An α-glucuronidase of Schizophyllum commune acting on polymeric xylan

Maija Tenkanen (Corresponding Author), Matti Siika-aho

Research output: Contribution to journalArticleScientificpeer-review

117 Citations (Scopus)

Abstract

The main α-glucuronidase (EC 3.2.1.131) of the fungus Schizophyllum commune was purified to homogeneity using standard chromatographic methods; anion exchange, hydrophobic interaction chromatography and gel filtration. The enzyme had a molecular mass of 125 kDa as determined by SDS-polyacrylamide gel electrophoresis and a pI value of 3.6 according to isoelectric focusing. The N-terminal amino acid sequence of the S. commune α-glucuronidase did not show any homology with other α-glucuronidases. It exhibited maximal activity at pH values from 4.5 to 5.5 and was stable for 24 h between pH 6 and 8 at 40°C. The highest temperature at which the enzyme retained its full activity for 24 h at pH 5.8 was 40°C. The α-glucuronidase of S. commune was able to remove almost all 4-O-methylglucuronic acid groups from water-soluble polymeric softwood arabinoglucuronoxylans. The action of the enzyme on birchwood acetyl-glucuronoxylan was limited due to the high amount of acetyl substituents. The degree of hydrolysis of partially soluble deacetylated glucuronoxylan did not exceed 50% of the theoretical maximum. However, together with a xylanase hydrolysing the xylan backbone the action of the α-glucuronidase of S. commune on glucuronoxylan was clearly enhanced. It was apparent that the enzyme was able to remove the 4-O-methylglucuronic groups mainly from soluble substrates.

Original languageEnglish
Pages (from-to)149 - 161
Number of pages13
JournalJournal of Biotechnology
Volume78
Issue number2
DOIs
Publication statusPublished - 2000
MoE publication typeA1 Journal article-refereed

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Schizophyllum
Xylans
Glucuronidase
Enzymes
Gels
Softwoods
Molecular mass
Chromatography
Polyacrylates
Electrophoresis
Fungi
Amino acids
Isoelectric Focusing
Hydrolysis
Ion exchange
Hydrophobic and Hydrophilic Interactions
Negative ions
Gel Chromatography
Anions
Polyacrylamide Gel Electrophoresis

Cite this

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abstract = "The main α-glucuronidase (EC 3.2.1.131) of the fungus Schizophyllum commune was purified to homogeneity using standard chromatographic methods; anion exchange, hydrophobic interaction chromatography and gel filtration. The enzyme had a molecular mass of 125 kDa as determined by SDS-polyacrylamide gel electrophoresis and a pI value of 3.6 according to isoelectric focusing. The N-terminal amino acid sequence of the S. commune α-glucuronidase did not show any homology with other α-glucuronidases. It exhibited maximal activity at pH values from 4.5 to 5.5 and was stable for 24 h between pH 6 and 8 at 40°C. The highest temperature at which the enzyme retained its full activity for 24 h at pH 5.8 was 40°C. The α-glucuronidase of S. commune was able to remove almost all 4-O-methylglucuronic acid groups from water-soluble polymeric softwood arabinoglucuronoxylans. The action of the enzyme on birchwood acetyl-glucuronoxylan was limited due to the high amount of acetyl substituents. The degree of hydrolysis of partially soluble deacetylated glucuronoxylan did not exceed 50{\%} of the theoretical maximum. However, together with a xylanase hydrolysing the xylan backbone the action of the α-glucuronidase of S. commune on glucuronoxylan was clearly enhanced. It was apparent that the enzyme was able to remove the 4-O-methylglucuronic groups mainly from soluble substrates.",
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An α-glucuronidase of Schizophyllum commune acting on polymeric xylan. / Tenkanen, Maija (Corresponding Author); Siika-aho, Matti.

In: Journal of Biotechnology, Vol. 78, No. 2, 2000, p. 149 - 161.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

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PY - 2000

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