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Applied and Environmental Microbiology, May 2009, p. 2750-2757, Vol. 75, No. 9
0099-2240/09/$08.00+0     doi:10.1128/AEM.02320-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Cellobiose Dehydrogenase from the Ligninolytic Basidiomycete Ceriporiopsis subvermispora{triangledown}

Wolfgang Harreither,1 Christoph Sygmund,1 Evelyn Dünhofen,1,{dagger} Rafael Vicuña,2 Dietmar Haltrich,1 and Roland Ludwig1,3*

Department of Food Sciences and Technology, Division of Food Biotechnology, BOKU University of Natural Resources and Applied Life Sciences, A-1190 Vienna, Austria,1 Departamento de Genética Molecular y Microbiología, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Casilla 114-D, and Instituto Milenio de Biologica Fundamental y Aplicada, Santiago, Chile,2 Research Centre Applied Biocatalysis, A-8010 Graz, Austria3

Received 9 October 2008/ Accepted 26 February 2009

Cellobiose dehydrogenase (CDH), an extracellular flavocytochrome produced by several wood-degrading fungi, was detected in cultures of the selective delignifier Ceriporiopsis subvermispora when grown on a cellulose- and yeast extract-based liquid medium. CDH amounted to up to 2.5% of total extracellular protein during latter phases of the cultivation and thus suggested an important function for the fungus under the given conditions. The enzyme was purified 44-fold to apparent homogeneity. It was found to be present in two glycoforms of 98 kDa and 87 kDa with carbohydrate contents of 16 and 4%, respectively. The isoelectric point of both glycoforms is around 3.0, differing by 0.1 units, which is the most acidic value so far reported for a CDH. By using degenerated primers of known CDH sequences, one cdh gene was found in the genomic DNA, cloned, and sequenced. Alignment of the 774-amino-acid protein sequence revealed a high similarity to CDH from other white rot fungi. One notable difference was found in the longer interdomain peptide linker, which might affect the interdomain electron transfer at higher temperatures. The preferred substrate of C. subvermispora CDH is cellobiose, while glucose conversion is strongly discriminated by a 155,000-fold-lower catalytic efficiency. This is a typical feature of a basidiomycete CDH, as are the acidic pH optima for all tested electron acceptors in the range from 2.5 to 4.5.

* Corresponding author. Mailing address: Department für Lebensmittelwissenschaften und Technologie, Universität für Bodenkultur, Muthgasse 18/2/71, A-1190 Vienna, Austria. Phone: 431 36006 6280. Fax: 431 36006 6251. E-mail: roland.ludwig{at}a-b.at

{triangledown} Published ahead of print on 6 March 2009.

{dagger} Present address: AGES PharmMed, A-1030 Vienna, Austria.

Applied and Environmental Microbiology, May 2009, p. 2750-2757, Vol. 75, No. 9
0099-2240/09/$08.00+0     doi:10.1128/AEM.02320-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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