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Applied Microbiology and Biotechnology

, Volume 28, Issue 6, pp 543–545 | Cite as

Purification of a novel enzyme involved in catechin degradation by Calvatia gigantea

  • M. Galiotou-Panayotou
  • P. Rodis
  • B. J. Macris
  • D. Stathakos
Biotechnology

Summary

A novel enzyme, involved in the degradation of catechin by Calvatia gigantea, was purified 114-fold over the crude extract yielding 24% purified enzyme with a specific activity 16.1 U/mg protein. Two isozymic forms (I and II) were isolated, both exhibiting the same kinetic characteristics with maximum activity at pH 8 and 35°C. SDS electrophoresis of I and II revealed the presence of two identical components in each form with molecular weights 50 500 and 49 500.

Keywords

Enzyme Molecular Weight Purification Electrophoresis Crude Extract 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag 1988

Authors and Affiliations

  • M. Galiotou-Panayotou
    • 1
  • P. Rodis
    • 1
  • B. J. Macris
    • 1
  • D. Stathakos
    • 1
  1. 1.Biology InstituteN.R.C. DemocritosAttikiGreece

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