Properties of ligninase from Phanerochaete chrysosporium and their possible applications.
The wood-degrading fungus Phanerochaete chrysosporium Burds produces a family of enzymes which degrade lignin and lignin-like substrates. These ligninases exhibit a high degree of homology in being hemeprotein peroxidases, in Mr, in cross reactivity to polyclonal antibodies, in being glycosylated, and in catalytic properties. The predominant ligninase is able to generate cation radicals in its aromatic substrates. These radicals can undergo a variety of reactions thus explaining the nonspecific nature of the enzyme. A similar mechanism is suggested for the other isoenzymes. There are numerous potential applications for ligninases. These include: biopulping, waste treatment of byproduct lignins, detoxification of environmental pollutants, and modification of lignins to produce small molecular weight organics.
Tien
M
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Department of Molecular and Cell Biology, Pennsylvania State University, University Park.
D001487:Basidiomycota / Q000201:enzymology*; D001673:Biodegradation, Environmental; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D007527:Isoenzymes / Q000378:metabolism; D007700:Kinetics; D008031:Lignin / Q000378:metabolism*; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000037:antagonists & inhibitors / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*
D007527:Isoenzymes; D008031:Lignin; D010105:Oxygenases; C044391:ligninase