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

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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.

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Authors and Affiliations

  1. Friedrich Schiller Universität of Jena, Institut für Mikrobiologie, Lehrstuhl Technische Mikrobiologie, Philosophenweg 12, D-07743 Jena, Germany, , , , , , DE

    I. Schneegaß, M. Hofrichter, K. Scheibner & W. Fritsche

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  1. I. Schneegaß
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  2. M. Hofrichter
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  3. K. Scheibner
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  4. W. Fritsche
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Received: 23 May 1997 / Received revision: 1 July 1997 / Accepted: 4 July 1997

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Schneegaß, I., Hofrichter, M., Scheibner, K. et al. Purification of the main manganese peroxidase isoenzyme MnP2 from the white-rot fungus Nematoloma frowardii b19. Appl Microbiol Biotechnol 48, 602–605 (1997). https://doi.org/10.1007/s002530051102

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  • DOI: https://doi.org/10.1007/s002530051102

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