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

46 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.

Original languageEnglish
Pages (from-to)145-52
Number of pages8
JournalFEMS Microbiology Letters
Volume181
Issue number1
DOIs
Publication statusPrint publication - 1 Dec 1999
Externally publishedYes

Keywords

  • Amino Acid Sequence
  • Anaerobiosis
  • Animals
  • Base Sequence
  • Ciliophora/enzymology
  • DNA, Complementary/genetics
  • Electrophoresis, Polyacrylamide Gel
  • Glucans/metabolism
  • Gram-Positive Bacteria/enzymology
  • Immunoblotting
  • Molecular Sequence Data
  • Phylogeny
  • Rumen/parasitology
  • Sequence Analysis, DNA
  • Xylan Endo-1,3-beta-Xylosidase
  • Xylans/metabolism
  • Xylosidases/chemistry

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