Xylanase XYN IV from Trichoderma reesei showing exo- and endo-xylanase activity

Maija Tenkanen, Mária Vršanská, Matti Siika-Aho, Dominic W. Wong, Vladimír Puchart, Merja Penttilä, Markku Saloheimo, Peter Biely (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

39 Citations (Scopus)

Abstract

A minor xylanase, named XYN IV, was purified from the cellulolytic system of the fungus Trichoderma reesei Rut C30. The enzyme was discovered on the basis of its ability to attack aldotetraohexenuronic acid (HexA-2Xyl-4Xyl-4Xyl, HexA3Xyl3), releasing the reducing-end xylose residue. XYN IV exhibited catalytic properties incompatible with previously described endo-β-1,4-xylanases of this fungus, XYN I, XYN II and XYN III, and the xylan-hydrolyzing endo-β-1,4-glucanase EG I. XYN IV was able to degrade several different β-1,4-xylans, but was inactive on β-1,4-mannans and β-1,4-glucans. It showed both exo-and endo-xylanase activity. Rhodymenan, a linear soluble β-1,3-β-1,4-xylan, was as the best substrate. Linear xylooligosaccharides were attacked exclusively at the first glycosidic linkage from the reducing end. The gene xyn4, encoding XYN IV, was also isolated. It showed clear homology with xylanases classified in glycoside hydrolase family 30, which also includes glucanases and mannanases. The xyn4 gene was expressed slightly when grown on xylose and xylitol, clearly on arabinose, arabitol, sophorose, xylobiose, xylan and cellulose, but not on glucose or sorbitol, resembling induction of other xylanolytic enzymes from T. reesei. A recombinant enzyme prepared in a Pichia pastoris expression system exhibited identical catalytic properties to the enzyme isolated from the T. reesei culture medium. The physiological role of this unique enzyme remains unknown, but it may involve liberation of xylose from the reducing end of branched oligosaccharides that are resistant toward β-xylosidase and other types of endoxylanases. In terms of its catalytic properties, XYN IV differs from bacterial GH family 30 glucuronoxylanases that recognize 4-O-methyl-d-glucuronic acid (MeGlcA) substituents as substrate specificity determinants.

Original languageEnglish
Pages (from-to)285-301
JournalFEBS Journal
Volume280
Issue number1
DOIs
Publication statusPublished - 1 Jan 2013
MoE publication typeA1 Journal article-refereed

Fingerprint

Trichoderma
Xylose
Enzymes
Xylans
glucuronoxylan xylanohydrolase
Fungi
Xylosidases
Endo-1,4-beta Xylanases
Xylitol
Mannans
Glucuronic Acid
Arabinose
Gene encoding
Pichia
Sorbitol
Glycoside Hydrolases
Substrates
Substrate Specificity
Oligosaccharides
Cellulose

Keywords

  • exo- and endo-acting β-1,4-xylanase
  • glycoside hydrolase family 30
  • Trichoderma reesei
  • xylan
  • xylooligosaccharides

Cite this

Tenkanen, Maija ; Vršanská, Mária ; Siika-Aho, Matti ; Wong, Dominic W. ; Puchart, Vladimír ; Penttilä, Merja ; Saloheimo, Markku ; Biely, Peter. / Xylanase XYN IV from Trichoderma reesei showing exo- and endo-xylanase activity. In: FEBS Journal. 2013 ; Vol. 280, No. 1. pp. 285-301.
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title = "Xylanase XYN IV from Trichoderma reesei showing exo- and endo-xylanase activity",
abstract = "A minor xylanase, named XYN IV, was purified from the cellulolytic system of the fungus Trichoderma reesei Rut C30. The enzyme was discovered on the basis of its ability to attack aldotetraohexenuronic acid (HexA-2Xyl-4Xyl-4Xyl, HexA3Xyl3), releasing the reducing-end xylose residue. XYN IV exhibited catalytic properties incompatible with previously described endo-β-1,4-xylanases of this fungus, XYN I, XYN II and XYN III, and the xylan-hydrolyzing endo-β-1,4-glucanase EG I. XYN IV was able to degrade several different β-1,4-xylans, but was inactive on β-1,4-mannans and β-1,4-glucans. It showed both exo-and endo-xylanase activity. Rhodymenan, a linear soluble β-1,3-β-1,4-xylan, was as the best substrate. Linear xylooligosaccharides were attacked exclusively at the first glycosidic linkage from the reducing end. The gene xyn4, encoding XYN IV, was also isolated. It showed clear homology with xylanases classified in glycoside hydrolase family 30, which also includes glucanases and mannanases. The xyn4 gene was expressed slightly when grown on xylose and xylitol, clearly on arabinose, arabitol, sophorose, xylobiose, xylan and cellulose, but not on glucose or sorbitol, resembling induction of other xylanolytic enzymes from T. reesei. A recombinant enzyme prepared in a Pichia pastoris expression system exhibited identical catalytic properties to the enzyme isolated from the T. reesei culture medium. The physiological role of this unique enzyme remains unknown, but it may involve liberation of xylose from the reducing end of branched oligosaccharides that are resistant toward β-xylosidase and other types of endoxylanases. In terms of its catalytic properties, XYN IV differs from bacterial GH family 30 glucuronoxylanases that recognize 4-O-methyl-d-glucuronic acid (MeGlcA) substituents as substrate specificity determinants.",
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Xylanase XYN IV from Trichoderma reesei showing exo- and endo-xylanase activity. / Tenkanen, Maija; Vršanská, Mária; Siika-Aho, Matti; Wong, Dominic W.; Puchart, Vladimír; Penttilä, Merja; Saloheimo, Markku; Biely, Peter (Corresponding Author).

