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Laccase-Catalyzed Decolorization of Malachite Green: Operation Optimization and Deposition Mechanism

• Jie Yang,
• Xiaodan Yang,
• Yonghui Lin,
• Tzi Bun Ng,
• Juan Lin,
• Xiuyun Ye

x

• Published: May 28, 2015
• https://doi.org/10.1371/journal.pone.0127714

Figures

Abstract

Malachite green (MG) was decolorized past laccase (LacA) of white-rot fungus Cerrena sp. with strong decolorizing ability. Decolorization conditions were optimized with response surface methodology. A highly significant quadratic model was adult to investigate MG decolorization with LacA, and the maximum MG decolorization ratio of 91.half-dozen% was predicted nether the conditions of 2.eight U mL^-1 LacA, 109.9 mg 50^-i MG and decolorization for 172.iv min. Kinetic studies revealed the Kk and 1000cat values of LacA toward MG were 781.ix mM and 9.5 southward^-ane, respectively. UV–visible spectra confirmed degradation of MG, and the degradation mechanism was explored with liquid chromatography–mass spectrometry (LC-MS) analysis. Based on the LC-MS spectra of degradation products, LacA catalyzed MG degradation via two simultaneous pathways. In addition, the phytotoxicity of MG, in terms of inhibition on seed germination and seedling root elongation of Nicotiana tabacum and Lactuca sativa, was reduced subsequently laccase treatment. These results suggest that laccase of Cerrena was effective in decolorizing MG and promising in bioremediation of wastewater in food and aquaculture industries.

Citation: Yang J, Yang X, Lin Y, Ng TB, Lin J, Ye Ten (2015) Laccase-Catalyzed Decolorization of Malachite Green: Operation Optimization and Degradation Machinery. PLoS ONE 10(v): e0127714. https://doi.org/10.1371/journal.pone.0127714

Academic Editor: Kristiina Hildén, University Of Helsinki, FINLAND

Received: Nov 20, 2014; Accustomed: April 17, 2015; Published: May 28, 2015

Copyright: © 2015 Yang et al. This is an open admission article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted utilise, distribution, and reproduction in any medium, provided the original author and source are credited

Information Availability: All relevant data are within the newspaper.

Funding: The work was funded by grants from Natural Scientific discipline Foundation of People's republic of china (41306120), Oceanic Public Welfare Industry Special Research Projection of Red china (2013418015), Fujian Provincial Development and Reform Commission Bio-industry Special Projection ([2011]1598), Fuzhou Science and Technology Bureau (2012-1000-125) and the Foundation of Central Laboratory of Yangtze River H2o Environment, Ministry of Teaching (Tongji University), Communist china, (No. YRWEF201506). The funders had no role in study pattern, data drove and assay, decision to publish, or preparation of the manuscript.

Competing interests: The authors have declared that no competing interests exists.

Introduction

Malachite green (MG) is a triphenylmethane dye used in aquaculture to control protozoan and fungal infections of farmed fish. MG is also used in nutrient, medical and textile industries. MG is readily absorbed by fish and reduced to leucomalachite green (LMG), a colorless, toxic metabolite [1–3]. MG is environmentally persistent; MG and LMG can accumulate in fish tissues. MG has a wide toxicity spectrum covering microorganisms and college eukaryotes [i,4]. Its toxic effects include organ amercement, impaired growth and reproduction, developmental abnormalities and mutagenic/carcinogenic potentials [iii,5]. Furthermore, the dye effluent can be disposed of untreated into water bodies and be used for agronomics, thereby affecting soil fertility [vi]. Although banned in many countries, MG is still used in many areas worldwide due to its efficacy, low cost and availability and thereby continues to pose threats to the environs, food prophylactic and human health. Concrete and chemical methods of MG removal have been proposed, such equally adsorption [7] and photodegradation [8,9]. These processes are often ineffective, not economically feasible and tin can cause secondary pollution. On the other hand, biodegradation has shown promise in MG treatment [10,11]. Triphenylmethane reductase and cytochrome P450 mediate MG reduction to LMG [five,12–14]. Therefore, enzyme-catalyzed MG oxidation without forming LMG derivatives is desired for MG decolorization and detoxification [2,4,15–21].

