| Literature DB >> 21194634 |
Tatiana Marchis1, Paola Avetta, Alessandra Bianco-Prevot, Debora Fabbri, Guido Viscardi, Enzo Laurenti.
Abstract
Reactive dyes are widely employed in textile industries and their removal from wastewaters is a relevant environmental problem. In addition to chemical and physical methods, several bioremediation approaches, involving intact micro-organisms or isolated enzymes, have been proposed to decolorize dye solutions. In this paper, we report the complete and fast decolourization of a Cu(II)-phthalocyanine based reactive dye (Remazol Turquoise Blue G 133) by means of the soybean peroxidase/H(2)O(2) system. The oxidative degradation of the dye in aqueous solution at 25°C was studied as function of pH, revealing a quantitative decolourization yield at acidic pH values with a maximum of activity at pH 3.3. The reaction products were identified and characterized by HPLC-diode array detector (DAD)-mass spectrometry (MS), ionic chromatography and EPR techniques. This analysis showed that the enzyme catalyses the breaking of the phthalocyanine ring producing sulfophthalimide as the main degradation product, and the release of stoichiometric amount of ammonium and Cu(II) ions. Copyright ÂEntities:
Mesh:
Substances:
Year: 2010 PMID: 21194634 DOI: 10.1016/j.jinorgbio.2010.11.009
Source DB: PubMed Journal: J Inorg Biochem ISSN: 0162-0134 Impact factor: 4.155