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Abstract
Direct Red 28 is a carcinogenic direct diazo dye used for the coloration of paper products. It is recalcitrant and is mostly found in effluents of paper factories. Bacteria in consortia and monocultures those capable of decolorizing Direct Red 28 were isolated previously. The culture Xanthomonas campestris MTCC10, 108 was found able to decolorize dye consortia of Direct Red 28, Amido Black, Reactive Black, Reactive Blue, Reactive Red concentration of 20 mg/l each, thus making final concentration approximately to 100 mg/l. It was observed that the rate of decolorization by Xanthomonas campestris MTCC10, was varied when incubated under optimum environmental conditions. Dye degradation occurred in the supernatant of sonicated cells, indicating that the dye degrading enzyme was located intracellularly. In present study the active component responsible for decolorization. Direct Red 28 was found as azoreductase rather than laccase and peroxidases enzymes. The optimum concentration of NADH was 0.10 mM and 250 μg of enzyme resulted reduction of 100 μg/ml (highest) Direct Red 28. Based on these results, the optimal enzyme assay conditions were 100μg/ml Direct Red 28, 0.1mM NADH and 250 μg/ml enzyme in 1 ml assay mixture.
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References
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References
Banat, I.M., Nigam, P., Singh, D. and Marchant, R., 1996. Microbial decolorization of textile dye containing effluents: A review. Biores. Technol.58: 217 – 227. DOI: https://doi.org/10.1016/S0960-8524(96)00113-7
Bradford, M. M., 1976. A rapid and sensitive method for the quantification of protein dye binding of microgram quantities of protein. Anal. Biochem. 72: 248–254. DOI: https://doi.org/10.1016/0003-2697(76)90527-3
Cerniglia, C.E., Freeman, J.P., Franklin, W. and Pack, L.D., 1982. Metabolism of azo dyes derived from benzidine, 3, 3'--Dimethylbenzidine and 3, 3'--dimethoxybenzidine to potentially carcinogenic aromatic amines by intestinal bacteria. Carcinogenesis. 3: 1255-1260. DOI: https://doi.org/10.1093/carcin/3.11.1255
Chung, K.T., 1983. The significance of azo-reduction in the mutagenesis and carcinogenesis of azo dyes. Mutat. Res. 114:269-281. DOI: https://doi.org/10.1016/0165-1110(83)90035-0
Collier, S.W., Storm, J.E. and Bronaugh, R.L., 1993. Reduction of azo dyes during in vitro percutaneous Absorption. Toxicol. Appl. Pharmacol. 118: 73 –79. DOI: https://doi.org/10.1006/taap.1993.1011
Dillon, D., Combes, R. and Zeiger, E., 1994. Activation by caecal reduction of the azo dye D&C Red No. 9 to a bacterial mutagen. Mutagenesis. 9: 295 –299. DOI: https://doi.org/10.1093/mutage/9.4.295
Have, R. T., Hartmans, S., Teunissen, P.J.M., Field, Y. A., 1997. Purification and characterisation of two peroxidase isozymes produced by Bjerkandera sp. Strain BOS55. FEBS Letters 422: 391 – 394. DOI: https://doi.org/10.1016/S0014-5793(98)00044-1
Huang, Q., Walter, J. and Weber, J. R., 2002. Peroxidase catalyzed oxidative coupling of phenol in the presence of geosorbants: Effects of sorbent chemicals characteristics, American Chemical Society, Environmental Chemistry Awards Symposia, 224th ACS National Meeting, Boston, MA, USA.
Levine, W.G., 1991. Metabolism of azo dyes: Implications for detoxification and activation. Drug Metab. Rev. 23: 253–309. DOI: https://doi.org/10.3109/03602539109029761
Macwana, R. S., 2007. Identification and isolate of an azoreductase from Enterococcus faecium .Ph.D. thesis submitted to Oklahoma State University.
Morgan, D.L., Dunnick, J.K., Goehl, T., Jokinen, M.P., Matthews, H.B., Zeiger, E. and Mennear, J.H., 1984. Summary of the National Toxicology Program Benzidine Dye Initiative. Environ. Health Perspect. 102: 63-78. DOI: https://doi.org/10.1289/ehp.9410263
Nachiyar, C. V. and Rajkumar, G. S., 2003. Degradation of tannery and textile dyes, Navitan Fast Blue S5R by Pseudomanse Aeroginosa. World J. Microbiol. Biotechnol. 19: 609-614
Pearce, C.I., Loyd, J.T., and Guthrie, J.T., 2003. The removal of colour from textile waste water using whole bacteria cells: A review. Dyes and Pigments 58: 179 – 196. DOI: https://doi.org/10.1016/S0143-7208(03)00064-0
Punj, S. and John, G., 2008. Purification and identification of an FMN-dependent NAD(P)H azo reductase from Enterococcus faecalis. Curr. Issues Mol Biol 11:59-66.
Stolz, A., 2001. Basic and Applied aspects in the microbial degradation of azo dyes.Appl. Microbiol. Biotechnol. 56: 69 – 80 DOI: https://doi.org/10.1007/s002530100686
Zarvazina, A.G., Leontivevsky, A.A., Golovleva, L.A. and Trofimov, S.Y., 2004. Biotransformation of soil humic acids by blue laccase of Panus tigrinus 8/18: an in vitro-study. Soil Biol. and Biochem. 36: 359 – 369. DOI: https://doi.org/10.1016/j.soilbio.2003.10.010
Zimmermann, T., Kulla, H.G. and Leisinger, T., 1982. Properties of purified orange II azoreductase, the enzyme initiating azo dye degradation by Pseudomonas KF46. Euro. J.Biochem. 129: 197 – 203. DOI: https://doi.org/10.1111/j.1432-1033.1982.tb07040.x