Decolorization Of Industrial Dyes Research Articles

AND logic gate supported novel speckled phosphorus-doped carbon dots decorated ZrO2/CaO/MgO sonocatalysts for efficient MB dye decolorization

Textile dyes are significant contributors to aquatic pollution in developing nations, and also the current pace of human-caused contamination of worldwide freshwater bodies is frightening. Herein, we report the sonocatalytic decolorization of the methylene blue (MB) dye using a novel synthesis of composite materials of zirconium oxide (ZrO2), calcium oxide (CaO), and magnesium oxide (MgO) nanoparticles (NPs) decorated by phosphorus-doped carbon dots (PCDs). The monoclinic phase of ZrO2 has shown the highest catalytic activity, thus imparting greater decolorization efficiency (DE) in the synthesized metal oxide nanoparticles (MONPs) decorated with PCDs (MONPs@PCDs). The sonocatalytic efficiency of MONPs@PCDs was evaluated using MB as the analyte molecule. We report DE of up to 99.54% via speckled PCDs decoration and synergistic effect in a short time of 30 min at just 20 kHz frequency. The sonocatalytic activity of MONPs@PCDs is AND logic gate supported and was found as ZCMO@PCDs (99.54%) > ZMO@PCDs (96.47%) > ZO@PCDs (94.68%) > ZCO@PCDs (93.40%). However, the sonocatalytic activity of MONPs was only ZCMO (11.21%) > ZMO (9.26%) > ZO (3.79%) > ZCO (2.92%), under identical experimental conditions. The synergistic effect in polymetallic systems opens new pathways to be explored in sonocatalysis. We confirmed the synthesis of PCDs and their speckled decoration on the surface of MONPs using scanning electron microscopy (SEM), and transmission electron microscopy (TEM). The speckled nanocomposites, i.e., MONPs@PCDs, showed an enhanced and faster decolorization efficiency than the bare MONPs, as demonstrated by the kinetics studies as 101 fold increase in k values and 101 fold decrease in t1/2 values. Novelty statementNovel nanocomposites have been developed for MB dye decolorization using a low frequency of just 20 kHz and possessing 99.54–93.40% DE in only 30 min, thus may aid in industrial dye decolorization and the reuse of wastewater for environmental sustainability.

Textile Dye Decolorization Ability of Decaying Hardwood Associated Fungi

Random disposal of synthetic textile dyes has created severe damage to the environment. These dye effluents, even at very low concentrations, can be toxic, mutagenic and carcinogenic to various organisms. Complex chemical structures enable the textile dyes to remain stable and inert towards degradation in soil and water. Therefore, textile dye decolorization has gained special attention in the recent past. Biological means of dye decolorization have become one of the attractive decolorization methods. Fungi show a great potency in decolorizing a wide variety of dyes by secreting highly oxidative and nonspecific ligninolytic enzymes such as laccases. The main aim of the current study was to evaluate the dye decolorization abilities of selected fungal isolates associated with decaying hardwoods in Sri Lanka. A total of 10 wood decay fungal isolates were screened for the laccase production and lignin degradation using guaiacol and lignin powder amended media respectively. Phlebiopsis flavidoalba, Phanerochaete chrysosporium, P. pseudomagnoliae and two Schizophyllum commune strains showed both laccase production as well as lignin degradation abilities. Although unable to produce laccases, Fusarium pseudensiforme and Aspergillus fischeri showed lignin degradation ability. Azo Disperse Rubine Red, Indigo Carmine Blue and Disperse Black were selected as textile dyes. Three replicates from each isolate were incubated for 21 days in potato dextrose broth amended with each dye in two concentrations, and percentage reduction in absorbance at 610 nm (for the Indigo Carmine Blue dye) and 400 nm (for Azo Disperse Rubine Red and Disperse Black) were estimated. Dye introduced potato dextrose broth, without fungal isolates were used as controls. P. flavidoalba was the best in decolorizing Azo Disperse Rubine Red (25 mg/L) and Disperse Black (50 mg/L) dyes showing the reduction of absorbance values by 89% and 81% respectively. For the Indigo Carmine Blue dye, F. pseudensiforme showed the highest percent decolorization of 85% at 0.1 ml/L concentration. This is the first report of these organism's ability to decolorize industrial dyes. Based on the results it was evident that some of the hardwood decay fungi have industrial dye decolorization abilities where they can be effectively utilized in dye decolorization and in future bioremediation research as well.
 Keywords: Dye decolorization, Laccase, Wood decay, Fungi, Lignin
 Acknowledgement: Authors acknowledge the TWAS Research Grant 18-020 RG/BIO/AS_I, NSF Sri Lanka RG/2019//BT/03 and ICGEB/CRP/LKA/18-3

