Degradation of textile dyes using immobilized lignin peroxidase-like metalloporphines under mild experimental conditions

Abstract

BackgroundSynthetic dyes represent a broad and heterogeneous class of durable pollutants, that are released in large amounts by the textile industry. The ability of two immobilized metalloporphines (structurally emulating the ligninolytic peroxidases) to bleach six chosen dyes (alizarin red S, phenosafranine, xylenol orange, methylene blue, methyl green, and methyl orange) was compared to enzymatic catalysts. To achieve a green and sustainable process, very mild conditions were chosen.ResultsIPS/MnTSPP was the most promising biomimetic catalyst as it was able to effectively and quickly bleach all tested dyes. Biomimetic catalysis was fully characterized: maximum activity was centered at neutral pH, in the absence of any organic solvent, using hydrogen peroxide as the oxidant. The immobilized metalloporphine kept a large part of its activity during multi-cycle use; however, well-known redox mediators were not able to increase its catalytic activity. IPS/MnTSPP was also more promising for use in industrial applications than its enzymatic counterparts (lignin peroxidase, laccase, manganese peroxidase, and horseradish peroxidase).ConclusionsOn the whole, the conditions were very mild (standard pressure, room temperature and neutral pH, using no organic solvents, and the most environmental-friendly oxidant) and a significant bleaching and partial mineralization of the dyes was achieved in approximately 1 h. Therefore, the process was consistent with large-scale applications. The biomimetic catalyst also had more promising features than the enzymatic catalysts.

Heterogeneous oxidation of the dye Brilliant Green with H 2 O 2 catalyzed by supported manganese porphyrins

“…Bleaching percentages were high as 82% after one hour of reaction[57], in agreement with our results for supported MnP1 obtained at a MnP/oxidant/dye molar ratio of 1:5000:10 (MnP1-S-Mag 81% dye bleaching and MnP1-Hallo…”

“…Here, the pH of the bleaching reaction lay between 6 and 7. Comparison of the present work with the work by Zucca et al [57] showed that this MnP with similar structure efficiently catalyze bleaching reactions.…”

“…75% dye bleaching after one hour of reaction). Zucca and co-workers [57] also showed that neutral pH was best for the bleaching reactions. Here, the pH of the bleaching reaction lay between 6 and 7.…”

Emerging Tools for Recognition and/or Removal of Dyes from Polluted Sites: Molecularly Imprinted Membranes

“…Lignin (LiP) and manganese peroxidase (MnP) exhibit similar reaction mechanism. Recently, Zucca and co-workers [196] demonstrated as two immobilized metallo-porphirine (structurally similar to the ligninolytic peroxidase) to bleach six different dyes. The two different enzymes effectively bleached all tested dyes working in mild operating conditions (standard pressure, room temperature and neutral pH, using no organic solvents).…”

Biomimetic Sulfide Oxidation by the Means of Immobilized Fe(III)‐5,10,15,20‐tetrakis(pentafluorophenyl)porphin under Mild Experimental Conditions

“…In our previous studies, we reported the immobilization of some metalloporphins onto solid supports emulating the structure of cytochrome P-450 and ligninolytic peroxidases. These catalytic adducts were able to oxidize both lignin model compounds (recently reviewed in [26]) and durable textile dyes [27][28][29].…”