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Applied and Environmental Microbiology, August 2003, p. 5015-5018, Vol. 69, No. 8
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.8.5015-5018.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Chlorination and Cleavage of Lignin Structures by Fungal Chloroperoxidases

Patricia Ortiz-Bermúdez,1 Ewald Srebotnik,2 and Kenneth E. Hammel1,3*

Department of Bacteriology, University of Wisconsin, Madison, Wisconsin 53706,1 Institut für Verfahrenstechnik, Umwelttechnik, und Technische Biowissenschaften, Technische Universität Wien, A-1060 Vienna, Austria,2 Institute for Microbial and Biochemical Technology, USDA Forest Products Laboratory, Madison, Wisconsin 537263

Received 20 February 2003/ Accepted 2 May 2003

Two fungal chloroperoxidases (CPOs), the heme enzyme from Caldariomyces fumago and the vanadium enzyme from Curvularia inaequalis, chlorinated 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane, a dimeric model compound that represents the major nonphenolic structure in lignin. Both enzymes also cleaved this dimer to give 1-chloro-4-ethoxy-3-methoxybenzene and 1,2-dichloro-4-ethoxy-5-methoxybenzene, and they depolymerized a synthetic guaiacyl lignin. Since fungal CPOs occur in soils and the fungi that produce them are common inhabitants of plant debris, CPOs may have roles in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown.


* Corresponding author. Mailing address: Institute for Microbial and Biochemical Technology, USDA Forest Products Laboratory, One Gifford Pinchot Dr., Madison, WI 53726. Phone: (608) 231-9528. Fax: (608) 231-9262. E-mail: kehammel{at}wisc.edu.


Applied and Environmental Microbiology, August 2003, p. 5015-5018, Vol. 69, No. 8
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.8.5015-5018.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.




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