Applied Microbiology and Biotechnology

, Volume 48, Issue 5, pp 602–605 | Cite as

Purification of the main manganese peroxidase isoenzyme MnP2 from the white-rot fungus Nematoloma frowardii b19

  • I. Schneegaß
  • M. Hofrichter
  • K. Scheibner
  • W. Fritsche
SHORT CONTRIBUTION

Abstract

The main manganese peroxidase isoenzyme MnP2 of the South American white-rot fungus Nematoloma frowardii b19 was purified to homogeneity using anion-exchange chromatography (Mono Q) and preparative isoelectric focusing. The purified enzyme has a molecular mass of 44 kDa and a pI of 3.2.

Keywords

Enzyme Chromatography Purification Manganese Molecular Mass 
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 Berlin Heidelberg 1997

Authors and Affiliations

  • I. Schneegaß
    • 1
  • M. Hofrichter
    • 1
  • K. Scheibner
    • 1
  • W. Fritsche
    • 1
  1. 1.Friedrich Schiller Universität of Jena, Institut für Mikrobiologie, Lehrstuhl Technische Mikrobiologie, Philosophenweg 12, D-07743 Jena, GermanyDE

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