Acceleration of anthraquinone-type dye removal by white-rot fungus under optimized environmental conditions

The decolorization of the recalcitrant dye Remazol Brilliant Blue R (RBBR) by the culture filtrate of Polyporus sp. S133 and the effect of various environmental factors were investigated. Both biodegradation and biosorption were playing an important role in bioremoval mechanisms. The highest biosorption of RBBR in Polyporussp. S133 was shown by all carbon sources such as sucrose, glucose, fructose, and starch. No biosorption was shown by the addition of aromatic compounds and metal ions; 97.1 % RBBR decolorization was achieved in 120-rpm culture for 96 h, as compared to 49.5 % decolorization in stationary culture. Increasing the shaking rotation of the culture to more than 120 rpm was proven to give a negative effect on decolorization. The highest production of laccase was shown at pH 4 and constantly decreases when the pH level increases. The addition of glucose, ammonium tartrate, Cu2+, and protocatechuic acid was the suitable environmental condition for RBBR decolorization. There was a positive relationship between all environmental conditions and laccase production in the decolorization of RBBR

Enzymatic decolorization of textile dyeing effluents

Commercial azo, triarylmethane, antraquinonic, and indigoid textile dyes are efficiently decolorized with enzyme preparations from Pleuratus ostreatus, Schizophyllum commune, Neurospora crassa, Polvporus sp., Sclerotium rolfsii, Trametes villosa, and Myceliophtora thermophila. The nature of substituents on the dyes' benzene rings influences enzyme activity, and hydroxyl and amino groups enhance decolorization. The presence of lignin peroxidase and/or manganese peroxidase in addition to Iaccase (P. Ostreatus, S. commune, S. rolfsii, N. crassa) increases decolorization by up to 25%, The effect of textile dyeing auxiliaries depends on the individual enzymes. Polyporus sp. and T. villosa are inhibited up to 20% by copper and iron chelating agents and anionic detergents, while the S. Commune enzymes lose up to 70% of their activity