A xylanase produced by the rumen anaerobic protozoan Polyplastron multivesiculatum shows close sequence similarity to family 11 xylanases from Gram-positive bacteria

E  Devillard; C J  Newbold; K P  Scott; E  Forano; R J Wallace; J P  Jouany; H J Flint

doi:10.1111/j.1574-6968.1999.tb08837.x

A xylanase produced by the rumen anaerobic protozoan Polyplastron multivesiculatum shows close sequence similarity to family 11 xylanases from Gram-positive bacteria

E Devillard, C J Newbold, K P Scott, E Forano, R J Wallace, J P Jouany, H J Flint

The Rowett Institute of Nutrition and Health

Research output: Contribution to journal › Article › peer-review

49 Citations (Scopus)

Abstract

We report for the first time the cloning and characterisation of a protozoal enzyme involved in plant cell wall polysaccharide degradation. A cDNA library was constructed from the ruminal protozoan Polyplastron multivesiculatum and a stable clone expressing xylanase activity was isolated. The encoded enzyme belongs to the glycoside hydrolase family 11, and phylogenetic analysis indicates a closer relationship with catalytic domains from Gram-positive bacteria than the other fibrolytic eukaryotes from the rumen, the anaerobic fungi. (C) 1999 Published by Elsevier Science B.V. All rights reserved.

Original language	English
Pages (from-to)	145-152
Number of pages	8
Journal	FEMS Microbiology Letters
Volume	181
Issue number	1
DOIs	https://doi.org/10.1111/j.1574-6968.1999.tb08837.x
Publication status	Published - 1 Dec 1999

Keywords

rumen
protozoa
xylanase
polyplastron multivesiculatum
cellulolytic bacteria
fungi
gene
populations
cellulases
digestion
protein
domains
enzymes
sheep

Access to Document

10.1111/j.1574-6968.1999.tb08837.xLicence: Unspecified

Cite this

Devillard, E., Newbold, C. J., Scott, K. P., Forano, E., Wallace, R. J., Jouany, J. P., & Flint, H. J. (1999). A xylanase produced by the rumen anaerobic protozoan Polyplastron multivesiculatum shows close sequence similarity to family 11 xylanases from Gram-positive bacteria. FEMS Microbiology Letters, 181(1), 145-152. https://doi.org/10.1111/j.1574-6968.1999.tb08837.x

@article{9daf840442b6496bafba7910334b7538,

title = "A xylanase produced by the rumen anaerobic protozoan Polyplastron multivesiculatum shows close sequence similarity to family 11 xylanases from Gram-positive bacteria",

abstract = "We report for the first time the cloning and characterisation of a protozoal enzyme involved in plant cell wall polysaccharide degradation. A cDNA library was constructed from the ruminal protozoan Polyplastron multivesiculatum and a stable clone expressing xylanase activity was isolated. The encoded enzyme belongs to the glycoside hydrolase family 11, and phylogenetic analysis indicates a closer relationship with catalytic domains from Gram-positive bacteria than the other fibrolytic eukaryotes from the rumen, the anaerobic fungi. (C) 1999 Published by Elsevier Science B.V. All rights reserved.",

keywords = "rumen, protozoa, xylanase, polyplastron multivesiculatum, cellulolytic bacteria, fungi, gene, populations, cellulases, digestion, protein, domains, enzymes, sheep",

author = "E Devillard and Newbold, {C J} and Scott, {K P} and E Forano and Wallace, {R J} and Jouany, {J P} and Flint, {H J}",

year = "1999",

month = dec,

day = "1",

doi = "10.1111/j.1574-6968.1999.tb08837.x",

language = "English",

volume = "181",

pages = "145--152",

journal = "FEMS Microbiology Letters",

issn = "0378-1097",

publisher = "Oxford University Press",

number = "1",

}

TY - JOUR

T1 - A xylanase produced by the rumen anaerobic protozoan Polyplastron multivesiculatum shows close sequence similarity to family 11 xylanases from Gram-positive bacteria

AU - Devillard, E

AU - Newbold, C J

AU - Scott, K P

AU - Forano, E

AU - Wallace, R J

AU - Jouany, J P

AU - Flint, H J

PY - 1999/12/1

Y1 - 1999/12/1

N2 - We report for the first time the cloning and characterisation of a protozoal enzyme involved in plant cell wall polysaccharide degradation. A cDNA library was constructed from the ruminal protozoan Polyplastron multivesiculatum and a stable clone expressing xylanase activity was isolated. The encoded enzyme belongs to the glycoside hydrolase family 11, and phylogenetic analysis indicates a closer relationship with catalytic domains from Gram-positive bacteria than the other fibrolytic eukaryotes from the rumen, the anaerobic fungi. (C) 1999 Published by Elsevier Science B.V. All rights reserved.

AB - We report for the first time the cloning and characterisation of a protozoal enzyme involved in plant cell wall polysaccharide degradation. A cDNA library was constructed from the ruminal protozoan Polyplastron multivesiculatum and a stable clone expressing xylanase activity was isolated. The encoded enzyme belongs to the glycoside hydrolase family 11, and phylogenetic analysis indicates a closer relationship with catalytic domains from Gram-positive bacteria than the other fibrolytic eukaryotes from the rumen, the anaerobic fungi. (C) 1999 Published by Elsevier Science B.V. All rights reserved.

KW - rumen

KW - protozoa

KW - xylanase

KW - polyplastron multivesiculatum

KW - cellulolytic bacteria

KW - fungi

KW - gene

KW - populations

KW - cellulases

KW - digestion

KW - protein

KW - domains

KW - enzymes

KW - sheep

U2 - 10.1111/j.1574-6968.1999.tb08837.x

DO - 10.1111/j.1574-6968.1999.tb08837.x

M3 - Article

VL - 181

SP - 145

EP - 152

JO - FEMS Microbiology Letters

JF - FEMS Microbiology Letters

SN - 0378-1097

IS - 1

ER -

A xylanase produced by the rumen anaerobic protozoan Polyplastron multivesiculatum shows close sequence similarity to family 11 xylanases from Gram-positive bacteria

Abstract

Keywords

Access to Document

Fingerprint

Cite this