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Textile Dye Biodecolorization by Manganese Peroxidase: a Review

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Textile Dye Biodecolorization by Manganese Peroxidase: a Review molecules Review Textile Dye Biodecolorization by Manganese Peroxidase: A Review Yunkang Chang 1,2, Dandan Yang 2, Rui Li 2, Tao Wang 2,* and Yimin Zhu 1,* 1 Institute of Environmental Remediation, Dalian Maritime University, Dalian 116026, China; [email protected] 2 The Lab of Biotechnology Development and Application, School of Biological Science, Jining Medical University, No. 669 Xueyuan Road, Donggang District, Rizhao 276800, China; [email protected] (D.Y.); [email protected] (R.L.) * Correspondence: [email protected] (T.W.); [email protected] (Y.Z.); Tel.: +86-063-3298-3788 (T.W.); +86-0411-8472-6992 (Y.Z.) Abstract: Wastewater emissions from textile factories cause serious environmental problems. Man- ganese peroxidase (MnP) is an oxidoreductase with ligninolytic activity and is a promising biocatalyst for the biodegradation of hazardous environmental contaminants, and especially for dye wastewater decolorization. This article first summarizes the origin, crystal structure, and catalytic cycle of MnP, and then reviews the recent literature on its application to dye wastewater decolorization. In addition, the application of new technologies such as enzyme immobilization and genetic engineering that could improve the stability, durability, adaptability, and operating costs of the enzyme are highlighted. Finally, we discuss and propose future strategies to improve the performance of MnP-assisted dye decolorization in industrial applications. Keywords: manganese peroxidase; biodecolorization; dye wastewater; immobilization; recombi- nant enzyme Citation: Chang, Y.; Yang, D.; Li, R.; Wang, T.; Zhu, Y. Textile Dye Biodecolorization by Manganese Peroxidase: A Review. Molecules 2021, 26, 4403. https://doi.org/ 1. Introduction 10.3390/molecules26154403 The textile industry produces large quantities of wastewater containing different types of dyes used during the dyeing process, which cause great harm to the environment [1,2]. Academic Editors: Rudy Many dyes and their intermediate metabolites have been identified as mutagenic, terato- J. Richardson and David C. Lacy genic, or carcinogenic, and represent serious health threats to living ecosystems [3]. At present, the treatment of dye wastewater mainly relies on physical or chemical Received: 1 July 2021 management techniques, including chemical reduction, adsorption, ionizing radiation, Accepted: 18 July 2021 precipitation, flocculation and flotation, membrane filtration, electric coagulation, electro- Published: 21 July 2021 chemical destruction, and ion exchange ozonation [4,5]. These technologies have obvious shortcomings such as the excessive use of chemicals, sludge production, expensive factory Publisher’s Note: MDPI stays neutral requirements or high operating expenses, low decolorization efficiencies, and the inability with regard to jurisdictional claims in to handle large numbers of dyes with different structures, so they are not economically published maps and institutional affil- suitable for large-scale wastewater decolorization [6]. iations. The current focus is to reduce toxicity and develop an efficient, economical, and green dye detoxification and decolorization technology. Compared with physical and chemical methods, biological methods offer beneficial and effective prospects due to their economical and environmentally friendly advantages, as well as being simple to use, safe, and efficient, Copyright: © 2021 by the authors. with no secondary pollution [7,8]. Therefore, biotechnology is considered the best choice Licensee MDPI, Basel, Switzerland. to degrade and remove these pollutants effectively. In the biotechnology field, enzyme This article is an open access article biocatalysis is currently the main research area due to its broad application prospects [9,10]. distributed under the terms and Manganese peroxidases (EC 1.11.1.13; MnPs) are a family of heme-containing gly- conditions of the Creative Commons coproteins belonging to the oxidoreductase group. It was discovered in Phanerochaete Attribution (CC BY) license (https:// chrysosporium and is also found in many bacteria and white-rot fungi (WRF) [11–14]. There creativecommons.org/licenses/by/ are different MnPs in nature with differentiated properties. For example, long and short 4.0/). Molecules 2021, 26, 4403. https://doi.org/10.3390/molecules26154403 https://www.mdpi.com/journal/molecules Molecules 2021, 26, 4403 2 of 15 MnPs were reported in WRF associated with the presence/absence of the C-terminal tail ex- tension, and these showed different catalytic and stability properties [15]. According to the residues of the Mn2+-binding site, three novel subfamilies of MnP were described in Agari- cales