An α-glucuronidase from Trichoderma reesei RUT C-30

Matti Siika-aho, Maija Tenkanen, Johanna Buchert, Jurgen Puls, Liisa Viikari

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

The major α-glucuronidase of T. reesei Rut C-30 was purified by chromatographic methods. The molecular and hydrolytic properties of the purified enzyme were studied. The enzyme had a molecular weight of 91,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and a pI of 5.0–6.2 as determined by chromatofocusing. The pH optimum was pH 4.5–6.0 and the enzyme was stable for 24 h at 40°C at pH 4.8–5.5. The purified α-glucuronidase preferred low-molecular-weight xylooligomers as substrate. The enzyme seemed to act almost exclusively on the bond between the terminal xylose at the nonreducing end of a xylose chain and the methyl glucuronic acid attached to it. Minor activity against long-chain glucuronoxylan was also detected. A significant enhancing effect of α-glucuronidase on the hydrolysis of glucuronoxylan by pure xylanases was observed.
Original languageEnglish
Pages (from-to)813-819
Number of pages7
JournalEnzyme and Microbial Technology
Volume16
Issue number9
DOIs
Publication statusPublished - 1994
MoE publication typeA1 Journal article-refereed

Fingerprint

Trichoderma
Glucuronidase
Enzymes
Xylose
Molecular Weight
Molecular weight
Glucuronic Acid
Sodium dodecyl sulfate
Polyacrylates
Electrophoresis
Sodium Dodecyl Sulfate
Polyacrylamide Gel Electrophoresis
Hydrolysis
Gels
Acids
Substrates
glucuronoxylan

Cite this

Siika-aho, Matti ; Tenkanen, Maija ; Buchert, Johanna ; Puls, Jurgen ; Viikari, Liisa. / An α-glucuronidase from Trichoderma reesei RUT C-30. In: Enzyme and Microbial Technology. 1994 ; Vol. 16, No. 9. pp. 813-819.
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title = "An α-glucuronidase from Trichoderma reesei RUT C-30",
abstract = "The major α-glucuronidase of T. reesei Rut C-30 was purified by chromatographic methods. The molecular and hydrolytic properties of the purified enzyme were studied. The enzyme had a molecular weight of 91,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and a pI of 5.0–6.2 as determined by chromatofocusing. The pH optimum was pH 4.5–6.0 and the enzyme was stable for 24 h at 40°C at pH 4.8–5.5. The purified α-glucuronidase preferred low-molecular-weight xylooligomers as substrate. The enzyme seemed to act almost exclusively on the bond between the terminal xylose at the nonreducing end of a xylose chain and the methyl glucuronic acid attached to it. Minor activity against long-chain glucuronoxylan was also detected. A significant enhancing effect of α-glucuronidase on the hydrolysis of glucuronoxylan by pure xylanases was observed.",
author = "Matti Siika-aho and Maija Tenkanen and Johanna Buchert and Jurgen Puls and Liisa Viikari",
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An α-glucuronidase from Trichoderma reesei RUT C-30. / Siika-aho, Matti; Tenkanen, Maija; Buchert, Johanna; Puls, Jurgen; Viikari, Liisa.

In: Enzyme and Microbial Technology, Vol. 16, No. 9, 1994, p. 813-819.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - An α-glucuronidase from Trichoderma reesei RUT C-30

AU - Siika-aho, Matti

AU - Tenkanen, Maija

AU - Buchert, Johanna

AU - Puls, Jurgen

AU - Viikari, Liisa

N1 - Project code: BREL4306

PY - 1994

Y1 - 1994

N2 - The major α-glucuronidase of T. reesei Rut C-30 was purified by chromatographic methods. The molecular and hydrolytic properties of the purified enzyme were studied. The enzyme had a molecular weight of 91,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and a pI of 5.0–6.2 as determined by chromatofocusing. The pH optimum was pH 4.5–6.0 and the enzyme was stable for 24 h at 40°C at pH 4.8–5.5. The purified α-glucuronidase preferred low-molecular-weight xylooligomers as substrate. The enzyme seemed to act almost exclusively on the bond between the terminal xylose at the nonreducing end of a xylose chain and the methyl glucuronic acid attached to it. Minor activity against long-chain glucuronoxylan was also detected. A significant enhancing effect of α-glucuronidase on the hydrolysis of glucuronoxylan by pure xylanases was observed.

AB - The major α-glucuronidase of T. reesei Rut C-30 was purified by chromatographic methods. The molecular and hydrolytic properties of the purified enzyme were studied. The enzyme had a molecular weight of 91,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and a pI of 5.0–6.2 as determined by chromatofocusing. The pH optimum was pH 4.5–6.0 and the enzyme was stable for 24 h at 40°C at pH 4.8–5.5. The purified α-glucuronidase preferred low-molecular-weight xylooligomers as substrate. The enzyme seemed to act almost exclusively on the bond between the terminal xylose at the nonreducing end of a xylose chain and the methyl glucuronic acid attached to it. Minor activity against long-chain glucuronoxylan was also detected. A significant enhancing effect of α-glucuronidase on the hydrolysis of glucuronoxylan by pure xylanases was observed.

U2 - 10.1016/0141-0229(94)90041-8

DO - 10.1016/0141-0229(94)90041-8

M3 - Article

VL - 16

SP - 813

EP - 819

JO - Enzyme and Microbial Technology

JF - Enzyme and Microbial Technology

SN - 0141-0229

IS - 9

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