The Use of Horse Radish Peroxidase, an Eco-Friendly Method for Removal of Phenol from Industrial Effluent (original) (raw)
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Removal of phenolic compounds by peroxidase derived from agricultural waste
2005
This study focuses on the removal of phenolic compounds by peroxidase derived from agricultural waste, The phenols studied are phenol, o-cresol, n-cresol, p-cresol, 2-chlorophenol, 3-chlorophenol, 4-chlorphenol, catechcol, resorcinol, hydroquinone, 1-naphthol and 2-naphthol. The extraction of crude POD from sweet potato with phosphate buffer exhibited the highest activity and removal efficiency. The optimum conditions for removal of phenol was at 30 ํC, 100 min, pH 7,20 ppm of phenol, 0.5% w/w of H[subscript 2]O[subscript 2], 10 units/mL of crude POD, 20 ppm of PEG-6000 and phosphate buffer as solvent. Rate of conversion of phenol under this condition was 1.045 [micromol] per h. The optimum condition for removal of phenols was at 30 ํC, 100 min, pH 7,20 ppm of phenols, 1.0% w/w of H[subscript 2]O[subscript 2], 4 units/mL of crude POD and phosphate buffer as solvent. The product from the removal of phenol by POD is polymer consisted of 2-phenoxy-biphenyl, 1,1'-biphenyl-2,2'-d...
Biotechnology and Bioprocess Engineering, 2009
^Äëíê~Åí= Role of white radish peroxidase has been investigated in the treatment of water contaminated with phenols, particularly α-naphthol. Water polluted with α-naphthol was treated with white radish peroxidase under various experimental conditions. The treatment of α-naphthol polluted water by this enzyme in presence of polyethylene glycol enhanced its removal. Studies carried out in absence of polyethylene glycol showed only 36% of α-naphthol removal however, 96% of it was removed in presence of 0.1 mg/mL of polyethylene glycol in 100 mM sodium phosphate buffer, pH 6.5, and 0.75 mM H 2 O 2 at 40°C. The other phenols oxidized and removed from waste water under similar experimental conditions were 18%, ã-cresol; 30%, é-chlorophenol; 62%, é-bromophenol; 20%, benzyl alcohol; 21%, quinol; 38%, 2,6-dichlorophenol; 13%, 2,4-dichlorophenol; and 2%, native phenol. Mixtures of different phenolic compounds removed under identical treatment conditions were 63%, A; 40%, B; 52%, C; 41%, D; 72%, E; 66%, F; and 72%, G. Thus, peroxidase in presence of an additive, polyethylene glycol could be a suitable tool for the removal of phenolic compounds from industrial effluents.
Journal of Materials Science and Engineering B, 2017
In the light of the increasing burden of pollutants in major rivers and stringent environmental legislation, adaptation to eco-friendly treatment approaches is desperately required to decontaminate industrial effluents before its discharge to rivers and other fresh water-bodies. In present study, we have designed a simple and efficient method for removal of phenols from effluent wastewater using an immobilized preparation of HRP (horseradish peroxidase). The enzyme was isolated in bulk amount from the roots of the Armoracia rusticana and covalently immobilized to polycarbonate supports using a photolabile linker FNAB (1-fluoro-2-notro-4-azidobenzene). The immobilized enzyme showed enhanced storage stability and reusability. The immobilized HRP was subsequently used for degradation of phenols in sewage and spiked wastewater. The phenol content of spiked wastewater was reduced to 93% in the 3 L reactor following treatment with immobilized HRP and H 2 O 2. The improvement in the quality of water upon treatment was reflected by the changes in pH, conductivity, TDS (total dissolved salts) and biodegradation of organic contents as indicated by 77% and 87% reduction in COD (chemical oxygen demand) and BOD (biochemical oxygen demand) respectively in the analyzed sample.
