• Journal of Mushroom
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• v.13 no.1
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• pp.63-67
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• 2015

White rot fungi produce lignin-degrading enzymes such as laccase, manganese peroxidase and lignin peroxidase. These extracellular oxidases efficiently degrade recalcitrant synthetic dyestuffs with diverse chemical structures. Here, we examined the activities of lignin-degrading enzymes in Trametes versicolor using triphenyl methane dyes, crystal violet (CV) and malachite green (MG). Both dyes were decolorized by T. versicolor in solid and liquid culture conditions. T. versicolor decolorized MG more quickly than CV in both conditions. Among three ligninolytic enzymes, laccase was most abundantly found in the decolorization processes of CV and MG. However, higher activity of laccase was needed to degrade CV than MG. The much less activity of MnP was also detected. But the increase of MnP activity was well corresponded to the decolorization efficiency of CV, suggesting the involvement of MnP in CV degrading process. However, its role in the degradation process of MG is supposed to be subsidiary to laccase.

• Korean Journal of Microbiology
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• v.33 no.4
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• pp.252-256
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• 1997

The white rot fungus Coriolus hiysutus decolorized several recalcitrant dyes. Four different types of dyes, including azo, triphenyl methane, heterocyclic, and polymeric dye, were treated by the mycelial preparation. Triphenyl methane dye, bromophenol blue lost over 95% of its color. Congo red and Poly R-478 were decolorized less than bromophenol blue, 57 and 55%, respectively. However, heterocyclic dye, methylene blue was not decolorized significantly and only red shift was observed. Extracellular laccase and peroxidase activities were appeared maximally in high level of dye decolorization media. In electrophoretic experiments, common active bands of laccase and peroxidase were found in all dye decolorized medium. These results indicated that the culture conditions which yield high levels of laccase and peroxidase activity lead to high levels of dye decolorization, and these two enzymes might be play an important roles in dye decolorization.

• Journal of the Korean Chemical Society
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• v.17 no.6
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• pp.411-415
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• 1973

The reaction between cyanide ion and triphenyl methane dyes is subject to marked catalysis by cationic micelles of cetyltrimethyl ammonium bromide(CTABr) and retarded by anionic micelles of sodium lauryl sulfate(NaLS). Added salts, anions inhibit the catalysis by CTABr, and cations, especially $Zn^{++},\;Cd^{++}$ decrease the retardation of the reaction rates in the presence of NaLS. The kinetic effects of the ionic micelles are much larger in water than in ethanol-water, methanol-water, propanol-water and acetone-water, but strange solvent effects, acceleration the reaction rates, was found in the reaction with malachite green in water-methanol system.

• Journal of Mushroom
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• v.20 no.2
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• pp.86-91
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• 2022

Pleurotus eryngii, a white rot fungus, produces two extracellular lignin-degrading enzymes, laccase and manganese peroxidase (MnP). Owing to these enzymes, P. eryngii efficiently degrades synthetic chemicals such as azo, phthalocyanine, and triphenyl methane dyes. In this study, we investigated the degradation processes of four aromatic dyes, congo red (CR), methylene blue (MB), crystal violet (CV), and malachite green (MG), by P. eryngii under solid and liquid culture conditions. CR and MG were the most quickly degraded under solid and liquid culture conditions, respectively. However, compared to CR, CV, and MG, MB was not degraded well under both culture conditions. The activities of ligninolytic enzymes (laccase and MnP) were also investigated. Laccase was identified to be the major enzyme for dye degradation. A positive relationship between decolorization and enzyme activity was observed for CR, MB, and CV degradation. In contrast, decolorization of MG ensued after high enzyme activity. These results indicate that the degradation process differs between MG and the other aromatic dyes. Therefore, P. eryngii could be a potential tool for the bioremediation of synthetic aromatic dye effluent.