Characterization of XYN10B, a modular xylanase from the ruminal protozoan Polyplastron multivesiculatum, with a family 22 carbohydrate-binding module that binds to cellulose

Estelle Devillard, Christel Bera-Maillet, Harry J Flint, Karen P Scott, C James Newbold, R John Wallace, Jean-Pierre Jouany, Evelyne Forano

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

A new xylanase gene, xyn10B, was isolated from the ruminal protozoan Polyplastron multivesiculatum and the gene product was characterized. XYN10B is the first protozoan family 10 glycoside hydrolase characterized so far and is a modular enzyme comprising a family 22 carbohydrate-binding module (CBM) preceding the catalytic domain. The CBM22 was shown to be a true CBM. It showed high affinity for soluble arabinoxylan and is the first example of a CBM22 that binds strongly to celluloses of various crystallinities. The enzymic properties of XYN10B were also analysed. Its optimal temperature and pH for activity were 39 degrees C and 7.0 respectively; these values being close to those of the ruminal ecosystem. The phylogenetic relationships between the XYN10B CBM22 or catalytic domain and related sequences from ruminal and non-ruminal bacteria and eukaryotes are reported. The xyn10B gene is shown to lack introns.

Original languageEnglish
Pages (from-to)495-503
Number of pages9
JournalBiochemical Journal
Volume373
Issue numberPt 2
DOIs
Publication statusPrint publication - 15 Jul 2003
Externally publishedYes

Fingerprint

Cellulose
Genes
Carbohydrates
Catalytic Domain
Glycoside Hydrolases
Eukaryota
Ecosystems
Introns
Ecosystem
Bacteria
Temperature
Enzymes
arabinoxylan

Keywords

  • Animals
  • Blotting, Western
  • Catalytic Domain
  • Cellulose/metabolism
  • Ciliophora/enzymology
  • Cloning, Molecular
  • Crystallization
  • DNA Primers/chemistry
  • DNA, Bacterial/metabolism
  • Glycoside Hydrolases/chemistry
  • Hydrogen-Ion Concentration
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Plasmids
  • Polymerase Chain Reaction
  • Polysaccharides/metabolism
  • Protein Binding
  • Protozoan Proteins/metabolism
  • Sequence Deletion
  • Substrate Specificity
  • Xylan Endo-1,3-beta-Xylosidase
  • Xylans/metabolism
  • Xylosidases/metabolism

Cite this

Devillard, Estelle ; Bera-Maillet, Christel ; Flint, Harry J ; Scott, Karen P ; Newbold, C James ; Wallace, R John ; Jouany, Jean-Pierre ; Forano, Evelyne. / Characterization of XYN10B, a modular xylanase from the ruminal protozoan Polyplastron multivesiculatum, with a family 22 carbohydrate-binding module that binds to cellulose. In: Biochemical Journal. 2003 ; Vol. 373, No. Pt 2. pp. 495-503.
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abstract = "A new xylanase gene, xyn10B, was isolated from the ruminal protozoan Polyplastron multivesiculatum and the gene product was characterized. XYN10B is the first protozoan family 10 glycoside hydrolase characterized so far and is a modular enzyme comprising a family 22 carbohydrate-binding module (CBM) preceding the catalytic domain. The CBM22 was shown to be a true CBM. It showed high affinity for soluble arabinoxylan and is the first example of a CBM22 that binds strongly to celluloses of various crystallinities. The enzymic properties of XYN10B were also analysed. Its optimal temperature and pH for activity were 39 degrees C and 7.0 respectively; these values being close to those of the ruminal ecosystem. The phylogenetic relationships between the XYN10B CBM22 or catalytic domain and related sequences from ruminal and non-ruminal bacteria and eukaryotes are reported. The xyn10B gene is shown to lack introns.",
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Characterization of XYN10B, a modular xylanase from the ruminal protozoan Polyplastron multivesiculatum, with a family 22 carbohydrate-binding module that binds to cellulose. / Devillard, Estelle; Bera-Maillet, Christel; Flint, Harry J; Scott, Karen P; Newbold, C James; Wallace, R John; Jouany, Jean-Pierre; Forano, Evelyne.

In: Biochemical Journal, Vol. 373, No. Pt 2, 15.07.2003, p. 495-503.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Characterization of XYN10B, a modular xylanase from the ruminal protozoan Polyplastron multivesiculatum, with a family 22 carbohydrate-binding module that binds to cellulose

AU - Devillard, Estelle

AU - Bera-Maillet, Christel

AU - Flint, Harry J

AU - Scott, Karen P

AU - Newbold, C James

AU - Wallace, R John

AU - Jouany, Jean-Pierre

AU - Forano, Evelyne

PY - 2003/7/15

Y1 - 2003/7/15

N2 - A new xylanase gene, xyn10B, was isolated from the ruminal protozoan Polyplastron multivesiculatum and the gene product was characterized. XYN10B is the first protozoan family 10 glycoside hydrolase characterized so far and is a modular enzyme comprising a family 22 carbohydrate-binding module (CBM) preceding the catalytic domain. The CBM22 was shown to be a true CBM. It showed high affinity for soluble arabinoxylan and is the first example of a CBM22 that binds strongly to celluloses of various crystallinities. The enzymic properties of XYN10B were also analysed. Its optimal temperature and pH for activity were 39 degrees C and 7.0 respectively; these values being close to those of the ruminal ecosystem. The phylogenetic relationships between the XYN10B CBM22 or catalytic domain and related sequences from ruminal and non-ruminal bacteria and eukaryotes are reported. The xyn10B gene is shown to lack introns.

AB - A new xylanase gene, xyn10B, was isolated from the ruminal protozoan Polyplastron multivesiculatum and the gene product was characterized. XYN10B is the first protozoan family 10 glycoside hydrolase characterized so far and is a modular enzyme comprising a family 22 carbohydrate-binding module (CBM) preceding the catalytic domain. The CBM22 was shown to be a true CBM. It showed high affinity for soluble arabinoxylan and is the first example of a CBM22 that binds strongly to celluloses of various crystallinities. The enzymic properties of XYN10B were also analysed. Its optimal temperature and pH for activity were 39 degrees C and 7.0 respectively; these values being close to those of the ruminal ecosystem. The phylogenetic relationships between the XYN10B CBM22 or catalytic domain and related sequences from ruminal and non-ruminal bacteria and eukaryotes are reported. The xyn10B gene is shown to lack introns.

KW - Animals

KW - Blotting, Western

KW - Catalytic Domain

KW - Cellulose/metabolism

KW - Ciliophora/enzymology

KW - Cloning, Molecular

KW - Crystallization

KW - DNA Primers/chemistry

KW - DNA, Bacterial/metabolism

KW - Glycoside Hydrolases/chemistry

KW - Hydrogen-Ion Concentration

KW - Magnetic Resonance Spectroscopy

KW - Molecular Sequence Data

KW - Plasmids

KW - Polymerase Chain Reaction

KW - Polysaccharides/metabolism

KW - Protein Binding

KW - Protozoan Proteins/metabolism

KW - Sequence Deletion

KW - Substrate Specificity

KW - Xylan Endo-1,3-beta-Xylosidase

KW - Xylans/metabolism

KW - Xylosidases/metabolism

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DO - 10.1042/BJ20021784

M3 - Article

C2 - 12693992

VL - 373

SP - 495

EP - 503

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - Pt 2

ER -