Oxidative Decarboxylations of 4-Hydroxymandelic Acid and 2-(4-Hydroxypbenyl)glycine by Laccase fromCoriolus versicolorand Bilirubin Oxidases fromTrachyderma tsunodaeandMyrothecium verrucaria

Agematu, Hitosi; Shibamoto, Norio; Nishida, Hiroshi; Okamoto, Rokuro; Shin, Takashi; Murao, Sawao

doi:10.1271/bbb.57.1877

Cited by 19 publications

(4 citation statements)

References 9 publications

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“…: Fr.) Kummer, P. radiata, laccase levels are enhanced in the presence of 2,5-xylidine (Fahraeus and Reinhammar 1967, Agematu et al 1993, Rogalski and Leonowicz 1992. According to Bollag and Leonowicz (1984), extracellular laccases are constitutively produced in white-rot fungi in small amounts, and Baldrian (2005) confirmed this by reporting that there are many taxonomic or physiological groups of fungi that do not produce significant amounts of laccase, or for which this enzyme is only produced by a few species.…”

Section: Discussionmentioning

confidence: 92%

Ligninolytic activity of Phlebiopsis gigantea strains in cultivation on Norway spruce wood

Żółciak

2019

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Abstract As a white-rot basidiomycetous and wood-decaying fungus, Phlebiopsis gigantea (Fr.: Fr.) Jülich is able to degrade lignin, cellulose and hemicellulose with a complex set of extracellular enzymes. Enzyme activity of this fungus has not been sufficiently explored. The aim of this study was to assess the activity of laccase and peroxidases as well as the level of micromolecular compounds in P. gigantea strains, grown on pieces of Norway spruce wood (sapwood and heartwood) over 50 days of incubation under laboratory conditions. Enzymatic activity was determined using spectrophotometry. Phlebiopsis gigantea strains showed laccase (Lacc), manganese peroxidase (MnP), lignin peroxidase (LiP) and versatile peroxidase (VP) activity. Hydroxy– and methoxyphenols were released during this process also. High levels of MnP activity (from 5.5 to 107.847 mU/μg of protein in cultures on sapwood and from 7.585 to 229.055 mU/μg of protein in cultures on heartwood) were observed in P. gigantea strains, as well as high activity of VP with manganese-oxidizing properties (from 3.36 to 61.708 mU/μg of protein on sapwood and from 1.7 to 254.479 mU/μg of protein on heartwood) compared with the other examined extracellular enzymes. The activity of Lacc ranged from 0 to 0.731 mU/μg of protein on sapwood and from 0 to 0.216 of protein on heartwood. LiP activity was also low and ranged from 0.025 to 0.593 mU/μg of protein on sapwood, and from 0.060 to 1.566 mU/μg of protein on heartwood. The activity of VP in terms of guaiacol-oxidizing properties ranged from 0.016 to 1.432 mU/μg of protein in cultures on sapwood, and from 0.042 to 1.238 mU/μg of protein on heartwood. Released hydroxyphenols for P. gigantea strains ranged from 39.204-129.157 μg of protocatechuic acid/ml in cultures on sapwood, and from 23.098-83.630 μg of protocatechuic acid/ml on heartwood. Methoxyphenols produced by P. gigantea strains ranged from 7.5 to 22.987 μg of vanillin acid/ml on sapwood, and from 10.187 to 36.885 μg of vanillin acid/ml on heartwood. Keywords: white-rot fungus, Phlebiopsis gigantea, laccase, manganese peroxidase, lignin peroxidase, versatile peroxidase, hydroxy–, methoxyphenols.

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Section: Discussionmentioning

confidence: 92%

Ligninolytic activity of Phlebiopsis gigantea strains in cultivation on Norway spruce wood

Żółciak

2019

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“…The laccase showed sequence homology with BOD from Myrothecium sp., and also showed BOD activity. It is known that BOD oxidizes some laccase substrates under alkaline conditions [14,15]. However, the alkaliphilic laccase from M. verrucaria 24G-4 showed higher speci¢city toward laccase substrates than common BOD.…”

Section: Discussionmentioning

confidence: 98%

Characterization of alkaliphilic laccase activity in the culture supernatant ofMyrothecium verrucaria24G-4 in comparison with bilirubin oxidase

Sulistyaningdyah

Ogawa

Tanaka

et al. 2004

FEMS Microbiology Letters

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An enzyme showing alkaliphilic laccase activity was purified from the culture supernatant of Myrothecium verrucaria 24G-4. The enzyme was highly stable under alkaline conditions, showed an optimum reaction pH of 9.0 for 4-aminoantipyrine/phenol coupling, and decolorized synthetic dyes under alkaline conditions. It showed structural and catalytic similarities with bilirubin oxidase, but preferably oxidized phenolic compounds. The enzyme catalyzed veratryl alcohol oxidation at pH 9.0 with 2,2P-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a mediator, suggesting that the laccase mediator system functioned well under alkaline conditions.

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“…As a result, MW is increasing and the content of OH phen is decreasing. However, laccase is able to decarboxylation of the just formed acids (Agematu et al 1993 ) and may attack the methoxy groups through demethylation (Leonowicz et al 1984 ) or demethoxylation (Potthast et al 1995 ). These reactions are the initial steps for transformation of the lignin polymer as interpreted by the quoted authors.…”

Section: Structural Characterization Analysismentioning

confidence: 95%

Physicochemical properties of sodium lignosulfonates (NaLS) modified by laccase

Zhou

Yang

et al. 2012

Holzforschung

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The ability of commercial laccase for improvement of the physicochemical properties of sodium lignosulfonate (NaLS) without any mediator has been investigated. Surface tension, adsorption characteristics, rheological behaviors and fl uidity of cement pastes were in focus. Gel permeation chromatography (GPC) shows an initial decrease and then an extensive increase of molecular weight (MW) of NaLS after incubation with laccase. Parallel to MW decrement, the content of phenolic groups is increasing, while an MW increment has the opposite effect. The UV-Vis spectra and the zeta potential of NaLS do not indicate further modifi cation of the substitution pattern on the aromatic ring. The surface tension of NaLS and the adsorbed amount of NaLS on MgO particles is elevated after laccase treatment. The electrostatic attraction between MgO particles and NaLS is the main driving force during this adsorption process. The dispersion effi ciency of laccase modifi ed NaLS on the MgO slurry and cement paste is improved.

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Oxidative Decarboxylations of 4-Hydroxymandelic Acid and 2-(4-Hydroxypbenyl)glycine by Laccase fromCoriolus versicolorand Bilirubin Oxidases fromTrachyderma tsunodaeandMyrothecium verrucaria

Cited by 19 publications

References 9 publications

Ligninolytic activity of Phlebiopsis gigantea strains in cultivation on Norway spruce wood

Ligninolytic activity of Phlebiopsis gigantea strains in cultivation on Norway spruce wood

Characterization of alkaliphilic laccase activity in the culture supernatant ofMyrothecium verrucaria24G-4 in comparison with bilirubin oxidase

Physicochemical properties of sodium lignosulfonates (NaLS) modified by laccase

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