Purification and mode of action of an alkali-resistant endo-1, 4-beta-glucanase from Bacillus pumilus.

@article{Christakopoulos1999PurificationAM,
  title={Purification and mode of action of an alkali-resistant endo-1, 4-beta-glucanase from Bacillus pumilus.},
  author={Paul Christakopoulos and Dimitris G. Hatzinikolaou and George Fountoukidis and Dimitris Kekos and Marc Claeyssens and Basil J. Macris},
  journal={Archives of biochemistry and biophysics},
  year={1999},
  volume={364 1},
  pages={61-6}
}
Alkaline endo-1,4-beta-d-glucanase was secreted by Bacillus pumilus grown in submerged culture on a combination of oat spelt xylan and corn starch as carbon sources. The enzyme was purified to homogeneity by Sephacryl S-200 and Q-Sepharose column chromatography. The protein corresponded to molecular mass and pI values of 67 kDa and 3.7, respectively. The enzyme was optimally active at pH 7.0-8.0 and 60 degrees C and retained 50% of its optimum activity at pH 12. The most notable characteristic… CONTINUE READING

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