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Study of the white-rot fungal degradation of selected phthalocyanine dyes by capillary electrophoresis and liquid chromatography

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Conneely, A, Smyth, Franklin and McMullan, Geoffrey (2002) Study of the white-rot fungal degradation of selected phthalocyanine dyes by capillary electrophoresis and liquid chromatography. ANALYTICA CHIMICA ACTA, 451 (2). pp. 259-270. [Journal article]

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The phthalocyanine dyes, Remazol Turquoise Blue G133, Everzol Turquoise Blue and Heligon Blue S4 are found to be biosorbed by Phanerochaete chrysosporium (white-rot fungi) and also metabolised by its ligninolytic extracellular enzymes resulting in dye decolourisation, formation of free copper ions and organic metabolites with ultimate extensive phthalocyanine ring break-down. It is believed that the ligninolytic extracellular enzyme laccase is involved in the early production of a metabolite M-8 which involves break-up of the conjugated phthalocyanine ring structure but which retains multi-negative charge. Another ligninolytic extracellular enzyme, manganese peroxidase, is believed to be involved in the release of Cu2+ from the phthalocyanine structure to give a non-copper-containing phthalocyanine metabolite M-1 with a slightly longer migration time than the parent dye and absorption at 666 nm. The phthalocyanine ring structure is also broken up by metabolic processes that involve desulphonation and oxidation to give phthalimide (M-3) and an unidentified electroactive metabolite M-2. Other minor, unidentified metabolites are observed using capillary electrophoresis and liquid chromatography. (C) 2002 Elsevier Science B.V. All rights reserved.

Item Type:Journal article
Faculties and Schools:Faculty of Life and Health Sciences
Faculty of Life and Health Sciences > School of Biomedical Sciences
Research Institutes and Groups:Biomedical Sciences Research Institute
Biomedical Sciences Research Institute > Northern Ireland Centre for Food and Health (NICHE)
Biomedical Sciences Research Institute > Pharmaceutical Science and Practice
ID Code:5025
Deposited By:Professor Geoffrey McMullan
Deposited On:23 Jan 2010 15:53
Last Modified:16 May 2012 15:56

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