White rot fungi are constructive lignin degraders by secreting ligninolytic enzymes including lignin peroxidases (EC 1.11.1.14), manganese peroxidases (EC 1.11.ane.13) and laccases (EC 1.10.three.ii) [22]. All these enzymes tin can degrade MG, and the specific enzyme in activeness depends on the fungus [21]. Laccases have attracted much research interest because they are environmental friendly and can oxidize a wide variety of phenolic and not-phenolic compounds. Belonging to the family unit of multicopper enzymes, laccases incorporate four (i type ane, one type 2 and 2 type 3) copper atoms per molecule and catalyze one-electron oxidation of substrates concomitant with four-electron reduction of molecular oxygen to water [22,23]. Laccase have of import applications in various processes such every bit dye decolorization and detoxification, wastewater treatment and bioremediation [24]. The substrate range of laccases can be further expanded with small molecular weight mediators, such equally 2,2'-azino-bis (3-ethylbenzothiazoline-six-sulfonate) (ABTS) and 1-hydroxybenzotriazole (HBT). The laccase/mediator system tin can facilitate the oxidation pathway; different radicals may be formed, depending on whether a mediator is involved or non [22,25–28].

In search of efficient laccase producers to promote industrial applications of laccases, we isolated a novel white rot fungus Cerrena sp. strain HYB07 with high laccase yield and potent decolorization ability towards structurally different dyes, such as MG [29]. In the nowadays work, a major laccase produced past HYB07, namely LacA, was used to decolorize MG in the absenteeism of a mediator. Response surface methodology (RSM) was adopted to optimize decolorization conditions with respect to dye concentration, enzyme activity and reaction fourth dimension. The degradation products were identified with liquid chromatography–mass spectrometry (LC-MS), and a novel degradation model of MG was proposed.

Materials and Methods

Chemicals and organism

MG and ABTS were purchased from Sigma-Aldrich. All reagents were of analytical course. The white rot mucus Cerrena sp. strain HYB07 was maintained on potato dextrose agar slants at four°C and stored in the culture collection of College of Biological Sciences and Applied science, Fuzhou University, China.

Enzyme production and purification

Fermentation of Cerrena sp. H'YB07 was carried out in potato dextrose broth supplemented with 0.5% yeast excerpt and 0.iv mM CuSO₄. After iii d, the fermentation broth was harvested, diluted in 25 mM Tris-HCl buffer (pH 7.5) and applied to a HiTrap DEAE FF cavalcade (GE Healthcare). Adsorbed proteins were eluted with a linear gradient of 0–1 M NaCl in 25 mM Tris-HCl buffer (pH 7.5). Fractions with laccase activity were collected and checked past SDS-PAGE. The major laccase produced by HYB07, LacA (GenBank accession number KF317949) [29], was purified to electrophoretic homogeneity. The specific action of LacA was 1952.4 U mg^-1. The enzyme action assay was carried out in a citrate-phosphate buffer (l mM, pH 3.0) at 45°C, and oxidation of ABTS was monitored spectrophotometrically at 420 nm (ε = 36,000 M^-1 cm^-1) for five min [29]. Ane unit of measurement of enzyme activity was divers equally the amount of laccase required to oxidize 1 μmol ABTS per min.

MG decolorization

The absorbance tiptop of MG was determined to be 614 nm by UV-visible assay. Purified LacA was used to decolorize MG at 28°C in an incubator (ZXSD-1270, LABWIT Scientific, Shanghai, Prc) in the dark. The 4 mL reaction mixture contained 50 mM citrate-phosphate buffer (pH 6.0), dye and laccase. Decolorization efficiency was monitored at 614 nm with a UV-Vis spectrophotometer (U-2910, Hitachi, Japan) and calculated according to the post-obit formula: Where D is the decolorization efficiency (%), A₀ is MG assimilation before LacA handling, and A_i is the residual MG assimilation subsequently LacA treatment.

Performance optimization of MG decolorization by RSM

Central blended blueprint (CCD) was chosen for the optimization of MG decolorization process past LacA. Iii independent variables, namely LacA concentration (Ten ₁), dye concentration (X ₂) and time (X _three) were evaluated at five levels (Table 1), and the percentage of MG decolorization was the dependent variable (response). The following equation was used to establish the quadratic model: where Y is the predicted response; X _ane, Ten ₂ and X _iii are the coded factors; β ₀ is a constant coefficient; β ₁, β _ii, β ₃ are the linear coefficients; β ₁₁, β ₂₂, β ₃₃ are the quadratic coefficients; β ₁ β ₂, β _i β _three, β ₂ β _three are the interactions of the coefficients.

Design-Proficient version 8.0 (Stat-Ease Inc., Minneapolis, U.s.) was used for experimental design and statistical analysis. Validation of the optimum decolorization results predicted by the model was conducted in triplicate.

