Textile Dye Biodecolorization by Manganese Peroxidase: A Review.
Ontology highlight
ABSTRACT:
SUBMITTER: Chang Y
PROVIDER: S-EPMC8348190 | biostudies-literature |
REPOSITORIES: biostudies-literature
Similar Datasets
Project description:Textile azo dye decolorizing bacteria were isolated from alkaline Lakes Abaya and Chamo using Reactive Red 239 (RR239) dye. Through subsequent screening process, strain CH12 was selected to investigate the effects of nutrient supplement, DO, pH, temperature, dye concentration and types on decolorization. Based on 16S rRNA gene sequence analysis, strain CH12 was identified as Bacillus sp. Decolorization efficiencies were significantly enhanced with carbon (≥98%) and organic nitrogen (∼100%) supplements. Complete decolorization was also observed under anoxic and anaerobic conditions, and at the temperature of 30 °C and the pH of 10. However, the azo dye decolorization efficiency of strain CH12 was significantly reduced when NaNO3 (1-8%) was supplemented or under aerobic culturing condition (≤6%), indicating that RR239 was less preferred electron acceptor. Overall, strain CH12 can be a promising candidate for decolorization applications due to its potential to effectively decolorize higher RR239 concentrations (50-250 mg/L) and six additional dyes.
| S-EPMC5508668 | biostudies-literature
Project description:The treatment of textile industrial wastewater is an important concern owing to its negative impact on the biosphere. The present study highlighted dye decolorization potential of bacterial consortium EDPA containing Enterobacter dissolvens AGYP1 and Pseudomonas aeruginosa AGYP2 in the presence of redox mediators. Rapid decolorization of Acid Maroon V (100 mg l-1) was achieved in the presence of lawsone compared to other redox mediators. The dye decolorization was best fitted with first order kinetics with higher reaction kinetics (k1 = 0.328 h-1) and regression coefficient (R2 = 0.979). The removal of dye by the consortium was 1.47 times faster in 8 h with 0.01 mM lawsone. The consortium EDPA was able to decolorize 1200 mg l-1 concentration of dye with apparent R max , K m and R max /K m values 1000 mg l-1 h-1, 5000 mg l-1 and 0.2 h-1, respectively. The lawsone-mediated system could decolorize the dye 80.44% in 10 h at the end of 11 dye spiking cycle. The superior biodecolorization of 14 different textile dyes was obtained in the presence of lawsone-mediated system. The intracellular enzyme activities of azoreductase, NADH-DCIP reductase, laccase, manganese peroxidase and lignin peroxidase increased significantly. The sequential microaerophilic-aerobic incubation resulted into 89.31% reduction of total aromatic amines. The microbial toxicity, phytotoxicity and genotoxicity measurements revealed biotransformation of toxic nature of dye Acid Maroon V into non-toxic metabolites by the action of consortium EDPA, and thus its suitability for biotreatment of dye containing industrial effluents.Supplementary informationThe online version contains supplementary material available at 10.1007/s13205-023-03466-6.
| S-EPMC9845506 | biostudies-literature
Project description:Two phylogenetically divergent genes of the new family of dye-decolorizing peroxidases (DyPs) were found during comparison of the four DyP genes identified in the Pleurotus ostreatus genome with over 200 DyP genes from other basidiomycete genomes. The heterologously expressed enzymes (Pleos-DyP1 and Pleos-DyP4, following the genome nomenclature) efficiently oxidize anthraquinoid dyes (such as Reactive Blue 19), which are characteristic DyP substrates, as well as low redox-potential dyes (such as 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid)) and substituted phenols. However, only Pleos-DyP4 oxidizes the high redox-potential dye Reactive Black 5, at the same time that it displays high thermal and pH stability. Unexpectedly, both enzymes also oxidize Mn(2+) to Mn(3+), albeit with very different catalytic efficiencies. Pleos-DyP4 presents a Mn(2+) turnover (56 s(-1)) nearly in the same order of the two other Mn(2+)-oxidizing peroxidase families identified in the P. ostreatus genome: manganese peroxidases (100 s(-1) average turnover) and versatile peroxidases (145 s(-1) average turnover), whose genes were also heterologously expressed. Oxidation of Mn(2+) has been reported for an Amycolatopsis DyP (24 s(-1)) and claimed for other bacterial DyPs, albeit with lower activities, but this is the first time that Mn(2+) oxidation is reported for a fungal DyP. Interestingly, Pleos-DyP4 (together with ligninolytic peroxidases) is detected in the secretome of P. ostreatus grown on different lignocellulosic substrates. It is suggested that generation of Mn(3+) oxidizers plays a role in the P. ostreatus white-rot lifestyle since three different families of Mn(2+)-oxidizing peroxidase genes are present in its genome being expressed during lignocellulose degradation.
