Open AccessA xylanase produced by the rumen anaerobic protozoan Polyplastron multivesiculatum shows close sequence similarity to family 11 xylanases from Gram‐positive bacteria
Author(s) -
Devillard Estelle,
Newbold C.James,
Scott Karen P.,
Forano Evelyne,
Wallace R.John,
Jouany JeanPierre,
Flint Harry J.
Publication year - 1999
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1999.tb08837.x
Subject(s) - xylanase , glycoside hydrolase , bacteria , biology , rumen , cloning (programming) , microbiology and biotechnology , enzyme , biochemistry , complementary dna , structural similarity , anaerobic bacteria , genetics , gene , fermentation , computer science , programming language
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.