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

Kaisa Poutanen; Jürgen Puls

doi:10.1007/BF00268208

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

Kaisa Poutanen
, Jürgen Puls

Thünen Institute of Wood Research

Research output: Contribution to journal › Article › Scientific › peer-review

214 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 language	English
Pages (from-to)	425-432
Journal	Applied Microbiology and Biotechnology
Volume	28
Issue number	4-5
DOIs	https://doi.org/10.1007/BF00268208
Publication status	Published - 1988
MoE publication type	A1 Journal article-refereed

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10.1007/BF00268208

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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 J{\"u}rgen Puls",

year = "1988",

doi = "10.1007/BF00268208",

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journal = "Applied Microbiology and Biotechnology",

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

AU - Poutanen, Kaisa

AU - Puls, Jürgen

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

SN - 0175-7598

VL - 28

SP - 425

EP - 432

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

IS - 4-5

ER -

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

Abstract

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