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

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 journal › Article › peer-review

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 language	English (US)
Pages (from-to)	171-179
Number of pages	9
Journal	Journal of Biochemistry, Molecular Biology and Biophysics
Volume	1
Issue number	3
State	Published - Jun 10 1998
Externally published	Yes

Keywords

Chainia sp.
Mode of action
Purification
Xylanase

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Genetics

Cite this

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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.",

keywords = "Chainia sp., Mode of action, Purification, Xylanase",

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AU - Hegde, S. S.

AU - Kumar, A. R.

AU - Suresh, C. G.

AU - Kotwal, S. M.

AU - Ganesh, K. N.

AU - Khan, M. I.

PY - 1998/6/10

Y1 - 1998/6/10

N2 - 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.

AB - 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.

KW - Chainia sp.

KW - Mode of action

KW - Purification

KW - Xylanase

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

Abstract

Keywords

ASJC Scopus subject areas

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