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Purification and biochemical characterization of an endoxylanase from Aspergillus versicolor

Purification and biochemical characterization of an endoxylanase from Aspergillus versicolor AbstractAn endoxylanase (β-1,4-xylan xylanohydrolase, EC 3.2.1.8) was purified from the culture filtrate of a strain of Aspergillus versicolor grown on oat wheat. The enzyme was purified to homogeneity by chromatography on DEAE-cellulose and Sephadex G-75. The purified enzyme was a monomer of molecular mass estimated to be 19 kDa by SDS-PAGE and gel filtration. The enzyme was glycoprotein with 71% carbohydrate content and exhibited a pI of 5.4. The purified xylanase was specific for xylan hydrolysis. The enzyme had a Km of 6.5 mg ml?1 and a Vmax of 1440 U (mg protein)?1. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png FEMS Microbiology Letters Oxford University Press

Purification and biochemical characterization of an endoxylanase from Aspergillus versicolor

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References (11)

Publisher
Oxford University Press
Copyright
© 1998 Federation of European Microbiological Societies.
ISSN
0378-1097
eISSN
1574-6968
DOI
10.1111/j.1574-6968.1998.tb13906.x
Publisher site
See Article on Publisher Site

Abstract

AbstractAn endoxylanase (β-1,4-xylan xylanohydrolase, EC 3.2.1.8) was purified from the culture filtrate of a strain of Aspergillus versicolor grown on oat wheat. The enzyme was purified to homogeneity by chromatography on DEAE-cellulose and Sephadex G-75. The purified enzyme was a monomer of molecular mass estimated to be 19 kDa by SDS-PAGE and gel filtration. The enzyme was glycoprotein with 71% carbohydrate content and exhibited a pI of 5.4. The purified xylanase was specific for xylan hydrolysis. The enzyme had a Km of 6.5 mg ml?1 and a Vmax of 1440 U (mg protein)?1.

Journal

FEMS Microbiology Letters – Oxford University Press

Published: Sep 17, 1998

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