Purification and Characterization of Cellobiose Dehydrogenases from the White Rot Fungus Trametes versicolor.

Applied and Environmental Microbiology
B P RoyF S Archibald

Abstract

The white rot fungus Trametes versicolor degrades lignocellulosic material at least in part by oxidizing the lignin via a number of secreted oxidative and peroxidative enzymes. An extracellular reductive enzyme, cellobiose dehydrogenase (CDH), oxidizes cellobiose and reduces insoluble Mn(IV)O(inf2), commonly found as dark deposits in decaying wood, to form Mn(III), a powerful lignin-oxidizing agent. CDH also reduces ortho-quinones and produces sugar acids which can promote manganese peroxidase and therefore ligninolytic activity. To better understand the role of CDH in lignin degradation, proteins exhibiting cellobiose-dependent quinone-reducing activity were isolated and purified from cultures of T. versicolor. Two distinct proteins were isolated; the proteins had apparent molecular weights of 97,000 and 81,000 and isoelectric points of 4.2 and 6.4, respectively. The larger CDH (CDH 4.2) contained both flavin and heme cofactors, whereas the smaller contained only a flavin (CDH 6.4). These CDH enzymes were rapidly reduced by cellobiose and lactose and somewhat more slowly by cellulose and certain cello-oligosaccharides. Both glycoproteins were able to reduce a very wide range of quinones and organic radical species but differed...Continue Reading

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Citations

Oct 12, 2004·FEBS Letters·Laura-Leena KiiskinenKristiina Kruus
Jan 19, 2013·Analytical and Bioanalytical Chemistry·Roland LudwigLo Gorton
May 25, 2015·Applied Biochemistry and Biotechnology·Justyna SulejJerzy Rogalski
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