|Industrialization has led to the introduction of a variety of synthetic organic (xeno-alien, biotic-nature) compounds which are generally toxic. One of the very pressing environmental problems of the textile industry is the removal of colour from effluents prior to discharge to local sewage treatment system. Brightly coloured water soluble dyes are problematic as they pass unaffected through conventional sewage treatment systems (Nikhath Kousar et al., 2000). Phenolic effluents which colour receiving waters are toxic to mammals and fish (Peyton, 1984). To depollute the dye waste water, the physico-chemical methods, adsorption, chemical precipitation, flocculation, photolysis, chemical oxidation and reduction, electro chemical treatment and ion-pair extraction have proved to be costly and less effective (Zollinger, 1987; Boman et al., 1988). Conventional biological treatment methods such as aerated lagoons and activated sludge processes require a long hydraulic detention time and long sludge retention time to overcome shock loads (Kumaran and Shivaraman, 1998). Emerging applications in Biotechnology include the search for enzymes that function well under extremes of conditions. Advantages of the enzymatic approach are the broad specificity of the enzymes, which enable them to react with a wide range of phenols and less sensitivity to the operational upsets. Peroxidases, laccascs and tyrosinase are now being.
|During acclimation to the textile dyeing effluent the growth of water hyacinth plant was profuse. But above 50% of the effluent, the plant growth was inhibited. Trivedy (1998), discussed the role of acclimation in bio-augmentation and enrichment of specialized cultures which treat the waste. Water hyacinth roots serve as a site for bacterial attachment. The activity of peroxidase is superior in water hyacinth (Shuangxi Shi and Xichung Wang, 1991). Increased enzyme activity indicated the phyto physiological metabolic activity and so the treatment of effluent. The specific activity of the crude extract was 6.25 x 10-2 . The specific activity of the enzyme during the precipitation with ammonium sulphate is presented in Table 1 and Fig. 1. 70% of ammonium sulphate precipitated source showed maximum activity of 9.70 x I0”2. The specific activity of the dialysate was 5.60 x 10’. The fraction profile of peroxidase by column chromotography is presented in Table 2 and Fig. 2. 6lh fraction exhibited a higher most activity of 2. Peroxidase has been purified and characterized from a number of higher plant systems including horse radish (Shannon et al., 1966), potato (Espelie and Kolattukudy, 1985), tobacco (Mader, 1980), turnip (Mazza et al., 1968) and barley (Saeki et al.. 1986). Production of peroxidase from Inonotus Weirii (Annikka Mustranta, 1987) and Aspergillus niger (Mellon. 1991) were also reported. Removal of phenolic compounds by peroxidase has been discussed by Alberti and Klibanov (1981); Klibanov and Morris (1981); Hakulinen (1988); Claus and Filip (1990). The enzyme converts soluble phenolics into insoluble polyphenolic precipitates which can be removed by filtration (Sun et al., 1992; wada et al.,
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