`Yellow' laccase of <i>Panus tigrinus</i> oxidizes non‐phenolic substrates without electron‐transfer mediators

Leontievsky, A. A.; Myasoedova, N. M.; Pozdnyakova, N. N.; Golovleva, Ludmila

doi:10.1016/s0014-5793(97)00953-8

Cited by 103 publications

(69 citation statements)

References 14 publications

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“…Yellow laccase is artificially reduced blue laccase as it does not have absorption at 600 nm and EPR spectrum (Leontievsky et al 1997;Pozdnyakova et al 2006). Alteration of blue-to-yellow laccase can occur by the reduction of type I copper site by aromatic product of lignin degradation or binding of specific amino acid of enzyme polypeptide to a molecule of modified product produced by lignin degradation; it can also be due to heterogeneity induced by glycosylation (Mot et al 2012).…”

Section: Yellow Laccasementioning

confidence: 99%

“…Alteration of blue-to-yellow laccase can occur by the reduction of type I copper site by aromatic product of lignin degradation or binding of specific amino acid of enzyme polypeptide to a molecule of modified product produced by lignin degradation; it can also be due to heterogeneity induced by glycosylation (Mot et al 2012). The modified molecule bound to the apoenzyme performs the function of electron-transfer mediator analogous to the role of 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) diammonium salt (ABTS) or other compounds in the reaction of blue laccase (Leontievsky et al 1997), hence having high redox potential which allows them to oxidize non-phenolic compounds without any mediators (Mot et al 2012) and having greater industrial potential (Daroch et al 2014). The change in protein conformation may explain the sensitivity of yellow laccase to CO and other inhibitors, e.g., P. tigrinus (Leontievsky et al 1997).…”

Section: Yellow Laccasementioning

confidence: 99%

“…The modified molecule bound to the apoenzyme performs the function of electron-transfer mediator analogous to the role of 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) diammonium salt (ABTS) or other compounds in the reaction of blue laccase (Leontievsky et al 1997), hence having high redox potential which allows them to oxidize non-phenolic compounds without any mediators (Mot et al 2012) and having greater industrial potential (Daroch et al 2014). The change in protein conformation may explain the sensitivity of yellow laccase to CO and other inhibitors, e.g., P. tigrinus (Leontievsky et al 1997). At present, information about the purification and characterization of yellow laccase is extremely limited and their catalytic properties are still seldom investigated.…”

Section: Yellow Laccasementioning

confidence: 99%

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Fungal laccase discovered but yet undiscovered

Agrawal

Chaturvedi

Verma

2018

Bioresour. Bioprocess.

178

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Laccases belongs to multinuclear copper-containing oxidase and can act on a variety of aromatic and non-aromatic compounds. Due to their broad substrate specificity, they are considered as a promising candidate in various industrial and biotechnological sectors. They are regarded as a "Green Tool"/"Green Catalyst" in biotechnology. The present review focuses on structure, reaction mechanism, categories, applications, economic feasibility, limitations, and future prospects of fungal laccases. Thus, this review would help in understanding laccases along with the areas, which has not been focused and requires attention. Since past, immense work has been carried out on laccases: yet, new discoveries and application are ever increasing which includes bio-fuel, bio-sensor, fiber board synthesis, bioremediation, clinical, textile industry, food, cosmetics, and many more. Hence, it can be stated that fungal laccase is an enzyme which is "discovered but yet undiscovered".

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Section: Yellow Laccasementioning

confidence: 99%

Section: Yellow Laccasementioning

confidence: 99%

Section: Yellow Laccasementioning

confidence: 99%

See 1 more Smart Citation

Fungal laccase discovered but yet undiscovered

Agrawal

Chaturvedi

Verma

2018

Bioresour. Bioprocess.

178

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“…The yellow laccase was suggested to be formed as a result of blue laccase modification by products of lignin degradation, which might play a role as natural electron-transfer mediators for the oxidation of nonphenolic substances. 41) 2. Degradation of β-O-4 model compounds.…”

Section: )mentioning

confidence: 99%

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

Higuchi

2004

Proc. Jpn. Acad., Ser. B

121

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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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“…Ultimately the multiple reactions give rise to polymerization, alkyl aryl cleavage, C 2 -oxidation or demethoxylation of the phenolic reductants (Kirk and Shimada, 1985). The non phenolic aromatic substances are oxidized by T. versicolor (Kawai et al, 1989) whereas non phenolic aromatics are oxidized directly in the presence of O 2 by laccases ( Leontievsky et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Biomethanization of Coal to Obtain Clean Coal Energy: A Review

Singh

2012

Energy Exploration & Exploitation

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This paper entails a review on the possibility of methanization of coal using microbial tool. Biomethanization process of coal begins with biodegradation of coal by specific bacteria and fungi. As a result of this, major polymers present in coal like proteins, polysaccharides, nucleic acids and lipids are hydrolyzed to monomers like aminoacids, sugars, purines, pyrimidines and long chain fatty acids. Their subsequent fermentation forms hydrogen, CO 2 and a number of reduced compounds like alcohols, short chain fatty acids, organic acids and certain aromatics. The oxidation of these reduced compounds further leads to the formation of acetate, hydrogen and CO 2 , methylated compounds and several intermediate compounds. Syntrophic relationship exists between fermenting bacteria and methanogens. The resultant oxidized compounds of fermenting bacteria are gradually utilized by specific methanogens to form methane. Hydrogenotrophic methanogens utilize H 2 and convert CO 2 into methane. Whereas acetate is utilized by acetoclastic methanogens to generate methane. The methylated compounds are utilized for methane formation by methylotrophic methanogens.

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`Yellow' laccase of Panus tigrinus oxidizes non‐phenolic substrates without electron‐transfer mediators

Cited by 103 publications

References 14 publications

Fungal laccase discovered but yet undiscovered

Fungal laccase discovered but yet undiscovered

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

Biomethanization of Coal to Obtain Clean Coal Energy: A Review

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