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

Kaisa Poutanen, Jurgen Puls

Research output: Contribution to journalArticleScientificpeer-review

198 Citations (Scopus)

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 languageEnglish
Pages (from-to)425-432
JournalApplied Microbiology and Biotechnology
Volume28
Issue number4-5
DOIs
Publication statusPublished - 1988
MoE publication typeA1 Journal article-refereed

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