Decolorization of triphenylmethane dyes by wild mushrooms
- Authors
- Kang, Hyeon Woo; Yang, Yun Hui; Kim, Sang Woo; Kim, Soonok; Ro, Hyeon-Su
- Issue Date
- Jun-2014
- Publisher
- KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING
- Keywords
- crystal violet; decolorization; malachite green; mushroom; triarylmethane dye
- Citation
- BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, v.19, no.3, pp 519 - 525
- Pages
- 7
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- BIOTECHNOLOGY AND BIOPROCESS ENGINEERING
- Volume
- 19
- Number
- 3
- Start Page
- 519
- End Page
- 525
- URI
- https://scholarworks.gnu.ac.kr/handle/sw.gnu/18970
- DOI
- 10.1007/s12257-013-0663-z
- ISSN
- 1226-8372
1976-3816
- Abstract
- Triphenylmethane dyes such as Crystal Violet (CV) and Malachite Green (MG) are common textile dyes. MG, which is toxic to humans, is widely used in aquaculture as an antifungal agent. In this study, 56 mushroom strains from 12 species of wild mushrooms were examined on dye-containing PDA plates to evaluate their potential for the bioremediation of synthetic dyes. Pycnoporus coccineus, Coriolus versicolor, and Lentinula edodes showed fair growth on CV, but only a few survived on MG. However, a decolorization experiment in an aqueous system revealed that the growth on MG-containing solid medium did not directly match the decolorization of MG in the aqueous system. C. versicolor IUM0061 grew well on both MG and CV plates, but could not decolorize MG in the reaction mixture. Conversely, HPLC analysis revealed that P. coccineus IUM0032, which could not grow on the MG plate, completely mineralized MG within 3 days. A subsequent enzyme activity assay revealed a high lignin peroxidase activity in the reaction mixture, indicating that lignin peroxidase is the key enzyme involved in degradation of MG in P. coccineus IUM0032.
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