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Title: Manganese Peroxidases of the White Rot Fungus Phanerochaete sordida

Source: APPLIED AND ENVIROMENTAL MICROBIOLOGY, Feb 1994, Vol. 60, No. 2, p. 599-605; 1994


Publication Year: 1994  View PDF »

Category: Journal Articles

Abstract: The ligninolytic enzymes produced by the white rot fungus Phanerochaete sordida in liquid culture were studied. Only manganese peroxidase (MnP) activity could be detected in the supernatant liquid of the cultures. Lignin peroxidase (LiP) and laccase activities were not detected under a variety of different culture conditions. The highest MnP activity levels were obtained in nitrogen-limited cultures grown under an oxygen atmosphere. The enzyme was induced by Mn(II). The initial pH of the culture medium did not significantly affect the MnP production. Three MnP isozymes were identified (MnPI, MnPII, and MnPIII) and purified to homogeneity by anion-exchange chromatography followed by hydrophobic chromatography. The isozymes are glycoproteins with approximately the same molecular mass (around 45 kDa) but have different pIs. The pIs are 5.3, 4.2, and 3.3 for MnPI, MnPII, and MnPIII, respectively. The three isozymes are active in the same range of pHs (pHs 3.0 to 6.0) and have optimal pHs between 4.5 and 5.0. Their amino-terminal sequences, although highly similar, were distinct, suggesting that each is the product of a separate gene.

Keywords: Manganese Peroxidases, White rot fungus, Phanerochaete sordida

File size: 1,555 kb(s)

Date posted: 05/17/2010
Current FPL Scientist associated with this product
Cullen, Daniel
Research Microbiologist

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