In vitro depolymerization of lignin by manganese peroxidase of Phanerochaete chrysosporium

Wariishi, Hiroyuki; Valli, Khadar; Gold, Michael H.

doi:10.1016/0006-291x(91)90919-x

Cited by 319 publications

(209 citation statements)

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“…Upon nitrogen limitation, P. chrysosporium produces a large number of oxidative enzymes involved in lignin biodegradation (4)(5)(6). Along with these enzymes, the fungus produces organic acids as evidenced by the drop in pH and the strong buffering capacity of the extracellular fluid of fungal cultures.…”

Section: Resultsmentioning

confidence: 99%

“…Phanerochaete chrysosporium is a wood-destroying fungus of the white-rot type that has been extensively characterized for its lignin-degrading activity. Under conditions that trigger the synthesis of the ligninolytic system (2,3), it secretes a large number of hemoprotein peroxidases (EC 1.11.1.7), which catalyze the depolymerization of lignin (4)(5)(6). These peroxidases can be divided into two isozyme families based on the catalytic activities, the lignin peroxidases (4,5) and the Mn peroxidases (7,8).…”

mentioning

confidence: 99%

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Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation.

Kuan

Tien

1993

Proc. Natl. Acad. Sci. U.S.A.

164

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Oxalate is produced by numerous wooddegrading fungi. Our studies here show that the white-rot fungus Phanerochaete chrysosponum produces extracellular oxalate under conditions that induce synthesis of the ligninolytic system. Little or no oxalate was detected in cultures grown under high nutrient nitrogen or carbon. This extracellular oxalate was identified and quantitated by HPLC. Its identity was further substantiated by its decomposition by the enzyme oxalate oxidase. The oxalate content of the extracellular fluid (peaking at 60 ,M) paralleled the extracellular activity of the lignin-degrading enzyme, Mn peroxidase. Significantly, we demonstrated that oxalate, at physiological concentrations, substantially stimulated Mn peroxidase-catalyzed phenol red oxidation, presumably by its ability to chelate Mn. Stopped flow studies also indicate that oxalate accelerates the turnover of Mn peroxidase. Furthermore, we discovered that oxalate can support Mn peroxidase-catalyzed oxidations in the absence of exogenous H202 and in the presence of dioxygen. These results allow us to propose an important role for oxalate, a ubiquitous compound produced by wood-destroying fungi, in lignin biodegradation.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation.

Kuan

Tien

1993

Proc. Natl. Acad. Sci. U.S.A.

164

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“…It displayed a strong association between aromatic Cl org , Mn, and microscopically observed fungi. Mn-peroxidase enzymes in white-rot fungi often play a key role in lignin degradation (Wariishi et al, 1991;Orth et al, 1993). In addition, numerous strains of white-rot fungi have been associated with the production of aromatic Cl org (de Jong et al, 1992(de Jong et al, , 1994.…”

Section: Summary and Implications For The Formation Of Different CL Omentioning

confidence: 99%

X-ray spectromicroscopic investigation of natural organochlorine distribution in weathering plant material

Leri

Marcus

Myneni

2007

Geochimica et Cosmochimica Acta

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“…~~~y s o s p o r~u r n [6], MP has been considered to play a secondary role in ligniii degradation, compared with LP, due to its incapacity to oxidize non-phenolic lignin substrates. The increasing interest in this enzyme in recent years is due to a number of reasons: its production by most white-rot fungi [14, 151 including lignin-degrading species that lack L P [ 16,171 ; its capacity to depolymerize synthetic lignin in vitro [18] and to oxidize non-phenolic compounds via peroxidation of lipids [19] ; and its production during fungal degradation of lignocellulose [20,211, with chelated Mn3+ being a potential lignin-oxidizing mediator for extensive delignification of wood and other lignocellulosic materials [22,231. Recently, it has been reported that an LP isoenzyme from I?…”

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confidence: 99%

Purification and Catalytic Properties of Two Manganese Peroxidase Isoenzymes from Pleurotus eryngii

Martı́nez

Ruíz-Dueñas

Guillén

et al. 1996

European Journal of Biochemistry

343

244

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The ligninolytic basidiomycetes Pleurotus eryngii, Pleurotus ostreatus, Pleurotus pulmonarius and Pleurotus sajor-caju did not exhibit detectable levels of manganese peroxidase (MP) when grown in liquid media with ammonium tartrate as N source. However, after examination of cells grown on different organic N-based media, high M P activity was obtained in peptone medium, up to nearly 3 U/ml in cultures of I? eryngii. Moreover, Mnz+ supplementation was not used to produce MP, since all Mn2+ concentrations assayed (1 -4000 pM) inhibited production of this enzyme in liquid medium.Two MP isoenzymes were purified to homogeneity from shaken or stationary cultures of I? eryngii grown in peptone medium. The purification process (which included chromatography on Biorad Q-cartridge, Sephacryl S-200 and Mono-Q) attained 56% activity yield with a purification factor of 25. The isoenzymes differed in PI (3.75 and 3.65), N-terminal sequence and some catalytic properties. They were in some aspects (e.g., molecular mass of 43 kDa) similar to Phanerochaete chrysosporium MP but exhibited some distinct characteristics, including Mn"-independent peroxidase activities against 2,6-dimethoxyphenol and veratryl alcohol, and higher resistance to H,O,. Recent studies have shown that M P are ubiquitous enzymes in ligninolytic fungi, but the results obtained suggest that differences in catalytic properties probably exist between different Mn2 ' -oxidizing peroxidases produced by these fungi.

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In vitro depolymerization of lignin by manganese peroxidase of Phanerochaete chrysosporium

Cited by 319 publications

References 19 publications

Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation.

Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation.

X-ray spectromicroscopic investigation of natural organochlorine distribution in weathering plant material

Purification and Catalytic Properties of Two Manganese Peroxidase Isoenzymes from Pleurotus eryngii

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