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Applied and Environmental Microbiology, August 2004, p. 4575-4581, Vol. 70, No. 8
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.8.4575-4581.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Novel Haloperoxidase from the Agaric Basidiomycete Agrocybe aegerita Oxidizes Aryl Alcohols and Aldehydes

René Ullrich,1,2* Jörg Nüske,1 Katrin Scheibner,3 Jörg Spantzel,4 and Martin Hofrichter2

Institute of Microbiology, Friedrich Schiller University of Jena,1 Department of Biotechnology, University of Applied Sciences of Jena, D-07743 Jena,4 Unit of Environmental Biotechnology, International Graduate School of Zittau, D-02763 Zittau,2 JenaBios GmbH, D-07749 Jena, Germany3

Received 6 January 2004/ Accepted 14 April 2004

Agrocybe aegerita, a bark mulch- and wood-colonizing basidiomycete, was found to produce a peroxidase (AaP) that oxidizes aryl alcohols, such as veratryl and benzyl alcohols, into the corresponding aldehydes and then into benzoic acids. The enzyme also catalyzed the oxidation of typical peroxidase substrates, such as 2,6-dimethoxyphenol (DMP) or 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonate) (ABTS). A. aegerita peroxidase production depended on the concentration of organic nitrogen in the medium, and highest enzyme levels were detected in the presence of soybean meal. Two fractions of the enzyme, AaP I and AaP II, which had identical molecular masses (46 kDa) and isoelectric points of 4.6 to 5.4 and 4.9 to 5.6, respectively (corresponding to six different isoforms), were identified after several steps of purification, including anion- and cation-exchange chromatography. The optimum pH for the oxidation of aryl alcohols was found to be around 7, and the enzyme required relatively high concentrations of H2O2 (2 mM) for optimum activity. The apparent Km values for ABTS, DMP, benzyl alcohol, veratryl alcohol, and H2O2 were 37, 298, 1,001, 2,367 and 1,313 µM, respectively. The N-terminal amino acid sequences of the main AaP II spots blotted after two-dimensional gel electrophoresis were almost identical and exhibited almost no homology to the sequences of other peroxidases from basidiomycetes, but they shared the first three amino acids, as well as two additional amino acids, with the heme chloroperoxidase (CPO) from the ascomycete Caldariomyces fumago. This finding is consistent with the fact that AaP halogenates monochlorodimedone, the specific substrate of CPO. The existence of haloperoxidases in basidiomycetous fungi may be of general significance for the natural formation of chlorinated organic compounds in forest soils.

* Corresponding author. Mailing address: Unit of Environmental Biotechnology, International Graduate School of Zittau, Markt 23, D-02763 Zittau, Germany. Phone: 49 3583 771521. Fax: 49 3583 771534. E-mail: ullrich{at}ihi-zittau.de.

Applied and Environmental Microbiology, August 2004, p. 4575-4581, Vol. 70, No. 8
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.8.4575-4581.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Anh, D. H., Ullrich, R., Benndorf, D., Svatos, A., Muck, A., Hofrichter, M. (2007). The Coprophilous Mushroom Coprinus radians Secretes a Haloperoxidase That Catalyzes Aromatic Peroxygenation. Appl. Environ. Microbiol. 73: 5477-5485 [Abstract] [Full Text]  


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