Novel biocatalyst from Microthielavia ovispora VKM F-1735 for industrial dye decolorization in the absence of mediators

The new ascomycete Microthielavia ovispora VKM F-1735 has been found to produce oxidases with laccase activity capable to decolorize many industrial dyes in the absence of any mediators. The optimal conditions of submerged cultivation of the fungus for production of the oxidases decolorizing dyes were developed. Two unusual homodimeric oxidases with laccase activity and different physicochemical properties could be purified from the fungal culture liquid. The purified oxidases possessed individual selectivity in relation to different laccase substrates. The oxidases I and II (147 and 160 kDa, respectively) were most active under acidic conditions at elevated temperatures of 64 and 66 °C, correspondingly. The activation phenomena for the fungal oxidases during incubation in the presence of nonionic surfactants or K+ and Co2+ ions was shown. The dynamics of decolorization of malachite green in various concentrations by the fungus oxidases was studied. Based on the identified intermediates the scheme of the dye transformation by the oxidases has been presented. Being a non-toxic protein component exhibiting the decolorizing activity against a wide range of industrial dyes without additional expensive mediators, the M. ovispora VKM F-1735 oxidase has great potential for the development of new effective “green” technologies for bioremediation of water resources and soils.

Synergetic decolorization of azo dyes using ultrasounds, photocatalysis and photo-fenton reaction

In the present work, ultrasound irradiation, photocatalysis with TiO2, Fenton/Photo-Fenton reaction, and the combination of those techniques were investigated for the decolorization of industrial dyes in order to study their synergy. Three azo dyes were selected from the weaving industry. Their degradation was examined via UV illumination, Fenton and Photo-Fenton reaction as well as ultrasound irradiation at low (20 kHz) and high frequencies (860 kHz). In these experiments, we investigated the simultaneous action of the ultrasound and UV irradiation by varying parameters like the duration of photocatalysis and ultrasound irradiation frequency. At the same time, US power, temperature, amount of TiO2 photocatalyst and amount of Fenton reagent remained constant. Due to their diverse structure, each azo dye showed different degradation levels using different combinations of the above-mentioned Advanced Oxidation Processes (AOPs). The Photo-Fenton reagent is more effective with US 20 kHz and US 860 kHz for the azo dyes originated from the weaving industry at pH = 3 as compared to pH = 6.8. The combination of the Photo-Fenton reaction with 860 kHz ultrasound irradiation for the same dye gave an 80% conversion at the same time. Experiments have shown a high activity during the first two hours. After that threshold, the reaction rate is decreased. FT-IR and TOC measurements prove the decolorization due to the destruction of the chromophore groups but not complete mineralization of the dyes.

Bacterial laccase of Anoxybacillus ayderensis SK3-4 from hot springs showing potential for industrial dye decolorization

IntroductionLaccases are green biocatalysts that possess attractive for the treatment of resistant environmental pollutants and dye effluents.PurposeTo exploit the laccase of Anoxybacillus ayderensis SK3-4 that possesses dye decolorization ability at room and higher temperature, we characterized the enzyme in considerable detail and investigated its ability to decolorize different dyes.ResultsA bacterial laccase gene designed as LacAn from Anoxybacillus ayderensis SK3-4 of hot springs was cloned and expressed in Escherichia coli. LacAn is a monomeric protein with a molecular weight of 29.8 kDa. The optimum pH and temperature for syringaldazine oxidation were 7.0 and 75 °C, respectively. LacAn was stable at pH values ranging from 6.5 to 8.5 above 65 °C. The enzyme activity was significantly enhanced by Cu2+ and Mg2+ but inhibited by Zn2+ and Fe2+. Furthermore, LacAn showed high decolorization capability toward five dyes (direct blue 6, acid black 1, direct green 6, direct black 19, and acid blue 93) in the absence of redox mediators. It also demonstrated a wide temperature range, and it can retain its high decolorization ability even at high temperatures.ConclusionsThese properties including better enzymatic properties and efficiency to decolorize dyes demonstrate that the bacterial laccase LacAn has potentials for further industrial applications.