In: FEBS Journal, Vol. 280, No. 1, 01.01.2013, p. 285-301.

Research output: Contribution to journalArticleScientificpeer-review

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T1 - Xylanase XYN IV from Trichoderma reesei showing exo- and endo-xylanase activity

AU - Tenkanen, Maija

AU - Vršanská, Mária

AU - Siika-Aho, Matti

AU - Wong, Dominic W.

AU - Puchart, Vladimír

AU - Penttilä, Merja

AU - Saloheimo, Markku

AU - Biely, Peter

N1 - CA2: TK404 CA2: TK400 CA2: TK402 SDA: BIC ISI: BIOCHEMISTRY & MOLECULAR BIOLOGY

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N2 - A minor xylanase, named XYN IV, was purified from the cellulolytic system of the fungus Trichoderma reesei Rut C30. The enzyme was discovered on the basis of its ability to attack aldotetraohexenuronic acid (HexA-2Xyl-4Xyl-4Xyl, HexA3Xyl3), releasing the reducing-end xylose residue. XYN IV exhibited catalytic properties incompatible with previously described endo-β-1,4-xylanases of this fungus, XYN I, XYN II and XYN III, and the xylan-hydrolyzing endo-β-1,4-glucanase EG I. XYN IV was able to degrade several different β-1,4-xylans, but was inactive on β-1,4-mannans and β-1,4-glucans. It showed both exo-and endo-xylanase activity. Rhodymenan, a linear soluble β-1,3-β-1,4-xylan, was as the best substrate. Linear xylooligosaccharides were attacked exclusively at the first glycosidic linkage from the reducing end. The gene xyn4, encoding XYN IV, was also isolated. It showed clear homology with xylanases classified in glycoside hydrolase family 30, which also includes glucanases and mannanases. The xyn4 gene was expressed slightly when grown on xylose and xylitol, clearly on arabinose, arabitol, sophorose, xylobiose, xylan and cellulose, but not on glucose or sorbitol, resembling induction of other xylanolytic enzymes from T. reesei. A recombinant enzyme prepared in a Pichia pastoris expression system exhibited identical catalytic properties to the enzyme isolated from the T. reesei culture medium. The physiological role of this unique enzyme remains unknown, but it may involve liberation of xylose from the reducing end of branched oligosaccharides that are resistant toward β-xylosidase and other types of endoxylanases. In terms of its catalytic properties, XYN IV differs from bacterial GH family 30 glucuronoxylanases that recognize 4-O-methyl-d-glucuronic acid (MeGlcA) substituents as substrate specificity determinants.

AB - A minor xylanase, named XYN IV, was purified from the cellulolytic system of the fungus Trichoderma reesei Rut C30. The enzyme was discovered on the basis of its ability to attack aldotetraohexenuronic acid (HexA-2Xyl-4Xyl-4Xyl, HexA3Xyl3), releasing the reducing-end xylose residue. XYN IV exhibited catalytic properties incompatible with previously described endo-β-1,4-xylanases of this fungus, XYN I, XYN II and XYN III, and the xylan-hydrolyzing endo-β-1,4-glucanase EG I. XYN IV was able to degrade several different β-1,4-xylans, but was inactive on β-1,4-mannans and β-1,4-glucans. It showed both exo-and endo-xylanase activity. Rhodymenan, a linear soluble β-1,3-β-1,4-xylan, was as the best substrate. Linear xylooligosaccharides were attacked exclusively at the first glycosidic linkage from the reducing end. The gene xyn4, encoding XYN IV, was also isolated. It showed clear homology with xylanases classified in glycoside hydrolase family 30, which also includes glucanases and mannanases. The xyn4 gene was expressed slightly when grown on xylose and xylitol, clearly on arabinose, arabitol, sophorose, xylobiose, xylan and cellulose, but not on glucose or sorbitol, resembling induction of other xylanolytic enzymes from T. reesei. A recombinant enzyme prepared in a Pichia pastoris expression system exhibited identical catalytic properties to the enzyme isolated from the T. reesei culture medium. The physiological role of this unique enzyme remains unknown, but it may involve liberation of xylose from the reducing end of branched oligosaccharides that are resistant toward β-xylosidase and other types of endoxylanases. In terms of its catalytic properties, XYN IV differs from bacterial GH family 30 glucuronoxylanases that recognize 4-O-methyl-d-glucuronic acid (MeGlcA) substituents as substrate specificity determinants.

KW - exo- and endo-acting β-1,4-xylanase

KW - glycoside hydrolase family 30

KW - Trichoderma reesei

KW - xylan

KW - xylooligosaccharides

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