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Roles of manganese and organic acid chelators in regulating lignin degradation and biosynthesis of peroxidases by Phanerochaete chrysosporium

Article Abstract:

Production of manganese polymerases (MnP) by Phanerochaete spp. is stimulated, lignin polymerases (LiP) are inhibited and depolymerization of high-molecular-weight lignin products occurs when manganese is present in ionic form in solution. Organic chelators stabilize the ionic Mn complexes, helping in the initial degradation reaction. Subsequent reoxidation of Mn by MnP results in the precipitation of Mn as MnO2 with the release of LiP inhibition, thus causing further degradation of the lignin and its mineralization. The MnO2 deposits produced by MnP help precipitate ionic Mn, thereby facilitating more efficient lignin degradation by LiP.

Author: Perez, Juana, Jeffries, Thomas W.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1992

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Bacteria are omnipresent on Phanerochaete chrysosporium Burdsall

Article Abstract:

Phanerochaete chrysosporium strains are always associated with bacteria that are not removed by treatment with antibiotics, heat or ozone. One of the bacteria is Agrobacterium radiobacter while two others are probably members of a taxon related to Burkholderia, and the Woese alpha group or the rRNA superfamily IV respectively. Bacterial growth is best on complex media and an acidic pH, and is inhibited at 4 degrees C and between 37-40 degrees C. No bacteria have been found associated with other white rot and brown rot fungi.

Author: Seigle-Murandi, F., Guiraud, P., Croize, J., Falsen, E., Eriksson, K.-E.L.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996

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Purification and partial characterization of a laccase from the white rot fungus Phanerochaete flavido-alba

Article Abstract:

The white rot fungus Phanerochaete flavido-alba excretes a laccase in addition to excreting a lignin-degrading peroxidases. The purification and analysis of this extracellular lignin-modifying enzyme give the molecular weight to be 94,000. The laccase has an isoelectric point lower than 3.55. The UV-visible spectrum of the protein is typical of copper-containing proteins. The purified laccase oxidizes dimethoxyphenol, guaiacol and syringaldazine.

Author: Perez, Juana, Martinez, Jose, Rubia, Teresa de la
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
Physiological aspects, Microbial enzymes

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Subjects list: Research, Bacteria, Wood-decaying fungi
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