Kinetic written report

Substrate specificity of LacA for MG was determined with nonlinear regression of the Michaelis-Menten equation past using GraphPad Prism version 5.0 (GraphPad Software, Inc., USA). The iv mL reaction consisted of MG (twenty, 50, 80, 100, 200, 300, 500, chiliad and 2000 mg L^-1), LacA (3 U mL^-1) in fifty mM citrate-phosphate buffer (pH 6.0). All experiments were performed in triplicate.

Identification of degradation products

For LC-MS, MG decolorization was performed at 25°C in water instead of buffer. Aliquots (2 μL) were injected into an HPLC system (Agilent 1200 Series, equipped with a Phenomenex Luna C-18 analytical column of two.0 mm x 150 mm length and 3 μm particle size) coupled with Agilent 6224 Accurate-Mass Time of Flight (TOF) MS. The compounds were resolved past using solvent A: 5 mM ammonium acetate supplemented with 0.5% formic acid and solvent B: acetonitrile. The menses rate was kept at 0.2 mL min^-1. A linear gradient was set as follows: t = 0–2, A = 95; t = 4–five, A = forty; t = 7–11, A = 10; t = 12–fifteen, A = 95. The cavalcade effluent was introduced into the electrospray ionization source of the mass spectrometer in positive ion way. The MS parameters were as follows: capillary voltage 3.five kV; nebulizer pressure 50 psi; drying gas flow 11 L min^-1; drying gas temperature 360°C; fragmentor voltage 130 V. LC-TOF MS authentic mass spectra were recorded across the range 70–400 m/z. Data processing was carried out with Applied Biosystems/MDS-SCIEX Analyst QS software (Frankfurt, Germany) with accurate mass application-specific additions from Agilent MSD TOF software. Accurate-mass internal mass calibration was performed automatically using a dual-nebulizer ion source. The reference masses were 121.0509 m/z and 922.0098 m/z.

Phytotoxicity study

Toxicity of MG before and after LacA decolorization was assayed with Nicotiana tabacum and Lactuca sativa with respect to seed germination and seedling root (radical) elongation. The seeds were placed in petri dishes (at least 30 seeds each plate) on filter paper pre-wet with MG solution (100 mg L^-1) before and after LacA treatment. The petri dishes were sealed with parafilm and stratified at four°C in the dark for 3 d to promote synchronous seed germination. The plates were so transferred to a plant growth chamber (PRX-250B, Saife Instruments, Ningbo, China) at 22°C. Distilled water was used equally the control. Formation rate and root length were determined afterwards 7 d. Radical emergence was used to determine formation; radical growth was measured by using the Image-Pro software (Media Cybernetics, San Diego, CA, USA).

Results and Discussion

Operation optimization of MG decolorization past LacA

Since the enzyme-mediated decolorization process is influenced by parameters such as dye concentration, enzyme activity and decolorization fourth dimension, optimization of LacA-mediated MG decolorization was carried out. RSM is a statistical technique for optimization of multiple variables to achieve the best performance conditions with fewest possible experiments. CCD was chosen to determine the optimum requirement of enzyme (X _one), dye (X _ii), and time (Ten ₃) for maximum dye decolorization (Table 1). The mathematical expression of the relationship to MG decolorization with the variables X ₁, X ₂ and Ten _iii is as follows:

ANOVA of the regression model demonstrated a high significance (P < 0.0001) of the model and an insignificant lack of fit (Table 2). The conclusion coefficient R² was 0.9581, and adjusted Rⁱⁱ (Adj-Rⁱⁱ) was 0.9204. Adequate precision, a measure out of the signal to noise ratio, was 15.93, indicating an adequate indicate. Variables 10 ₁, X _iii, Ten ₁ ² and X ₃ ² were pregnant model terms. Interactions betwixt the studied variables for dye decolorization are shown in 3D surface plots (Fig i).

The optimum levels of coded variables for maximum decolorization (91.64%) were predicted equally X _one = 0.763, X _ii = 0.199 and X ₃ = 0.874. These values correspond to LacA = 2.76 U mL^-1, MG = 109.93 mg L^-1 and time = 172.44 min. Experimental validation (LacA = ii.8 U mL^-1, MG = 110 mg 50^-1 and time = 172 min) was carried out using the optimized variables identified by RSM, and a decolorization efficiency of 89.88% with a 3.23% experimental mistake was obtained, which was shut to the predicted value of 91.64%. The adept correlation between the predicted and actual optimized decolorization efficiencies verified the validity of the response model.