Role of microalgal ligninolytic enzymes in industrial dye decolorization

In this study, the decolorization efficiency of seven microalgae isolates; Nostoc muscorum, Nostoc humifusum, Spirulina platensis, Anabaena oryzae, Wollea saccata, Oscillatoria sp. and Chlorella vulgaris was investigated for dye decolorization. The highest decolorization percentages of Brazilwood, Orange G, and Naphthol Green B dyes (99.5%, 99.5%, and 98.5%, respectively) were achieved by Chlorella vulgaris. However, the maximum efficiency for dye decolorization percentages of CV and malachite green dyes were exhibited by A. oryzae (97.4%) and W. saccata (93.3%). Ligninolytic enzymes activity assay was carried out for laccase and lignin peroxidase enzymes, which revealed a high efficiency of the C. vulgaris, A. oryzae and W. saccata to lignin containing compound degradation. The highest laccase production recorded by C. vulgaris with Brazilwood, Orange G, and Naphthol Green B dyes (665.0, 678.6, and 659.5 U/ml, respectively). Similarly, C. vulgaris gave a high lignin peroxidase enzyme production with the above three dyes respectively (306.00, 298.34, and 311.45 U/ml). In addition, A. oryzae and W. saccata showed the highest production of the laccase enzyme (634.6 and 577.45 U/ml, respectively) with CV and malachite green dyes. The degradation products have been characterized after decolorization and verified using FTIR analysis. The high decolorization percentages achieved by C. vulgaris, A. oryzae and W. saccata make them potential candidates for bioremediation and pre-processing to remove dyes from textile effluents.

Screening of five marine-derived fungal strains for their potential to produce oxidases with laccase activities suitable for biotechnological applications

BackgroundEnvironmental pollution is one of the major problems that the world is facing today. Several approaches have been taken, from physical and chemical methods to biotechnological strategies (e.g. the use of oxidoreductases). Oxidative enzymes from microorganisms offer eco-friendly, cost–effective processes amenable to biotechnological applications, such as in industrial dye decolorization. The aim of this study was to screen marine-derived fungal strains isolated from three coastal areas in Tunisia to identify laccase-like activities, and to produce and characterize active cell-free supernatants of interest for dye decolorization.ResultsFollowing the screening of 20 fungal strains isolated from the harbors of Sfax and Monastir (Tunisia), five strains were identified that displayed laccase-like activities. Molecular-based taxonomic approaches identified these strains as belonging to the species Trichoderma asperellum, Stemphylium lucomagnoense and Aspergillus nidulans. Among these five isolates, one T. asperellum strain (T. asperellum 1) gave the highest level of secreted oxidative activities, and so was chosen for further studies. Optimization of the growth medium for liquid cultures was first undertaken to improve the level of laccase-like activity in culture supernatants. Finally, the culture supernatant of T. asperellum 1 decolorized different synthetic dyes belonging to diverse dye families, in the presence or absence of 1-hydroxybenzotriazole (HBT) as a mediator.ConclusionsThe optimal growth conditions to produce laccase-like active cell-free supernatants from T. asperellum 1 were 1.8 mM CuSO4 as an inducer, 1% NaCl to mimic a seawater environment and 3% sucrose as a carbon source. The culture supernatant of T. asperellum 1 effectively decolorized different synthetic dyes belonging to diverse chemical classes, and the presence of HBT as a mediator improved the decolorization process.