Removal of phenolic compounds from synthetic wastewater using soybean peroxidase
Water Research, 1999
AbstractÐExperiments were conducted to investigate the eciency of using soybean peroxidase (SBP) to remove several dierent phenolic compounds from unbuered synthetic wastewater. The phenol derivatives studied included parent phenol, chlorinated phenols, cresols, 2,4-dichlorophenol and 4,4'-isopropylidenediphenol (commonly known as bisphenol A). Optimum conditions to achieve at least 95% removal of these compounds were determined for the following parameters: pH, SBP dose in the absence and presence of polyethylene glycol (PEG), hydrogen peroxide to substrate ratio, and PEG dose. Experimental results showed that SBP eciently removed aromatic compounds from synthetic wastewater in the presence of hydrogen peroxide. An increase in the hydrogen peroxide to substrate ratio beyond the optimum resulted in enzyme inactivation in all cases except for bisphenol A. The optimum pH for dierent phenolic compounds ranged from 5.5 to 8. For each substrate, the optimum enzyme dose in the presence of PEG varied signi®cantly. The studies showed that PEG only slightly reduced the amount of SBP required for 95% removal of the substrate. For most of the substrates, an increase in PEG dose beyond the optimum dose did not signi®cantly change the removal eciency. #
Environmental Technology & Innovation, 2020
Prosopis juliflora or Mesquite, one of the world's worst invaders, yields low-purity peroxidases (MPx), which remove phenols from the wastewater of textile and leather industries. Within 30 min, MPx removes phenols from wastewater of the textile industry (94.95 ± 0.82%) and leather industry (91.49 ± 1.54%). After treatment with MPx, the residual phenol in the wastewater remained much below the environmentally safe limit outlined by the USEPA. For maximum phenols removal, MPx requires 4-6 mM H 2 O 2 , whereas Horseradish peroxidase (HRP), a commercially available and the most widely used peroxidase, uses 8 mM H 2 O 2. MPx perform better than (HRP), in parameters such as phenol removal efficiency, need of chemical additive, stability, and time of preparation. MPx, therefore, offer an economically viable method for wastewater treatment and also obviate several challenges of using purified enzymes. Extraction from the non-edible invasive plant is an added benefit as it does not require specific cultivation conditions and address the concern of competing with food resource. Further, using an invasive plant as a bioresource will help in the management of aggressive invaders like P. julifora. We report a procedure to prepare MPx with a lesser number of chemicals and use it with a low concentration of H 2 O 2 for remediation of phenol from industrial wastewater. MPx, with high phenol removal capacity, shows the potential to act as an economic but effective alternative to purified peroxidases for environmental remediation withstanding the principles of the circular economy.
Removal of Phenol from Synthetic and Industrial Wastewater by Potato Pulp Peroxidases
Water, air, and soil pollution
Plant peroxidases have strong potential utility for decontamination of phenol-polluted wastewater. However, large-scale use of these enzymes for phenol depollution requires a source of cheap, abundant, and easily accessible peroxidase-containing material. In this study, we show that potato pulp, a waste product of the starch industry, contains large amounts of active peroxidases. We demonstrate that potato pulp may serve as a tool for peroxidase-based remediation of phenol pollution. The phenol removal efficiency of potato pulp was over 95 % for optimized phenol concentrations. The potato pulp enzymes maintained their activity at pH 4 to 8 and were stable over a wide temperature range. Phenol solutions treated with potato pulp showed a significant reduction in toxicity compared with untreated phenol solutions. Finally we determined that this method may be employed to remove phenol from industrial effluent with over 90 % removal efficiency under optimal conditions.
Biocatalysis and Agricultural Biotechnology, 2019
Plants seeds are an important source of enzymes with biotechnological interest. In particular, plant peroxidases, because of their enzymatic activity and stability, are used for the synthesis of phenolic resins, in the treatment of waste waters, or as labelling enzymes and in food industry. Thus, these enzymes can give a potential substitute of other polluting industrial catalysts to the conservation of the environment. In the present work, a novel plant peroxidase (named As-sP) was purified and characterised from seeds of Araujia sericifera. This enzyme (∼40 kDa) exhibits a maximum activity at pH 5.0 and is a haem-peroxidase, basing on both the spectroscopic properties and amino acid composition. As-sP activity increased by Ca 2+ , Cu 2+ , Mg 2+ ; while in presence of EDTA, it is lost. On the other hand, As-sP activity is stable in a range of 40-60°C, while decreased at higher temperature (70-80°C). Furthermore, the activity has been tested in presence of natural (chlorogenic acid, pyrogallol and guaiacol) or synthetic (ABTS) substrates, finding that chlorogenic acid (Km 38.6 ± 2.4 μM and Vmax 92.6 ± 3.9 μM min −1) was the most suitable. Finally, this enzyme was able to remove phenol from water solutions, and this capacity increases in presence of Ca 2+ and polyethylene glycol. This novel peroxidase, due to its enzymatic properties and heat stability, is a novel tool for bioremediation and can be used as a beneficial candidate for industrial applications, such as in decontamination of phenolpolluted waters.
Enzyme and Microbial Technology, 1998
Horseradish peroxidase has been proven effective in removing phenolic compounds in wastewater and additives such as polyethylene glycol have been found very effective in reducing the minimum enzyme dose required. The effect of additives on horseradish peroxidase-catalyzed removal of phenol was investigated in this study. In the absence of additive, active enzyme is predominantly inactivated by the polymer product formed during the reaction. The specific activity of horseradish peroxidase is higher due to the presence of additive. Experiments suggest that additives combine with the polymerization products formed during the reaction, because additives have a higher partition affinity with the polymer products than peroxidases. Most of the polymer product is coupled with additive so that less enzyme interacts with the polymer product. Horseradish peroxidase still combines with polymer products and becomes inactivated but at a much slower rate when additives are present. Consequently, the enzyme activity is protected by the additives.