CCD has been successfully practical for modeling and optimization of biological decolorization processes of dyes including reactive blackness 5 [30,31], Remazol Brilliant Blue R [32] and indigo carmine [xxx]. In these CCD studies, HBT is the most frequently used laccase mediator in order to achieve high decolorization efficiencies. For example, a maximum decolorization efficiency of approximately 96% was predicted with the conditions of 95.80 mg 50^-1 MG, 2.16 U mL^-one partially purified laccase from Pleurotus florida, 0.85 mM HBT and 3.02 h at pH 6.0 and 37 °C [xx]. Despite the efficacy of laccase mediators in enhancing dye decolorization, they add processing costs and can have adverse impacts on the enzyme activity or the environment [15,sixteen,28]. In our hands, at the same pH value of 6.0 as previous work [20], a similarly loftier decolorization efficiency was attained in the absence of a mediator at 28°C, demonstrating the potential and benefits of LacA in industrial applications. LacA was also efficient and eco-friendly compared with a recombinant manganese peroxidase isozyme H4, the latter decolorized 100 mg Fifty^-1 MG to a degree of 72% with MnSO₄ and hydrogen peroxide [33].

Kinetic study

The kinetic parameters of LacA-mediated MG decolorization were estimated from nonlinear regression of the Michaelis-Menten equation. The 1000 _thousand and 1000 _cat values were 781.9 mM and 9.5 s^-ane, respectively. Therefore, LacA had lower analogousness as well every bit turnover charge per unit for MG than for ABTS (93.4 μM and 2468.0 south^-one) [29]. The Grand _thousand value (781.9 mM) was also greater than that of a triphenylmethane reductase from Citrobacter sp. Strain KCTC 18061P (0.53 mM); the reductase converts MG to LMG [12].

LC-MS analysis of MG degradation products

UV-visible spectra of the MG solution showed non simply disappearance of the major peak of MG absorbance at 614 nm, but besides two pocket-size peaks at 315 nm and 425 nm, respectively, after LacA treatment (Fig 2), implying that decolorization was a upshot of biodegradation. This was confirmed past LC-TOF MS analysis. MG (1000/z 329.20) concentration significantly decreased with LacA decolorization (Fig three). Furthermore, unlike MG transformation with fungi Cunninghamella elegans [5], Penicillium pinophilum and Myrothecium roridum [13] or leaner Exiguobacterium sp. [fourteen] and Citrobacter sp. [12], in LacA-mediated MG degradation, reduction of MG to LMG was not detected.

Development of a feasible decolorization scheme requires identification and evaluation of toxicity/mutagenicity of the major and stable products of the process [ten,11,18]. Here, LC-TOF MS identified seven intermediates of LacA-catalyzed MG transformation (Fig 4). Amidst these intermediates, tetradesmethyl MG (m/z 273.14), (methyl aminophenyl)-phenyl-methanone (m/z 212.11) and (amino phenyl)-phenyl methanone (k/z 198.09) were more persistent products but diminished after prolonged incubation (eastward.m., overnight incubation).

Fig iv. The mass spectra of MG and its degradation products.

(A) MG, m/z 329.20 (retentiveness fourth dimension 7.23 min). (B) desmethyl MG, m/z 315.eighteen (retentiveness time 7.01 min). (C) didesmethyl MG, m/z 301.17 (retention fourth dimension 6.84 min). (D) tridesmethyl MG, m/z 287.16 (retention time vi.65 min). (Due east) tetradesmethyl MG 1000/z 273.14 (retention time half dozen.53 min). (F) (dimethyl amino-phenyl)-phenyl-methanone, m/z 226.12 (retentivity fourth dimension 9.xiv min). (Thou) (methyl amino-phenyl)-phenyl-methanone, g/z 212.xi (retentiveness time 8.48 min). (H) (amino phenyl)-phenyl methanone, m/z 198.09 (retention time 7.80 min).

https://doi.org/10.1371/journal.pone.0127714.g004

LacA-mediated MG degradation

Based on the intermediates identified also equally previous studies on MG deposition, we proposed a model for LacA-mediated MG degradation consisting of 2 parallel and competing deposition pathways (Fig 5). Pathway I started with successive N-demethylation of MG, similar to proposed pathways of MG breakup catalyzed by a laccase [16,xviii]. It is noteworthy that Northward-demethylation (i.e., complete conversion of MG to desmethyl MG, didesmethyl MG and tridesmethyl MG) does not event in MG decolorization. Further degradation or polymerization must occur to destroy the chromophore [16].

Besides pathway I, LacA besides mediated MG degradation via a second pathway (pathway Two). In this pathway, MG was first hydroxylated to its carbinol form [34], which was quickly broken down at the bond between the key carbon atom and the N,North-dimethylamino phenyl band into (dimethyl amino-phenyl)-phenyl-methanone and N,N-dimethylaniline. (dimethyl amino-phenyl)-phenyl-methanone was and so sequentially Northward-demethylated to (amino phenyl)-phenyl methanone. This pathway has not been previously reported for MG transformation catalyzed by only laccase (without a mediator), although it is the pathway of choice in the presence of a laccase mediator [18].

