An acetyl esterase of Trichoderma reesei and its role in the hydrolysis of acetyl xylans

Kaisa Poutanen, Maija Sundberg

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Abstract

An acetyl esterase was purified from Trichoderma reesei by cation and anion exchange chromatography.
The enzyme had a molecular weight of 45 000 as determined by SDS-electrophoresis, or 67 000 as determined by gel filtration. In chromatofocusing the enzyme was shown to consist of two isoenzymes with isoelectric points of 6.8 and 6.0. The enzyme showed activity towards naphthyl acetate, triacetin and glucose-and xylose acetates.
However, it liberated acetic acid from acetylated xylo-oligomers only to a small extent. The liberation of acetic acid from the oligomeric substrate was enhanced by addition of endoxylanase and β-xylosidase.
Original languageEnglish
Pages (from-to)419-424
JournalApplied Microbiology and Biotechnology
Volume28
Issue number4-5
DOIs
Publication statusPublished - 1988
MoE publication typeA1 Journal article-refereed

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