An α-L-arabinofuranosidase of Trichoderma reesei

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Abstract

An α-L-arabinofuranosidase (EC 3.2.1.55) of Trichoderma reesei was purified to homogeneity by cation- and anion-exchange chromatography. The enzyme had a molecular weight of 53 kDa as estimated by SDS electrophoresis.
The isoelectric point of the enzyme was 7.5 and its pH optimum was 4.0. The enzyme hydrolyzed beet arabinan and released arabinose from wheat straw arabinoxylan.
Original languageEnglish
Pages (from-to)271-281
JournalJournal of Biotechnology
Volume7
Issue number4
DOIs
Publication statusPublished - 1988
MoE publication typeA1 Journal article-refereed

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Trichoderma
Enzymes
Arabinose
Beta vulgaris
Isoelectric Point
Straw
Chromatography
Electrophoresis
Triticum
Anions
Cations
Ion exchange
Negative ions
Molecular Weight
Positive ions
Molecular weight

Cite this

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abstract = "An α-L-arabinofuranosidase (EC 3.2.1.55) of Trichoderma reesei was purified to homogeneity by cation- and anion-exchange chromatography. The enzyme had a molecular weight of 53 kDa as estimated by SDS electrophoresis. The isoelectric point of the enzyme was 7.5 and its pH optimum was 4.0. The enzyme hydrolyzed beet arabinan and released arabinose from wheat straw arabinoxylan.",
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An α-L-arabinofuranosidase of Trichoderma reesei. / Poutanen, Kaisa.

In: Journal of Biotechnology, Vol. 7, No. 4, 1988, p. 271-281.

Research output: Contribution to journalArticleScientificpeer-review

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AU - Poutanen, Kaisa

PY - 1988

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AB - An α-L-arabinofuranosidase (EC 3.2.1.55) of Trichoderma reesei was purified to homogeneity by cation- and anion-exchange chromatography. The enzyme had a molecular weight of 53 kDa as estimated by SDS electrophoresis. The isoelectric point of the enzyme was 7.5 and its pH optimum was 4.0. The enzyme hydrolyzed beet arabinan and released arabinose from wheat straw arabinoxylan.

U2 - 10.1016/0168-1656(88)90039-9

DO - 10.1016/0168-1656(88)90039-9

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