Isolation and characterization of an alkali and thermostable laccase from a novel Alcaligenes faecalis and its application in decolorization of synthetic dyes

A laccase producing new bacterial strain (Alcaligenes faecalis XF1) was isolated from green site of Chandigarh (India) by standard screening method. Nutrient broth medium containing 0.2 mM CuSO4 was used for the production of laccase. Maximum production (110 U/ml) was achieved after four days of incubation. The extracellular laccase from the medium was purified by simple salt precipitation and ion exchange technique to get 3.8 fold purified protein with 1637.8 U/mg specific activity. Purified laccase (named as LAC1*) revealed its optimum activity at pH 8.0 and 80 °C temperature, and displayed remarkable stability in the range of 70–90 °C and in the pH range (pH 7.0–9.0). The single bands on SDS-PAGE represents the purity of LAC1* with molecular weight of ∼71 kDa. The kinetic parameters for 2,6-DMP oxidation was Km, Vmax and kcat were 480 μM, 110 U/mL and 1375 s−1. Enzyme activity of the LAC1* was significantly enhanced by Cu2+, Mg2+, Mn2+, SDS and NaCl, and was slightly inhibited in the presence of conventional inhibitors like cysteine, EDTA and sodium azide. Extracellular nature and significant stability of LAC1* under extreme conditions of temperature, pH, heavy metals, halides and detergents confined its suitability for various biotechnological and industrial applications which required these qualities of laccase. So after recognizing all these properties the purified laccase was studied for its application in decolorization of industrial dyes.

Isolation and Investigation of the Effect of Soil and Textile Wastewater Bacteria on Decolorization of Industrial Dyes

Isolation and Investigation of the Effect of Soil and Textile Wastewater Bacteria on Decolorization of Industrial Dyes

Functional Hyper-Crosslinked Polypyrene for Reductive Decolorization of Industrial Dyes and Effective Mercury Removal from Aqueous Media.

A rigid and valuable hyper-crosslinked polymer (HCP) has been synthesized from the polycyclic aromatic hydrocarbon pyrene: hyper-crosslinked polypyrene (HCPPy). HCPPy was prepared through a simple one-step Friedel-Crafts alkylation reaction that involves ZnBr2 -catalyzed crosslinking in the presence of an external crosslinker, bromomethyl methyl ether (BME). Interestingly, the unreacted bromomethyl groups (-CH2 Br) on the surface of HCPPy could be quantified, which later aided in modification as per our requirement. We aimed at modifying with disulfide-containing cystamine dihydrochloride (Cys-HCPPy). Cys-HCPPy exhibited an extended π-conjugated system with uniform (∼1 μm diameter) morphology and high porosity (specific surface area: 445 m2 g-1 ). As a fundamental application, the Cys-HCPPy composite was used as a sorbent to remove Hg2+ ions from aqueous media. Thus, at pH 6, the adsorption capacity for mercury ions reached 1124.82 mg g-1 after 24 h. Furthermore, the immobilization of Ag nanoparticles on the surface of Cys-HCPPy (Ag@Cys-HCPPy) enhanced the catalytic properties, which allowed for the reductive decolorization of industrial dyes such as methylene blue, methyl orange, and Congo Red in the presence of NaBH4 as a reducing agent.

Surface Display of Bacterial Laccase CotA on Escherichia coli Cells and its Application in Industrial Dye Decolorization.

Laccase CotA from Bacillus subtilis 168 was successfully displayed on the membrane of Escherichia coli cells using poly-γ-glutamate synthetase A protein (PgsA) from B. subtilis as an anchoring matrix. Further analyses demonstrated that the fusion protein PgsA/CotA efficiently translocates to the cell surface of E. coli with an enzymatic activity of 65U/108 cells. Surface-displayed CotA was shown to possess improved enzymatic properties compared with those of the wild-type CotA, including higher thermal stability (above 90% activity at 70°C and nearly 40% activity at 90°C after 5-h incubation) and stronger inhibitor tolerance (approximately 80 and 65% activity when incubated with 200 and 400mM NaCl, respectively). Furthermore, the whole-cell system was demonstrated to have high enzymatic activity against anthraquinone dye, Acid Blue 62, triphenylmethane dye, Malachite Green, and azo dye, Methyl Orange with the decolorization percentages of 91, 45, and 75%, after 5-h incubation, respectively.

