Ubiquity of lignin-degrading peroxidases among various wood-degrading fungi.
Phanerochaete chrysosporium is rapidly becoming a model system for the study of lignin biodegradation. Numerous studies on the physiology, biochemistry, chemistry, and genetics of this system have been performed. However, P. chrysosporium is not the only fungus to have a lignin-degrading enzyme system. Many other ligninolytic species of fungi, as well as other distantly related organisms which are known to produce lignin peroxidases, are described in this paper. In this study, we demonstrated the presence of the peroxidative enzymes in nine species not previously investigated. The fungi studied produced significant manganese peroxidase activity when they were grown on an oak sawdust substrate supplemented with wheat bran, millet, and sucrose. Many of the fungi also exhibited laccase and/or glyoxal oxidase activity. Inhibitors present in the medium prevented measurement of lignin peroxidase activity. However, Western blots (immunoblots) revealed that several of the fungi produced lignin peroxidase proteins. We concluded from this work that lignin-degrading peroxidases are present in nearly all ligninolytic fungi, but may be expressed differentially in different species. Substantial variability exists in the levels and types of ligninolytic enzymes produced by different white not fungi.
Orth
A B
AB
Department of Molecular and Cell Biology, Pennsylvania State University, University Park 16802.
Royse
D J
DJ
Tien
M
M
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D005658:Fungi / Q000201:enzymology*; D042845:Laccase; D008031:Lignin / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D013045:Species Specificity
D008031:Lignin; D010088:Oxidoreductases; D000429:Alcohol Oxidoreductases; C052371:glyoxal oxidase; D042845:Laccase; D010544:Peroxidases; C051129:manganese peroxidase