Mycodecolorization Activity of Pleurotus Citrinopileatus for Chemically Different Textile Dye Under Varied Aromatic Amino Acids and Trace Elements
In the present study, ligninolytic enzymes laccase (benzenediol: oxygen reductase EC; 188.8.131.52) and Manganese Peroxidase (Mn(II): hydrogen-peroxide oxidoreductase EC; 184.108.40.206) activity and of White Rot Fungi (WRF) Pleurotus citrinopileatus were enhanced with the application of trace metal i.e. Copper and Manganese at 25 ppm and 50 ppm followed by aromatic amino acids (Phenylalanine, Tryptophan and Tyrosine) at 0.02 μM and 0.4 μM. Laccase and MnP activity were 213.42U and 202.28U respectively, observed at 300ppm of Methyl Red supplemented with Tyrosine (0.2μM) followed by treatment of Tryptophan (198.45U and 195.16U) and Phenylalanine (195.85U and 188.15U). Maximum Laccase and MnP activity (Tyrosine treated) were revealed maximum decolorization of Phenol Red and Methyl Red (84.14% and 78.20%) followed by Phenylalanine (80.92% and 73.80%) and Trypatophan (71.22% and 70.12%). The negative correlation of Laccase and MnP activity was observed with a higher concentration (>50ppm) of trace metal in the medium, while at 25ppm of copper supplemented medium increase three-fold of Laccase activity (585.56U) as tyrosine medium and similarly, Manganese (25ppm) inosculated medium revealed three-fold more MnP activity (478.95U). A lower amount of Cu hoists Laccase and MnP activity which decolorized 300ppm of Methyl Red and Phenol Red with maximum percent (92.3% and 88.15%) followed by Mn. Thus, Laccase and MnP enzymes both play an important role in decolorization of dyes, and its activity was enhanced with the application of lower concentration of trace metals followed by aromatic amino acids.