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

Kaisa Poutanen, Maija Sundberg

Research output: Contribution to journalArticleScientificpeer-review

83 Citations (Scopus)

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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Xylans
Trichoderma
Esterases
Hydrolysis
Acetic Acid
Triacetin
Enzymes
Xylosidases
Endo-1,4-beta Xylanases
Isoelectric Point
Isoenzymes
Gel Chromatography
Anions
Electrophoresis
Cations
Chromatography
Acetates
Molecular Weight

Cite this

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title = "An acetyl esterase of Trichoderma reesei and its role in the hydrolysis of acetyl xylans",
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.",
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volume = "28",
pages = "419--424",
journal = "Applied Microbiology and Biotechnology",
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An acetyl esterase of Trichoderma reesei and its role in the hydrolysis of acetyl xylans. / Poutanen, Kaisa; Sundberg, Maija.

In: Applied Microbiology and Biotechnology, Vol. 28, No. 4-5, 1988, p. 419-424.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - An acetyl esterase of Trichoderma reesei and its role in the hydrolysis of acetyl xylans

AU - Poutanen, Kaisa

AU - Sundberg, Maija

PY - 1988

Y1 - 1988

N2 - 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.

AB - 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.

U2 - 10.1007/BF00268207

DO - 10.1007/BF00268207

M3 - Article

VL - 28

SP - 419

EP - 424

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 0175-7598

IS - 4-5

ER -