Purification and characterization of an acetyl xylan esterase produced by Streptomyces lividans.

@article{Dupont1996PurificationAC,
  title={Purification and characterization of an acetyl xylan esterase produced by Streptomyces lividans.},
  author={Claude Dupont and Nicole Daigneault and François Shareck and Rolf Morosoli and Dieter Kluepfel},
  journal={The Biochemical journal},
  year={1996},
  volume={319 ( Pt 3)},
  pages={881-6}
}
The acetyl xylan esterase cloned homologously from Streptomyces lividans [Shareck, Biely, Morosoli and Kluepfel (1995) Gene 153, 105-109] was purified from culture filtrate of the overproducing strain S. lividans IAF43. The secreted enzyme had a molecular mass of 34 kDa and a pI of 9.0. Under the assay conditions with chemically acetylated birchwood xylan the kinetic constants of the enzyme were: specific activity, 715 units/mg, Km 7.94 mg/ml and Vmax 1977 units/mg. Optimal enzyme activity was… CONTINUE READING

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