Ceriporiopsis subvermispora is a white-rot basidiomycete that has ligninolytic activity. Lignin, along with cellulose, is a major polymeric component of wood that is rather refractory to biodegradation. It is degraded efficiently by only a small group of fungi. There are three main ligninolytic enzymes: manganese peroxidase, lignin peroxidase and lacasse. Ceriporiopsis subvermispora produces isoenzymes of manganese peroxidase and lacasse, but no isoenzymes of lignin peroxidase have been found. However, its ligninolytic activity is as high as in organisms possessing lignin peroxidase. Many groups around the world have studied C. subvermispora and other white-rot fungi for uses in biological ligninolysis in the pulp and paper industry.
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Mycelial mats of C. subvermispora grown in a basal medium. Mycelial mats and pellets of C. subvermispora
This organism produces oxalate oxidase, which catalyses the degradation of oxalate to carbon dioxide and hydrogen peroxide. This enzyme is secreted and could provide hydrogen peroxide for manganese peroxidase, which oxidises extracellular Mn(II) to Mn(III) providing a diffusible oxidant that can degrade lignin. The fungal oxalate oxidase is being studied by the group of Stephen Bornemann. For example, we have discovered two allelic isoforms of this enzyme. The unexpectedly high sequence identity between these isoforms and oxalate decarboxylases has provided important information about which amino acids define their reaction specificities.
