Article citationsMore>>

Jang, M.-S., Lee, Y.-M., Kim, C.-H., Lee, J.-H., Kang, D.-W., Kim, S.-J. and Lee, Y.-C. (2005) Triphenylmethane reductase from Citrobacter sp. Strain KCTC 18061P: Purification, characterization, gene cloning, and overexpression of a functional protein in Escherichia coli. Applied Environmental Microbiology, 71, 7955-7960. doi:10.1128/AEM.71.12.7955-7960.2005

has been cited by the following article:

• TITLE: Decolorization of triphenyl methane dyes by Fomitopsis feei

  AUTHORS: S. V. S. S. S. L. Hima Bindu Nidadavolu, Krishna Gudikandula, Shiva Krishna Pabba, Singara Charya Maringanti

  KEYWORDS: Triphenyl Methane Dyes; Fomitopsis feei; Dye Decolorization; Lignolytic Enzymes; Triphenyl Methane Reductase

  JOURNAL NAME: Natural Science, Vol.5 No.6A, June 18, 2013

  ABSTRACT: Six triphenylmethane dyes viz., bromophenol blue, basic fuchsin, methyl violet, methyl green, ethyl violet and malachite green were studied for their decolorization by Fomitopsis feei. Among, basic fuchsin (98%) was maximum decolorized followed by bromophenol blue (96.8%). However, the rate of bromophenol blue decolorization was very fast. There was no correlation between the lignolytic activity and dye decolurization of the dyes. The highest laccase and lignin peroxidase activities were observed in basic fuchsin (46 U/mL) and methyl green (44 U/mL) respectively after 21 days of incubation, which were poor dye degraders. The triphenylmethane reductase enzyme was the responsible enzyme for the decolorization of these triphenyl methane dyes. The treatment by using fungal organisms was considered to be the cost-effective and ecofriendly method of decolourization of effluents discharged from the dye industries.