Kinetic and Enzymatic Decolorization of Industrial Dyes Utilizing Plant-Based Biosorbents: A Review

Abstract Biosorption is a widely used technology for wastewater treatment, especially for removal of pollutants that are not easily biodegradable. Plant-based agricultural wastes have gained attention as effective biosorbents due to their low cost, potential for waste reuse, and their adsorption characteristics. An extensive list has been compiled of plant materials (e.g., different parts of plants) used for biosorption of industrial dyes and for enzyme-assisted decolorization. The purpose of this review was to summarize the information available on (i) adsorption of industrial dyes on plant-based biosorbents, (ii) factors affecting adsorption processes, (iii) isothermal and kinetic modeling, (iv) thermodynamics, and (v) fungal enzymatic decolorization of dyes on lignocellulosic biomasses in biosorption studies. A wide variety of plant wastes, mainly agricultural residues, can be used for biosorption, and fungal enzymes can accelerate the decolorization process. These low-cost biosorbents have showed quan...

Decolorization of Industrial Dyes by an Extracellular Peroxidase from Bacillus sp. F31

Decolorization of Industrial Dyes by an Extracellular Peroxidase from Bacillus sp. F31

EPR and LC-MS studies on the mechanism of industrial dye decolorization by versatile peroxidase from Bjerkandera adusta.

The mechanisms of industrial dye transformation by versatile peroxidase were elucidated. Purified versatile peroxidase from Bjerkandera adusta was able to decolorize different classes of dyes including azo and phthalocyanines, but unable to transform any of the anthraquinones tested. Kinetic constants for selected dyes were determined and the transformation products were analyzed by EPR spectroscopy and mass spectrometry. The EPR and MS analyses of the enzymatic decolorization products showed the cleavage of the azo bond in azo dyes and the total disruption of the phthalocyaninic ring in phthalocyanine dyes. The EPR analysis on two copper-containing dyes, reactive violet 5 (azo) and reactive blue 72 (phthalocyanine), showed that the transformation can or not break the metal-ion coordination bond according the dye nature. The role of the catalytic Trp172 in the dye transformation by a long-range electron transfer pathway was confirmed and the oxidation mechanisms are proposed and discussed.

Ligninolytic Oxidative System of Fungal Egyptian Isolates and their Applications in the Decolorization of Industrial Dyes

ABSTRACTThe aim of this study was to investigate the ligninolytic system of fungal strains isolated from Egyptian agricultural soil which are efficient in biodegradation and mineralization of lignin. They were identified morphologically, microscopically and confirmed by RAPD profiles. Based on PCR amplification and sequencing of the 18S rDNA gene an analytical phylogenetic tree was drawn for species confirmation. The screening experiment revealed that Emericella nidulans, Aspergillus fumigatus, Phoma betae, Penicillium oxalicum and Humicola grisea exhibited maximum potential for high lignin degradation. They showed higher lignin peroxidase and laccase activities. By process optimization, enhanced lignin degradation (94%) was achieved within 7 days in lignin-glucose medium when compared with lignin degradation (70%) obtained in glucose-free medium. The ligninolytic enzymatic activities had a great potential for decolorization of chemically different synthetic dyes (Azure B, Safranin, Crystal Violet and Malachite Green). The highest enzymatic activities and the highest decolorization rates were detected at a dye concentration of 0.2 g/L. The dye decolorization rate significantly increased with tryptophan addition as (1 mmol/L). Humicola grisea showed the highest decolorization rate (99%) with azure B. Phoma beta also showed a high decolorization rate (99% with crystal violet and 90% with safranin). The observed activity enhancement resulted from the protective effect of tryptophan against H2O2 inactivation.

Decolorization of Industrial Dyes by Immobilized Mycelia of Trametes Versicolor

ABSTRACTThe aim of this study was to compare the decolorization of several of the most utilized synthetic dyes in textile applications by immobilized white-rot fungus Trametes versicolor. Different immobilization methods for achieving maximum decolorization were explored. The initial dye concentration was 125 mg/L and the immobilized preparation concentration was 10% (w/v). Different degrees of decolorization were observed. Different operational stability of the immobilized preparations was accomplished. Increase of the immobilized preparation concentration up to 30% (w/v) was investigated. The study was performed in two stages: simulated incubation in a ‘batch’ reactor and trickle-bed continuous flow reactor During the decolorization process, laccase activity was detected. The dye-decolorizing activity of the immobilized culture was found to be associated with the processes of biodegradation, bio-oxidation and biosorption.