| S-EPMC4619462 | biostudies-literature
Project description:Irpex lacteus F17 is well-known for its ability to degrade recalcitrant aromatic pollutants, which mainly results from the action of the manganese peroxidase (MnP) that it is able to produce. Recently, the genome sequencing and annotation of this strain provided comprehensive picture of the ligninolytic peroxidase gene family. In addition to revealing the presence of 13 MnPs, genes for five dye-decolorizing peroxidases (DyPs) were also discovered in the I. lacteus F17 genome, which are unrelated to the fungal class II peroxidases. In the present study, amino acid sequences of five DyPs and 13 MnPs, representing two different families of heme peroxidases, were analyzed. Of these, two enzymes, a DyP (Il-DyP4) and a MnP (Il-MnP6) were expressed respectively in Escherichia coli, and were characterized by comparing their molecular models, substrate specificities, and catalytic features. The results showed that Il-DyP4 possessed a higher catalytic efficiency for some representative substrates, and a stronger decolorizing ability to a wide range of synthetic dyes in acidic conditions. Based on electrochemical measurements, Il-DyP4 was found to have a high redox potential of 27 mV at pH 3.5, which was superior to that of Il-MnP6 (- 75 mV), thereby contributing to its ability to oxidize high redox potential substrates, such as veratryl alcohol and polymeric dye Poly R-478. The results highlighted the potential of Il-DyP4 for use in industrial and environmental applications.
| S-EPMC6049852 | biostudies-literature
Project description:Ligninolytic enzymes, including laccase, manganese peroxidase, and dye-decolorizing peroxidase (DyP), have attracted much attention in the degradation of mycotoxins. Among these enzymes, the possible degradation pathway of mycotoxins catalyzed by DyP is not yet clear. Herein, a DyP-encoding gene, StDyP, from Streptomyces thermocarboxydus 41291 was identified, cloned, and expressed in Escherichia coli BL21/pG-Tf2. The recombinant StDyP was capable of catalyzing the oxidation of the peroxidase substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), phenolic lignin compounds 2,6-dimethylphenol, and guaiacol, non-phenolic lignin compound veratryl alcohol, Mn2+, as well as anthraquinone dye reactive blue 19. Moreover, StDyP was able to slightly degrade zearalenone (ZEN). Most importantly, we found that StDyP combined the catalytic properties of manganese peroxidase and laccase, and could significantly accelerate the enzymatic degradation of ZEN in the presence of their corresponding substrates Mn2+ and 1-hydroxybenzotriazole. Furthermore, the biological toxicities of the main degradation products 15-OH-ZEN and 13-OH-ZEN-quinone might be remarkably removed. These findings suggested that DyP might be a promising candidate for the efficient degradation of mycotoxins in food and feed.
| S-EPMC8473283 | biostudies-literature
Project description:Lignocellulose facilitates the fungal oxidization of recalcitrant organic pollutants through the extracellular ligninolytic enzymes induced by lignin in wood or other plant tissues. However, available information on this phenomenon is insufficient. Free radical chain reactions during lignin metabolism are important in xenobiotic removal. Thus, the effect of lignin on azo dye decolorization in vivo by Echinodontium taxodii was evaluated. In the presence of lignin, optimum decolorization percentages for Remazol Brilliant Violet 5R, Direct Red 5B, Direct Black 38, and Direct Black 22 were 91.75% (control, 65.96%), 76.89% (control, 43.78%), 43.44% (control, 17.02%), and 44.75% (control, 12.16%), respectively, in the submerged cultures. Laccase was the most important enzyme during biodecolorization. Aside from the stimulating of laccase activity, lignin might be degraded by E. taxodii, and then these degraded low-molecular-weight metabolites could act as redox mediators promoting decolorization of azo dyes. The relationship between laccase and lignin degradation was investigated through decolorization tests in vitro with purified enzyme and dozens of aromatics, which can be derivatives of lignin and can function as laccase mediators or inducers. Dyes were decolorized at triple or even higher rates in certain laccase-aromatic systems at chemical concentrations as low as 10 µM.
| S-EPMC4186836 | biostudies-literature
Project description:The extensive use of azo dyes by the global textile industry induces significant environmental and human health hazards, which makes efficient remediation crucial but also challenging. Improving dye removal efficiency will benefit the development of bioremediation techniques for textile effluents. In this study, an efficient system for azo dye (Direct Red 5B, DR5B) biodecolorization is reported, which uses the white-rot fungus Ganoderma lucidum EN2 and alkali lignin. This study suggests that the decolorization of DR5B could be effectively enhanced (from 40.34% to 95.16%) within 48 h in the presence of alkali lignin. The dye adsorption test further confirmed that the alkali-lignin-enhanced decolorization of DR5B was essentially due to biodegradation rather than physical adsorption, evaluating the role of alkali lignin in the dye biodegradation system. Moreover, the gas chromatography/mass spectrometry analysis and DR5B decolorization experiments also indicated that alkali lignin carried an excellent potential for promoting dye decolorization and displayed a significant role in improving the activity of lignin-modifying enzymes. This was mainly because of the laccase-mediator system, which was established by the induced laccase activity and lignin-derived small aromatic compounds.
