Influence of lignin peroxidase concentration and localisation in lignin biodegradation by Phanerochaete chrysosporium

Kurek, Bernard; Odier, Etiiene

doi:10.1007/bf00166793

Cited by 15 publications

(6 citation statements)

References 32 publications

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“…The addition of LiP in the presence or absence of veratryl alcohol to cultures of C. subvermispora did not significantly increase the rate of mineralization of the DHP. In experiments using reconstituted cultures of P. chrysosporium, Kurek and Odier (21) observed that the lignin mineralization rates increased with LiP concentrations up to 20 nkat/ml. At higher concentrations of the enzyme, the rate of mineraliza-tion decreased.…”

Section: Discussionmentioning

confidence: 98%

Extracellular Enzyme Production and Synthetic Lignin Mineralization by Ceriporiopsis subvermispora

Rüttimann-Johnson

Salas

Vicuña

et al. 1993

Appl Environ Microbiol

100

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The ability of the white rot fungus Ceriporiopsis subvermispora to mineralize 14C-synthetic lignin was studied under different culture conditions, and the levels of two extracellular enzymes were monitored. The highest mineralization rates (28% after 28 days) were obtained in cultures containing a growth-limiting amount of nitrogen source (1.0 mM ammonium tartrate); under this condition, the levels of manganese peroxidase (MnP) and laccase present in the culture supernatant solutions were very low compared with cultures containing 10 mM of the nitrogen source. In contrast, cultures containing a limiting concentration of the carbon source (0.1% glucose) showed low levels of both enzymes and also very low mineralization rates compared with cultures containing 1% glucose. Cultures containing 11 ppm of Mn(II) showed a higher rate of mineralization than those containing 0.3 or 40 ppm of this cation. Levels of MnP and laccase were higher when 40 ppm of Mn(II) was used. Mineralization rates were slightly higher in cultures flushed daily with oxygen, whereas laccase levels were lower and MnP levels were approximately the same as in cultures maintained under an air atmosphere. The presence of 0.4 mM veratryl alcohol reduced both mineralization rates and MnP levels, without affecting laccase levels. Lignin peroxidase activity was not detected under any condition. Addition of purified lignin peroxidase to the cultures in the presence or absence of veratryl alcohol did not enhance mineralization rates significantly. White rot fungi degrade lignin by the action of enzymes that are secreted into the medium. Two extracellular peroxidases, lignin peroxidase (LiP) (15, 30) and manganese peroxidase (MnP) (14, 25), and a copper-containing phenol oxidase (laccase) (6) have been widely studied, and evidence that they participate in lignin depolymerization has accumulated. Laccase and MnP are probably more widely distributed among white rot fungi than is LiP. Phanerochaete

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Section: Discussionmentioning

confidence: 98%

Extracellular Enzyme Production and Synthetic Lignin Mineralization by Ceriporiopsis subvermispora

Rüttimann-Johnson

Salas

Vicuña

et al. 1993

Appl Environ Microbiol

100

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“…The increased ability of the fungus to achieve lignin oxidation using a low molecular weight, freely diffusible oxidant such as the veratryl alcohol cation radical gives this theory merit. Chemicals that have been found to be indirectly oxidized by this LiP-dependent process include lignin [42], the herbicide 3-amino 1,2,4-triazole [43), and various organic acids [37,38).…”

Section: Pollutant Oxidation Mechanismsmentioning

confidence: 99%

Mechanisms white rot fungi use to degrade pollutants

Barr¹,

Aust²

1994

Environ. Sci. Technol.

219

182

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“…The significance of these peroxidases in lignin biodegradation is well documented. The decomposition of lignin by ligninolytic cultures has been correlated to the appearance and level of the extracellular enzymes (10,27). Mutants with low peroxidase activity also exhibit lowered total ligninolytic activity (17).…”

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confidence: 99%

Heterogeneity and regulation of manganese peroxidases from Phanerochaete chrysosporium

Pease

Tien

1992

J Bacteriol

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Lignin and Mn peroxidases are two families of isozymes produced by the lignin-degrading fungus Phanerochaete chrysosporium under nutrient nitrogen or carbon limitation. We purified to homogeneity the three major Mn peroxidase isozymes, H3 (pI = 4.9), H4 (pI = 4.5), and H5 (pI = 4.2). Amino-terminal sequencing of these isozymes demonstrates that they are encoded by different genes. We also analyzed the regulation of these isozymes in carbon- and nitrogen-limited cultures and found not only that the lignin and Mn peroxidases are differentially regulated but also that differential regulation occurs within the Mn peroxidase isozyme family. The isozyme profile and the time at which each isozyme appears in secondary metabolism differ in both nitrogen- and carbon-limited cultures. Each isozyme also responded differently to the addition of a putative inducer, divalent Mn. The stability of the Mn peroxidases in carbon- and nitrogen-limited cultures was also characterized after cycloheximide addition. The Mn peroxidases are more stable in carbon-limited cultures than in nitrogen-limited cultures. They are also more stable than the lignin peroxidases. These data collectively suggest that the Mn peroxidase isozymes serve different functions in lignin biodegradation.

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Influence of lignin peroxidase concentration and localisation in lignin biodegradation by Phanerochaete chrysosporium

Cited by 15 publications

References 32 publications

Extracellular Enzyme Production and Synthetic Lignin Mineralization by Ceriporiopsis subvermispora

Extracellular Enzyme Production and Synthetic Lignin Mineralization by Ceriporiopsis subvermispora

Mechanisms white rot fungi use to degrade pollutants

Heterogeneity and regulation of manganese peroxidases from Phanerochaete chrysosporium

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