Purification and characterisation of a major xylanase with cellulase and transferase activities from Fusarium oxysporum.

@article{Christakopoulos1996PurificationAC,
  title={Purification and characterisation of a major xylanase with cellulase and transferase activities from Fusarium oxysporum.},
  author={Paul Christakopoulos and Dimitris Kekos and Basil J. Macris and Marc Claeyssens and Mahalingeshwara K. Bhat},
  journal={Carbohydrate research},
  year={1996},
  volume={289},
  pages={91-104}
}
A major xylanase from Fusarium oxysporum was purified to homogeneity by gel filtration, affinity, and ion-exchange chromatographies. It has a molecular mass of 60.2 kDa and pI of 6.6 and was optimally active at pH 7.4 and at 50 degrees C. The enzyme was stable over the pH range 5.8-8.2 at 40 degrees C for 24 h and lost 45% of its original activity at pH 9.0 under the identical conditions. The enzyme rapidly hydrolysed xylans from oat spelts (husks) and birchwood, but the activities on… CONTINUE READING
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