Purification and characterization of an extracellular endo-xylanase from an actinomycete Chainia sp.

S. S. Hegde, A. R. Kumar, C. G. Suresh, S. M. Kotwal, K. N. Ganesh, M. I. Khan

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

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 languageEnglish (US)
Pages (from-to)171-179
Number of pages9
JournalJournal of Biochemistry, Molecular Biology and Biophysics
Volume1
Issue number3
StatePublished - Jun 10 1998
Externally publishedYes

Keywords

  • Chainia sp.
  • Mode of action
  • Purification
  • Xylanase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Genetics

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