| S-EPMC9866751 | biostudies-literature
Project description:Challenges exist in the wastewater treatment of dyes produced by the world's growing textiles industry. Common problems facing traditional wastewater treatments include low retention values and breaking the chemical bonds of some dye molecules, which in some cases can release byproducts that can be more harmful than the original dye. This research illustrates that track-etched polycarbonate filtration membranes with 100-nanometer diameter holes can be functionalized with azo dye direct red 80 at 1000 µM, creating a filter that can then be used to remove the entire negatively charged azo dye molecule for a 50 µM solution of the same dye, with a rejection value of 96.4 ± 1.4%, at a stable flow rate of 114 ± 5 µL/min post-functionalization. Post-functionalization, Na+ and NO3- ions had on average 17.9%, 26.0%, and 31.1% rejection for 750, 500, and 250 µM sodium nitrate solutions, respectively, at an average flow rate of 177 ± 5 µL/min. Post-functionalization, similar 50 µM azo dyes had increases in rejection from 26.3% to 53.2%. Rejection measurements were made using ultraviolet visible-light spectroscopy for dyes, and concentration meters using ion selective electrodes for Na+ and NO3- ions.
| S-EPMC9030370 | biostudies-literature
Project description:The biological treatment efficiency of dye wastewater using activated sludge (AS) is largely limited to the chromaticity and ecotoxicity of dyestuff. To alleviate this limitation, eleven industrial-grade disperse dyes were obtained from a fiber-dyeing factory, and for the first time, we studied the decolorization and detoxification effects of using the Pycnoporus laccase enzyme. Efficient decolorization was achieved with the following conditions: dye concentration 50 mg/L, 1-hydroxybenzotriazole (HBT) 0.15 mM, temperature 65 °C, pH 4, and laccase 0.33 U/mL. The decolorization rate of disperse dyes, ranging from 51 to 96% in this investigation, was highly dependent on the dye type, concentration, laccase loading, and HBT. The ecotoxicity of dyes was evaluated by studying the germination/growth of wheat seed as well as the respiratory rate of aerobic AS. Laccase treatment mitigated the phytotoxicity of dyes because of the higher wheat germination (e.g., increase of 38% for Black ECT 200%) and growth rate (e.g., increase of 91% for Blue 2BLN 200%). The reduced ecotoxicity of decolorized dye solution towards microorganisms was also confirmed by the finding that the oxygen uptake by aerobic AS was increased relative to that of the untreated samples (e.g., increase of 14 folds for Blue HGL 200%). In addition, the chemical oxygen demand (COD) of decolorized dye solution was slightly lower than that without decolorization during the respiratory test. The experimental results suggest that enzymatic decolorization and detoxification can be potentially used as a pretreatment method for disperse dye wastewater followed by AS treatment.
| S-EPMC9265578 | biostudies-literature
Project description:BackgroundAzo dyes are xenobiotic compounds that have bioaccumulated in the environment due to escalated industrial development. These are hazardous in nature, possessing carcinogenic and mutagenic effects on human beings.ObjectivesThe perspective of the present study was to isolate and to determine azo dye (Reactive Orange-16) degrading potential of marine actinobacteria isolated from sediment samples of Port Blair, India.Material and methodsActinobacteria with dye decolorization potential were isolated from sea sediment samples. The actinobacterial isolate with the highest dye decolorizing percentage was identified with the help of phenotypic, biochemical and molecular studies. The different physico-chemical parameters for dye decolorization were also optimized. The nature of decolorization by the potent isolate was determined with the help of High Performance Liquid chromatography (HPLC) and Fourier Transformed Infrared spectroscopy (FTIR) techniques. Further the toxicity of RO-16 decolorized products was investigated with the help of phytotoxcity assay.ResultsOut of six actinobacterial isolates, VITVAMB 1 possessed the most efficient RO-16 decolorization property. It decolorized 85.6% of RO-16 (250 mg L-1) within 24hrs. Isolate VITVAMB 1 was identified to be Nocardiopsis sp. Maximum dye decolorization occurred at pH 8, temperature 35°C, 3% salt concentration and a dye concentration of 50 mg L-1.ConclusionsThe nature of decolorization by Nocardiopsis sp. was biodegradation. Additionally, the degraded dye metabolites were found to be less toxic than pure dye. The high decolorization potential of VITVAMB 1 and the low toxicity of its degradation products make it a prospective dye removal system. The marine origin of VITVAMB 1 also makes it an attractive source for novel azo dye reducing enzymes.
| S-EPMC7080967 | biostudies-literature