Dye Decoloring Peroxidase Structure, Catalytic Properties and Applications: Current Advancement and Futurity

Abstract

Dye decoloring peroxidases (DyPs) were named after their high efficiency to decolorize and degrade a wide range of dyes. DyPs are a type of heme peroxidase and are quite different from known heme peroxidases in terms of amino acid sequences, protein structure, catalytic residues, and physical and chemical properties. DyPs oxidize polycyclic dyes and phenolic compounds. Thus they find high application potentials in dealing with environmental problems. The structure and catalytic characteristics of DyPs of different families from the amino acid sequence, protein structure, and enzymatic properties, and analyzes the high-efficiency degradation ability of some DyPs in dye and lignin degradation, which vary greatly among DyPs classes. In addition, application prospects of DyPs in biomedicine and other fields are also discussed briefly. At the same time, the research strategy based on genetic engineering and synthetic biology in improving the stability and catalytic activity of DyPs are summarized along with the important industrial applications of DyPs and associated challenges. Moreover, according to the current research findings, bringing DyPs to the industrial level may require improving the catalytic efficiency of DyP, increasing production, and enhancing alkali resistance and toxicity.

Direct Electrochemical Generation of Catalytically Competent Oxyferryl Species of Classes I and P Dye Decolorizing Peroxidases

“…Dye decolorizing peroxidases (DyPs) are a relatively novel family of heme peroxidases that uses hydrogen peroxide as an electron source for catalyzing the oxidation, and in some cases the hydrolysis, of a wide variety of substrates. This includes lignin, phenolic and non-phenolic lignin units, synthetic dyes, aromatic sulfides and even metals ions such as iron and manganese [ 1 , 2 , 3 , 4 , 5 ]. While DyPs were first identified and purified in 1999 [ 6 , 7 ], it took almost a decade to recognize them as an independent peroxidase family with unique features [ 8 ].…”

Design and Engineering of an Efficient Peroxidase Using Myoglobin for Dye Decolorization and Lignin Bioconversion

“…Based on the above HPLC and ESI-MS results, we proposed a generation route of the reaction products, which may involve the generation of reactive radical species upon the activation of H 2 O 2 by the heme enzymes [ 13 , 19 , 30 , 46 , 47 ], resulting in various types of bond cleavages. As shown in Figure 9 , for the oxidative cleavage, the monomers can hardly exist alone, and they might be recombined into new species.…”

Engineering globins for efficient biodegradation of malachite green: two case studies of myoglobin and neuroglobin

“…6B(a Based on the ESI-MS results, we proposed a generation route of the reaction products, which may involve the generation of reactive radical species upon the activation of H 2 O 2 by these enzymes, resulting in different bond cleavages of the substrate. [38][39][40] The cleavage of the C-C bond involving the central carbon by removal of one or two benzenes may generate DLBP and DM-BA. N-Demethylation of DLBP was also observed in a stepwise manner by Du et al 6 Given the identication of MLBP, ABP, MM-PM, DM-PM, and M-PM, the degradation could also be initiated by N-demethylation of MG, followed by oxidation or further N-demethylation.…”