinose from wheat straw arabinoxylan.
| Original language | English |
|---|---|
| Pages (from-to) | 271-281 |
| Journal | Journal of Biotechnology |
| Volume | 7 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 1988 |
| MoE publication type | A1 Journal article-refereed |