including MnP-ESD (Glu/Ser/Asp Mn2+-oxidation site), MnP-DGD (Asp/Gly/Asp Mn2+-oxidation site), and MnP-DED (Asp/Glu/Asp Mn2+-oxidation site) [16]. However, the Mn2+-binding site is not the unique feature of MnPs, because versatile peroxidases (VPs), which evolved directly from MnPs, also possess such a site and can oxidize Mn2+ to Mn3+ [17]. For enzyme applications, MnPs can catalyze the peroxide-dependent degradation of a variety of toxic dye pollutants, phenolic compounds, antibiotics, and polycyclic aromatic hydrocarbons, so are promising biocatalysts for hazardous environmental contaminants biodegradation [18,19]. Moreover, the use of MnPs is suitable for dye wastewater decol- orization as the process is simple and the enzyme can be recycled, thus reducing operating costs [20–22]. This review article summarizes the latest application of MnPs for wastewater dye decolorization and its future development prospects and challenges. 2. The Crystal Structure of MnPs The crystal structure of an enzyme provides information on the catalytic mecha- nism and for potential in-depth design and transformation, and for realizing the green biotechnological use of enzymes [23–25]. The heme conformation of MnP is similar to that of lignin peroxidase (LiP) and is evolutionarily conserved [26]. In its resting-state form, MnP is a strongly helical protein containing a Fe3+ penta-coordinated structure with the porphyrin ring of the heme cofactor and a proximal histidine, with the sixth coordination position open for H2O2 [27]. To date, several crystal structures of MnP from different sources have been reported, and the highest-resolution crystal structures (~0.93Å) of MnP complexed with Mn2+ (Mn- MnP) are shown in Figure1[ 28]. The conserved Ca2+ ions are important for the stability of the protein [29]; these are indicated as gold yellow spheres and the position of the Mn2+ substrate is shown in violet. The active site is composed of three highly conserved amino acids (Glu35, Glu39, and Asp179) and one heme propionate. The Mn2+ substrate binds in the center of the active site, and the heme propionate (HEM) is located in the internal hydrophobic cavity of the enzyme. The spatial structure of HEM is further stabilized by four hydrogen bonds (green dashed line), two electrostatic interactions (orange dashed line), and some other weak interactions. The catalytic site of heme peroxidases is strongly conserved, with only minor variations occurring in the replacement of Phe with Trp in several enzymes such as ascorbate peroxidase and cytochrome c. The Asp–His pair (242 and 173, respectively) is also conserved. Molecules 2021, 26, 4403 3 of 15 Molecules 2021, 26, x 3 of 15 E39 E35 2+ B D179 A His46 C Phe45 Arg42 Ca2+ E39 E35 Mn2+ D179 C a 2+ His173 Asp242 Phe190 M13 I41 D 2+ F45 R42 D179 F269 S172 R177 A176 L169 K180 F190 P142 V81 I151 P144 L129 FigureFigure 1. 1.The The overalloverall structure structure ( A(A),), active active site site structure structure (B (B,C,C),), and and interaction interaction mode mode (D (D) of) of Mn–MnP Mn– MnP refined at 0.93 Å resolution [28]. PDB ID: 3M5Q. refined at 0.93 Å resolution [28]. PDB ID: 3M5Q. 3.3. MnPMnP CatalysisCatalysis AtAt thethe beginningbeginning of of the the catalytic catalytic cycle, cycle, H H2O2O22 oror organicorganic peroxideperoxide binds binds to to the the enzyme enzyme 3+3+ inin resting resting state state in in ferric ferric (Fe (Fe )) formform (Figure(Figure2 ).2). This This process process releases releases one one molecule molecule of of H H2O2O andand formsforms MnP–compound MnP–compound I I (Fe (Fe4+4+-oxo-porphyrin-oxo-porphyrin radicalradical complex),complex), withwith twotwo oxidation oxidation equivalents. This oxidizes Mn2+ to Mn3+, forming MnP–compound II (Fe4+-oxo-porphyrin Molecules 2021, 26, 4403 4 of 15 Molecules 2021, 26, x 4 of 15 equivalents. This oxidizes Mn2+ to Mn3+, forming MnP–compound II (Fe4+-oxo-porphyrin complex).complex). Immediately Immediately afterwards, afterwards, the the MnP–compound MnP–compound II combinesII combines with with Mn Mn2+ in2+ ain similar a simi- 3+ mannerlar manner to generate to generate Mn Mn, releasing3+, releasing one one molecule molecule of of H 2HO,2O, and and is is reduced reduced to to the the original original statestate of of ferric ferric MnP, MnP, completing completing the the catalytic catalytic cycle cycle [30 [30].]. FigureFigure 2. 2.The The MnP MnP catalytic catalytic cycle cycle [ 30[30].]. TheThe MnP MnP catalytic catalytic cycle cycle resembles resembles that that of of other other lignin lignin and and heme heme peroxidases peroxidases in in the the presencepresence of of native native Fe Fe3+3+ enzymesenzymes andand twotwo reactivereactiveintermediates intermediates [ 31[31].]. However, However, in in contrast contrast 2+ toto other other peroxidases, peroxidases, MnP MnP preferentially
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