An extracellular cellulase-free endo 1,4-β-D-xylanase from an actinomycete Chainia sp. has been purified to homogeneity by ammonium sulfate precipitation, successive chromatography on CM Sephadex C50 and Sephadex G50 followed by FPLC (M molecular mass of the enzyme indicates a single species with a mass of 21 000 and 21 485, as determined by SDS-PAGE and Laser Desorption Mass Spectroscopy, respectively. The purified xylanase is a non- glycosylated protein with pl of 9.4-9.5. The enzyme is low in basic, aromatic and sulfur containing amino acids and the partial N-terminal sequence exhibits remarkable homology with other actinomycete xylanases.
|Original language||English (US)|
|Number of pages||9|
|Journal||Journal of Biochemistry, Molecular Biology and Biophysics|
|State||Published - Jun 10 1998|
- Chainia sp.
- Mode of action
ASJC Scopus subject areas
- Molecular Biology