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.

Trametes versicolor showed the ability of degrading synthetic dyes such as congo red (CR) and methylene blue (MB) in solid and liquid culture conditions. The T. versicolor strains isolated in Korea degraded MB more efficiently than CR, differently most of other white mushrooms known to have difficulties in degrading MB than other dyes. Thus the Koren strains of T. versicolor showed the commercial potential to be used for cleaning dye-contaminated region without any patent-related problem. The main enzyme responsible for dye deradation was laccase. The manganese peroxidase (MnP) was also detected and supposed to be involved in the degradation process of synthetic dyes. However, no lignin peroxidase (LiP) was detected from degradation process, indicating LiP is not the enzyme T. versicolor use to degrade CR and MB.