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Activities of ligninolytic enzymes of the white rot fungus, phanerochaete chrysosporium and its recalcitrant substance degradability

Feng Wu, Hiroaki Ozaki, Yutaka Terashima, Toshihiro Imada, Yumiko Ohkouchi

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Abstract

The factors influencing the activities of extracellular ligninolytic enzymes synthesized by white rot fungus,Phanerochaete chrysosporium , were investigated by batch culture experiments. The LiP activity was maximal under the nitrogen-sufficient condition, compared with the activities under both conditions of the nitrogen-limited and nitrogen-excess. The manganese-dependent peroxidase (MnP) activity was highest under nitrogen-limited condition. Veratryl alcohol was found to be the most important substrate enhancing lignin peroxidase (LiP) activity in carbon-limited medium. The decolorization of azo dye (Reactive Red 22) by P. chrysosporium in the presence of both LiP and MnP under carbon-limited condition was greater than that in the presence of MnP under nitrogen-limited condition. Two chlorinated substances (2,6-DCP and MCPA) were degraded under conditions of nitrogen-limitation and notrogen-sufficiency. The azo dyes were also decolorized by the crude extracellular ligninolytic enzymes from P. chrysosporium.

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The factors influencing the activities of extracellular ligninolytic enzymes synthesized by white rot fungus,Phanerochaete chrysosporium , were investigated by batch culture experiments. The LiP activity was maximal under the nitrogen-sufficient condition, compared with the activities under both conditions of the nitrogen-limited and nitrogen-excess. The manganese-dependent peroxidase (MnP) activity was highest under nitrogen-limited condition. Veratryl alcohol was found to be the most important substrate enhancing lignin peroxidase (LiP) activity in carbon-limited medium. The decolorization of azo dye (Reactive Red 22) by P. chrysosporium in the presence of both LiP and MnP under carbon-limited condition was greater than that in the presence of MnP under nitrogen-limited condition. Two chlorinated substances (2,6-DCP and MCPA) were degraded under conditions of nitrogen-limitation and notrogen-sufficiency. The azo dyes were also decolorized by the crude extracellular ligninolytic enzymes from P. chrysosporium.

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Available abstract

The factors influencing the activities of extracellular ligninolytic enzymes synthesized by white rot fungus,Phanerochaete chrysosporium , were investigated by batch culture experiments. The LiP activity was maximal under the nitrogen-sufficient condition, compared with the activities under both conditions of the nitrogen-limited and nitrogen-excess. The manganese-dependent peroxidase (MnP) activity was highest under nitrogen-limited condition. Veratryl alcohol was found to be the most important substrate enhancing lignin peroxidase (LiP) activity in carbon-limited medium. The decolorization of azo dye (Reactive Red 22) by P. chrysosporium in the presence of both LiP and MnP under carbon-limited condition was greater than that in the presence of MnP under nitrogen-limited condition. Two chlorinated substances (2,6-DCP and MCPA) were degraded under conditions of nitrogen-limitation and notrogen-sufficiency. The azo dyes were also decolorized by the crude extracellular ligninolytic enzymes from P. chrysosporium.

Key concepts: Phanerochaete, Chrysosporium, Lignin peroxidase, Manganese peroxidase, Chemistry, Lignin, Food science, Biodegradation

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