Simultaneous presence of both pathways in our model probably contributed to fast and efficient degradation of MG and could be accounted for by the speculated high redox potential of LacA. Bioinformatics analysis suggests that LacA is a loftier-redox-potential laccase, considering that three amino acids, namely Ser113, Glu456 and Phe459, conserved among fungal laccases with high redox potentials, were also present in LacA [23,35].

Reported fungal laccases take various redox potentials ranging from 400 to 800 mV, which are normally higher than those of institute laccases and other blue copper oxidases [22]. The efficiency of substrate oxidation past a laccase depends on the difference between the redox potentials of the substrate and the type 1 Cu. Oxidation of substrates with redox potentials college than those of laccases, such equally non-phenolic compounds, tin be facilitated by electron transfer mediators. A laccase mediator oxidized get-go by a laccase tin in plow oxidize non-phenolic substrates, thus enhancing the performance and efficiency of the laccase. For case, after oxidation past a laccase, di-cation ABTSⁱⁱ⁺ has a redox potential of 885 mV and oxidizes the substrate via an electron transfer route. In contrast, some other synthetic mediator HBT or natural phenolic mediators follow a hydrogen atom transfer mechanism [22]. Laccase/mediator oxidation of the substrate may proceed differently from laccase oxidation of the substrate without a mediator [22,26–28]. Indeed, based on absorbance maximum changes, Papinutti and Forchiassin proposed that the machinery of MG modification by Fomes sclerodermeus laccase is different when HBT is added [25]. Afterwards, Chhabra et al. identified ii independent, mutually exclusive degradation pathways of MG by laccase in the presence and absence of a mediator. With the laccase/ABTS arrangement, MG is hydroxylated and cleaved down (pathway II), while laccase alone initiates MG transformation with stepwise N-demethylation (pathway I) [eighteen]. This was non the case in our analysis; MG deposition with LacA or LacA/ABTS rendered identical intermediates from both pathways.

Phytotoxicity study

Toxicity of MG solution earlier and afterward LacA handling was evaluated with Nicotiana tabacum and Lactuca sativa in terms of seed formation and seedling root elongation (Table 3). While consummate germination was observed in the water control, MG inhibited germination of both Nicotiana tabacum and Lactuca sativa seeds past 36% and 75%, respectively. Decreased seedling root elongation by MG was also observed, and the average seedling root length in MG was approximately only 30% of that in the water control. After LacA-mediated deposition, inhibition of MG on seed germination was eliminated, and MG inhibition on root elongation was alleviated. Incomplete restoration of radical length indicated that compared to germination, seedling root elongation was more sensitive to residual MG metabolites present afterward LacA-catalyzed decolorization. Similar to our phytotoxicity examination results, MG impaired seed formation and root elongation rates of Phaseolus mungo and Triticum aestivum, and MG degradation by laccase from bacteria Kocuria rosea [36] or white-rot mucus Pleurotus ostreatus [19] resulted in products with lower toxicity on plant growth. Du et al. have reported complete and partial emptying of germination inhibition for Lucerne (Medicago sativa Linn.) and Chinese cabbage (Brassica chinensis Linn.) seeds, respectively, after MG removal with Pseudomonas sp. strain DY1 for 12 h [37]. Seedling root length of both establish species in treated MG solution was as well partially restored to the level of the water command [37]. Reduction of phytotoxicity of other dyes, such as RBBR [32] and Cherry-red BLI [6], upon enzymatic decolorization has also been described, and incomplete reversion of root elongation in treated dye solutions are often observed.

Conclusions

MG decolorization past a novel laccase, LacA, was optimized with CCD to achieve a maximum decolorization efficiency of 91.64% in the absence of a laccase mediator. Based on the intermediates identified by LC-MS, LacA catalyzed MG transformation via ii separate, co-existing pathways, likely owing to the high redox potential of the enzyme and contributing to effective decolorization and deposition of MG. Accompanying decolorization, LacA reduced toxicity of MG. LacA is a promising candidate for applications in MG removal as well as bioremediation of nutrient and aquaculture wastewater.

Author Contributions

Conceived and designed the experiments: JY JL Ten. Ye. Performed the experiments: JY X. Yang YL. Analyzed the information: JY TBN 10. Ye. Contributed reagents/materials/analysis tools: JY YL JL. Wrote the paper: JY TBN X. Ye.

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Source: https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0127714

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