Overproduction of lignin peroxidase by Phanerochaete chrysosporium (BKM-F-1767) under nonlimiting nutrient conditions

Article Abstract:

The synthesis and isoenzyme composition of the ligninolytic system under nonlimiting nutrient conditions in Phanerochaete chrysosporium BKM-F-1767 were characterized using a nonimmersed liquid culture system and conditions close to those occurring in nature. The response of P. chrysosporium to any kind of starvation conditions may be controlled by a broad regulatory mechanism, but the factors that trigger overproduction of the individual components of the ligninolytic system may differ.

Lignin

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Ligninolytic system formation by Phanerochaete chrysosporium in air

Article Abstract:

The formation of lignin peroxidase (LIP) and manganese peroxidase depends on the concentration of oxygen while the formation of glyoxal oxidase depends on the concentration of nitrogen when the fungus Phanerochaete is grown in a liquid culture. If the concentration of nitrogen is high and that of carbon is low, LIP is produced only if air is also present and polysaccharides are not formed. If the concentration of carbon is high, LIP is formed only if pure oxygen is present.

Wood-decaying fungi

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Lignin peroxidase isozymes from Phanerochaete chrysosporium can be enzymatically dephosphorylated

Article Abstract:

An enzymatic fraction with extracellular lignin peroxidase (LIP) from Phanerochaete chrysosporium was analyzed to determine its enzymatic profile during enzymatic dephosphorylation. Analyis of an enzymatic fraction with LIP dephosphorylating (LpD) activity indicated the presence of unchanged LIP catalytic properties during dephosphorylation. Furthermore, LIP dephosphorylation is characterized by LpD-mediated postranslational modification.

Analysis, Physiological aspects, Microbial enzymes, Peroxidase, Enzyme structure-activity relationships, Fungi, Pathogenic, Pathogenic fungi

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