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

Research output: Contribution to journalArticle

41 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 languageEnglish
Pages (from-to)145-152
Number of pages8
JournalFEMS Microbiology Letters
Volume181
Issue number1
DOIs
Publication statusPublished - 1 Dec 1999

Keywords

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

Cite this

A xylanase produced by the rumen anaerobic protozoan Polyplastron multivesiculatum shows close sequence similarity to family 11 xylanases from Gram-positive bacteria. / Devillard, E ; Newbold, C J ; Scott, K P ; Forano, E ; Wallace, R J; Jouany, J P ; Flint, H J.

In: FEMS Microbiology Letters, Vol. 181, No. 1, 01.12.1999, p. 145-152.

Research output: Contribution to journalArticle

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