Metabolism of phenanthrene by Phanerochaete chrysosporium.

Lipid Peroxidation by the Manganese Peroxidase of Phanerochaete chrysosporium Is the Basis for Phenanthrene Oxidation

The manganese peroxidase (MnP) of Phanerochaete chrysosporium supported Mn(II)-dependent, H202independent lipid peroxidation, as shown by two findings: linolenic acid was peroxidized to give products that reacted with thiobarbituric acid, and linoleic acid was peroxidized to give hexanal. MnP also supported the slow oxidation of phenanthrene to 2,2'-diphenic acid in a reaction that required Mn(...

Lipid Peroxidation by the Manganese Peroxidase of Phanerochaete chrysosporium Is the Basis for Phenanthrene Oxidation by the Intact Fungus.

The manganese peroxidase (MnP) of Phanerochaete chrysosporium supported Mn(II)-dependent, H(2)O(2)-independent lipid peroxidation, as shown by two findings: linolenic acid was peroxidized to give products that reacted with thiobarbituric acid, and linoleic acid was peroxidized to give hexanal. MnP also supported the slow oxidation of phenanthrene to 2,2'-diphenic acid in a reaction that require...

Biodegradation of polycyclic aromatic hydrocarbons by white rot fungi Phanerochaete chrysosporium in sterile and unsterile soil

Ligninolytic white rot fungus, Phanerochaete chrysosporium, isolated from soil sample of petroleum refinery, was used for degradation of five polycyclic aromatic hydrocarbons (PAHs: acenaphthene, anthracene, phenanthrene, fluoranthene and pyrene), simultaneously and individually in sterile and unsterile soil. For maximum biodegradation, after 42 days of incubation, optimum conditions were pH 7....

Phenanthrene Removal from Soil by a Strain of Aspergillus niger Producing Manganese Peroxidase of Phanerochaete chrysosporium

Polycyclic aromatic hydrocarbon-degrading capabilities of Phanerochaete laevis HHB-1625 and its extracellular ligninolytic enzymes.

The ability of Phanerochaete laevis HHB-1625 to transform polycyclic aromatic hydrocarbons (PAHs) in liquid culture was studied in relation to its complement of extracellular ligninolytic enzymes. In nitrogen-limited liquid medium, P. laevis produced high levels of manganese peroxidase (MnP). MnP activity was strongly regulated by the amount of Mn2+ in the culture medium, as has been previously...