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

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 encode...

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Published in:FEMS microbiology letters 1999-12, Vol.181 (1), p.145-152
Main Authors: Devillard, Estelle, Newbold, C.James, Scott, Karen P., Forano, Evelyne, Wallace, R.John, Jouany, Jean-Pierre, Flint, Harry J.
Format: Article
Language:English
Subjects:
glycoside hydrolase
Polyplastron multivesiculatum
polysaccharides
Protozoa
Rumen
Xylanase
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container_issue 1
container_start_page 145
container_title FEMS microbiology letters
container_volume 181
creator Devillard, Estelle
Newbold, C.James
Scott, Karen P.
Forano, Evelyne
Wallace, R.John
Jouany, Jean-Pierre
Flint, Harry J.
description 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.
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subjects glycoside hydrolase
Polyplastron multivesiculatum
polysaccharides
Protozoa
Rumen
Xylanase
title A xylanase produced by the rumen anaerobic protozoan Polyplastron multivesiculatum shows close sequence similarity to family 11 xylanases from Gram-positive bacteria
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