Laccase-catalyzed decolorization of the synthetic azo-dye diamond black PV 200 and of some structurally related derivatives

The kinetics of laccase-catalyzed transformation of the azo-dye Diamond Black PV 200 (CI Mordant Black 9) and various related synthesized derivatives were analyzed for dependence on pH and substrate structure. The reaction mixture of Diamond Black PV 200 was analyzed by HPLC/MS_/MS and it was shown that upon laccase oxidation, reactive chinoid fragments of lower molecular weight were formed. These may further oligomerize as indicated by the appearance of a number of compounds with increased molecular weight. The pH optimum for the decolorization was pH 5 for Diamond Black PV 200 which did not change significantly when the substitution pattern of its basic structure was varied. Biodegradability, however, was strongly dependent on the structure of the dyes

Specificities of a chemically modified laccase from trametes hirsuta on soluble and cellulose-bound substrates

Laccases could prevent fabrics and garments from re-deposition of dyes during washing and finishing processes by degrading the solubilized dye. However, laccase action must be restricted to solubilized dye molecules thereby avoiding decolorization of fabrics. Chemical modification of enzymes can provide a powerful tool to change the adsorption behaviour of enzymes on water insoluble polymers. Polyethylene glycol (PEG) was covalently attached onto a laccase from Trametes hirsuta. Different molecular weights of the synthetic polymer were tested in terms of adsorption behaviour and retained laccase activity. Covalent attachment of PEG onto the laccase resulted in enhanced enzyme stability while with increasing molecular weight of attached PEG the substrate affinity for the laccase conjugate decreased. The activity of the modified laccases on fibre bound dye was drastically reduced decreasing the adsorption of the enzyme on various fabrics. Compared to the 5 kDa PEG laccase conjugate (K/S value 47.60

A halotolerant laccase from Chaetomium strain isolated from desert soil and its ability for dye decolourization

13 p.-6 fig.-3 tab.A novel fungal laccase produced by the ascomycete Chaetomium sp. isolated from arid soil was purified and characterized and its ability to remove dyes was determined. Extracellular laccase was purified 15-fold from the crude culture to homogeneity with an overall yield of 50% using ultrafiltration and anion-exchange chromatography. The purified enzyme was found to be a monomeric protein with a molecular mass of 68 kDa, estimated by SDS-PAGE, and with an isoelectric point of 5.5. The optimal temperature and pH value for laccase activity toward 2,6-DMP were 60 °C and 3.0, respectively. It was stable at temperatures below 50 °C and at alkaline conditions. Kinetic study showed that this laccase showed higher affinity on ABTS than on 2,6-DMP. Its activity was enhanced by the presence of several metal ions such as Mg2+, Ca2+ and Zn2+, while it was strongly inhibited by Fe2+, Ag+ and Hg2+. The novel laccase also showed high, remarkable sodium chloride tolerance. Its ability to decolorize different dyes, with or without HBT (1-hydroxy-benzotriazole), as redox mediator, suggests that this protein may be useful for different industrial applications and/or bioremediation processes.Peer reviewe