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

193 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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Xylosidases
Xylans
Trichoderma
Hydrolysis
Betula
Xylose
Isoelectric Point
Enzymes
Electrophoresis
Glycoproteins
Molecular Weight
Gels
Temperature

Cite this

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title = "Characteristics of Trichoderma reesei {\ss}-xylosidase and its use in the hydrolysis of solubilized xylans",
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.",
author = "Kaisa Poutanen and Jurgen Puls",
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journal = "Applied Microbiology and Biotechnology",
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Characteristics of Trichoderma reesei ß-xylosidase and its use in the hydrolysis of solubilized xylans. / Poutanen, Kaisa; Puls, Jurgen.

In: Applied Microbiology and Biotechnology, Vol. 28, No. 4-5, 1988, p. 425-432.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Characteristics of Trichoderma reesei ß-xylosidase and its use in the hydrolysis of solubilized xylans

AU - Poutanen, Kaisa

AU - Puls, Jurgen

PY - 1988

Y1 - 1988

N2 - 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.

AB - 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.

U2 - 10.1007/BF00268208

DO - 10.1007/BF00268208

M3 - Article

VL - 28

SP - 425

EP - 432

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 0175-7598

IS - 4-5

ER -