Biological decolorization of industrial dyes by Candida tropicalis and Bacillus firmus

Disperse dyes are chiefly used by textile industries for the coloration of polyester and cellulose triacetate and their blended fibres. Their extensive use and recalcitrant nature, high tinctorial strength renders the voluminous textile effluents intensively colored and causes environmental concerns. Decolorization of representative members of Dianix CC and Dianix S brands (DyStar Pvt. Ltd.) of disperse dyes were tested with Candida tropicalis and Bacillus firmus isolated respectively from contaminated soil samples and sludge of a domestic sewage drain. While both the cultures efficiently remove color from the aqueous solutions of the dyes, the yeast culture was found to decolorize most of the tested disperse dyes through biotransformation, the bacterial culture showed color removal mainly by adsorption on the cell pellets. Formation of cleavage products such as p-nitroaniline was observed in the case of Dianix Orange E-3R, indicating reductive cleavage of the azo linkage of the dye.

Efficient industrial dye decolorization by Bacillus sp. VUS with its enzyme system

This work presents role of different enzymes in decolorization of industrial dye Orange T4LL by Bacillus sp. VUS. Bacillus sp. strain VUS decolorized dye Orange T4LL, under static anoxic condition in 24 h. During decolorization of Orange T4LL a significant induction in the activities of lignin peroxidase, tyrosinase, and reductases (NADH-DCIP, azo, and riboflavin) was observed. The biodegradation was monitored by Ultraviolet–visible spectroscopy, Fourier transform infrared spectroscopy, and high performance liquid chromatography. The final products 4-methyl-2- o-tolylazo-benzene-1,3-diamine and [3-(phenyl-hydrazono)-cyclohexa-1,4-dienyl]-methanol were characterized by gas chromatography–mass spectroscopy. Phytotoxicity, COD, and BOD revealed non-toxicity of degraded products. Phytotoxicity study demonstrated non-toxicity of the biodegraded products for crop plants with respect to Triticum aestivum and Sorghum bicolor. Bacillus sp. VUS with its enzyme system could be a useful tool for textile effluent treatment.

Improving the functional expression of a Bacillus licheniformislaccase by random and site-directed mutagenesis

BackgroundLaccases have huge potential for biotechnological applications due to their broad substrate spectrum and wide range of reactions they are able to catalyze. These include, for example, the formation and degradation of dimers, oligomers, polymers, and ring cleavage as well as oxidation of aromatic compounds. Potential applications of laccases include detoxification of industrial effluents, decolorization of textile dyes and the synthesis of natural products by, for instance, dimerization of phenolic acids. We have recently published a report on the cloning and characterization of a CotA Bacillus licheniformis laccase, an enzyme that catalyzes dimerization of phenolic acids. However, the broad application of this laccase is limited by its low expression level of 26 mg l-1 that was achieved in Escherichia coli. To counteract this shortcoming, random and site-directed mutagenesis have been combined in order to improve functional expression and activity of CotA.ResultsA CotA double mutant, K316N/D500G, was constructed by combining random and site-directed mutagenesis. It can be functionally expressed at an 11.4-fold higher level than the wild-type enzyme. In addition, it is able to convert ferulic acid much faster than the wild-type enzyme (21% vs. 14%) and is far more efficient in decolorizing a range of industrial dyes. The investigation of the effects of the mutations K316N and D500G showed that amino acid at position 316 had a major influence on enzyme activity and position 500 had a major influence on the expression of the laccase.ConclusionThe constructed double mutant K316N/D500G of the Bacillus licheniformis CotA laccase is an appropriate candidate for biotechnological applications due to its high expression level and high activity in dimerization of phenolic acids and decolorization of industrial dyes.

Decolorization of industrial dyes catalyzed by laccase from a mushroom Lentinula edodes

Decolorization of industrial dyes catalyzed by laccase from a mushroom Lentinula edodes