An extracellular H2O2-requiring enzyme preparation involved in lignin biodegradation by the white rot basidiomycete Phanerochaete chrysosporium

Glenn, Jeffrey K.; Morgan, Meredith A.; Mayfield, Mary B.; Kuwahara, Masaaki; Gold, Michael H.

doi:10.1016/0006-291x(83)90672-1

Cited by 572 publications

(186 citation statements)

References 24 publications

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“…They further found using ligninolytic culture experiments with 18 O that the benzyl hydroxyl oxygen atom of the phenylglycol was derived from molecular oxygen. Subsequently Tien and Kirk 9) and Glenn et al 10) dis- (Fig. 4).…”

Section: )-6)mentioning

confidence: 91%

Microbial degradation of lignin: Role of lignin peroxidase, manganese peroxidase, and laccase

Higuchi

2004

Proc. Jpn. Acad., Ser. B

124

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Lignin peroxidase (LiP), laccase (LA) and manganese peroxidase (MnP) of white-rot basidiomycetes such as Phanerochaete chrysosporium, Coliorus versicolor, Phlebia radiata and Pleurotus eryngii catalyze oxidative degradation of lignin substructure model compounds and synthetic lignins (DHPs). Side chain-and aromatic ring cleavage products of both phenolic and non-phenolic substrates oxidized by LiP were isolated and characterized by NMR and MS. The cleavage mechanism was elucidated by using O. Recent studies suggested that LiP is capable of oxidizing lignin directly at the protein surface via a long-range electron transfer process. LA and MnP, which oxidize phenolic but not non-phenolic moieties, generally degrade lignin stepwise from phenolic moieties. However, recent studies indicated that MnP and LA can degrade both phenolic and non-phenolic aromatic moieties of lignin with some special mediators. (1), 4-ethoxy-3-methoxyphenylglycerol-β-guaiacyl ether; (2), 4-ethoxy-3-methoxyphenylglycerol-β, γ-cyclic carbonate; (3), 4-ethoxy-3-methoxyphenylglycerol-β-methyl oxalate; (4), 4-ethoxy-3-methoxyphenylglycerol-β-mucorate. As the case of the degradation of β-O-4 lignin substructure model dimers by LiP, the cyclic carbonates and formate ester of arylglycerols, and arylglycerol were isolated from degradation products of the DHP by LiP ; the chemical structures of the products were identified by GC-MS. These results indicated that the lignin polymer is really degraded by the LiP of white-rot fungi.Active sites of LiP to substrates. Doyle and his group 19) recently found that by cultivating wood-rotting fungi in an agar medium containing several phenolic compounds, such as gallic acid, tannic acid, and hydroquinone, that white-rot fungi produced a large darkened zone around the mycerial mat, but no zone of darkening was associated with the growth of brown-rot fungi. Davidson et al. 37) subsequently investigated the reaction using 210 species of wood-rotting fungi, and concluded that the white-rotting type coincides with Bavendamm's reaction in general, and that the reaction is helpful in identifying fungi. The enzyme responsible for Bavendamm's reaction was extensively studied in the next 10 years, and characterized to be laccase (LA). 38) LA, p-diphenol oxidase (EC 1.10.3.2) has been isolated and characterized as a blue, copper containing oxidase from a lac tree (Rhus spp) and several fungi. White rot fungi constitutively produce laccase during primary metabolism. 39)1. Degradation of β-1 model compounds. Kawai et al. 40) found that phenolic β-1 model compounds are degraded by LiP of P. chrysosporium and LA of C. versicolor via similar pathways. 1-(3,5-Dimethoxy-4-hydroxyphenyl)-2-(3,5-dimethoxy-4-ethoxyphenyl)-propane-1,3-diol (1, Fig. 6) was converted by LA of C. versicolor to 1-(3,5-dimethoxy-4-hydroxyphenyl)-2-(3,5-dimethoxy-4-ethoxyphenyl)-3-hydroxypropanone (2)by Cα oxidation, 2-(3,5-dimethoxy-4-ethoxyphenyl)-3-hydroxypropanal (5), 2,6-dimethoxy-p-hydroquinone (4) and its benzoquinone (3) by alkyl-ph...

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Section: )-6)mentioning

confidence: 91%

Microbial degradation of lignin: Role of lignin peroxidase, manganese peroxidase, and laccase

Higuchi

2004

Proc. Jpn. Acad., Ser. B

124

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“…Phanerochaete chrysosporium has long been the organism of choice for studies of lignin degradation, and much of this work has focused on two peroxidases, lignin peroxidase (LIP) [3][4][5][6] and manganese peroxidase (MnP) [7][8][9], secreted by this fungus under ligninolytic conditions. LiP has generally been considered the key component of this ligninolytic system, at least in part because its high redox potential makes it capable of oxidizing the non-phenolic aromatic moieties that can comprise up to 85% of the lignin polymer [3,10]. However, many white-rot fungi, including a number of aggressive lignin degraders, seem to operate without expressing LiP activity [11][12][13].…”

Section: Introductionmentioning

confidence: 99%

A fungal metabolite mediates degradation of non‐phenolic lignin structures and synthetic lignin by laccase

et al. 1996

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Lignin peroxidase is generally considered to be a primary catalyst for oxidative depolymerization of fignin by white-rot fungi. However, some white-rot fungi lack lignin peroxidase. Instead, many produce laccase, even though the redox potentials of known laccases are too low to directly oxidize the non-phenolic components of lignin. Pycnoporus cinnabarinus is one example of a laccase-producing fungus that degrades lignin very efficiently. To overcome the redox potential barrier, P.cinnabarinus produces a metabolite, 3-hydroxyanthranilate that can mediate the oxidation of nowphenolic substrates by laccase. This is the first description of how laccase might function in a biological system for the complete depolymerization of lignin.

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“…This type of enzyme (synonym ligninase) was first discovered in nitrogen-limited cultures of P. chrysosporium (Glenn et al 1983, Tien & Kirk 1983 and later also found in other white-rots, e.g. Phlebia radiata and Trametes versicolor (Hatakka et al 1987, Jonsson et al 1987, Hatakka 1994, Pointing et al 2005.…”

Section: Enzyme Reactionmentioning

confidence: 95%

Wood production, wood technology, and biotechnological impacts

Kües¹

2007

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An extracellular H2O2-requiring enzyme preparation involved in lignin biodegradation by the white rot basidiomycete Phanerochaete chrysosporium

Cited by 572 publications

References 24 publications

Microbial degradation of lignin: Role of lignin peroxidase, manganese peroxidase, and laccase

Microbial degradation of lignin: Role of lignin peroxidase, manganese peroxidase, and laccase

A fungal metabolite mediates degradation of non‐phenolic lignin structures and synthetic lignin by laccase

Wood production, wood technology, and biotechnological impacts

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