Removal of α-naphthol and other phenolic compounds from polluted water by white radish (Raphanus sativus) peroxidase in the presence of an additive, polyethylene glycol

Ashraf, Humaira; Husain, Qayyum

doi:10.1007/s12257-009-0002-6

Cited by 17 publications

(11 citation statements)

References 27 publications

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“…in eliminating aromatic compounds like various phenols from both synthetic and real wastewaters [21,27,48]. Peroxidases, in the presence of hydrogen peroxide (H 2 O 2 ), which acts as electron acceptor, are able to catalyze the oxidative polymerization of phenolic compounds to form insoluble polymers [49].…”

Section: Calculated Value (A-b=c) (X) 630mentioning

confidence: 99%

Application of Diethylaminoethyl Cellulose Immobilized Pointed Gourd (Trichosanthes dioica) Peroxidase in Treatment of Phenol and α-Naphthol

Singh¹

2015

J Bioprocess Biotech

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Recently, enzymatic treatment using peroxidases in removal of aromatic compounds has gained importance. In this study pointed gourd peroxidase was salt fractionated and direct immobilization of these proteins on diethylaminoethyl cellulose for oxidation of phenol and α-naphthol has been investigated. The activated diethylaminoethyl cellulose was quite effective in high yield immobilization of peroxidases from pointed gourd and it could bind ~576 units per g of the matrix. Immobilized pointed gourd peroxidase on this anion exchanger showed very high effectiveness factor 'Ɛ' as 0.91 with an activity yield of 91%. Immobilized PGP (I-PGP) as compared to soluble counterparts (s-PGP) were more effective and removed 79%, 88% and 54% oxidation of phenol and α-naphthol by 75%, 81% and 61% at 30, 40 and 50°C respectively, with a treatment time of 140 min. In the absence CdCl2 s-PGP as well as I-PGP exhibited upto 93% of oxidation of these compounds; whereas the presence of CdCl2 of negatively affected the removal of phenol and α-naphthol. The reactor worked well continuously for over one month for effectively oxidizing/ removing phenol and α-naphthol by 54% and 61% respectively. Thus, such immobilized enzyme systems in reactor have a great future and could be exploited for treating organic pollutants present in industrial effluents.

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Section: Calculated Value (A-b=c) (X) 630mentioning

confidence: 99%

Application of Diethylaminoethyl Cellulose Immobilized Pointed Gourd (Trichosanthes dioica) Peroxidase in Treatment of Phenol and α-Naphthol

Singh¹

2015

J Bioprocess Biotech

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“…They have the capability to catalyze a large variety of aromatic compounds through a reaction in the presence of hydrogen peroxide. Hydrogen peroxide acts as an acceptor while other aromatic substrates donate the hydrogen atom [1][2][3]. Physiological functions of peroxidase enzymes in plants include oxidation of toxic reducing agents, elimination of hydrogen peroxide, biosynthesis and degradation of lignin in cell walls, auxin catabolism, defensive responses to wounding, defense against pathogen or insect attack and some respiratory processes [4].…”

Section: Introductionmentioning

confidence: 99%

“…In biochemistry, HRP is utilized extensively as a signal amplification via conjugated with antibody and/or gold (Au) nanoparticles to increase the detectability of the target molecules such as human IgG [9], haptoglobin (Hp) type and Hp complexes in human serum [10], Staphylococcal enterotoxin B (SEB) in food [11], and carcinoembryonic antigen (CEA) as a tumor marker [12]. Some applications of peroxidases in the environmental field, utilized for the treatment of waste water containing phenol [13,14], naphthol and phenolic compounds [2,15], have been reported. Moreover, enzyme peroxidase has been used for the syntheses of various aromatic chemicals and removal of peroxide from materials such as Abstract Thai local plants known as banana stalk, banana blossom, banana, sugar-cane, oroxylum indicum fruit, sesbania grandiflora fruit, and pigeon pea fruit were utilized for screening peroxidase enzyme to replace costly horseradish peroxidase in the hydrogen peroxide assay.…”

Section: Introductionmentioning

confidence: 99%

Employing peroxidase from Thai indigenous plants for the application of hydrogen peroxide assay

et al. 2016

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“…Of them, removal of naphthols, C 10 H 7 OH, should be placed at the top priority of tasks, because toxicity of naphthols is relatively high and their biodegradation is low. Naphthols were often discharged from industries related with medicine, dyestuff, photograph, and agrochemicals 1, 2. In addition, 1‐naphthol is a major component of the pesticide napropamide and a principal reaction product in the hydrolysis of the pesticide carbaryl.…”

Section: Introductionmentioning

confidence: 99%

“…As described above, many studies have been reported on removal of various phenol compounds 13–17. In addition, some studies were also reported on enzymatic treatment of naphthols 1, 2, 19, 20. But, little was reported on tyrosinase‐catalyzed quinone oxidation of naphthols and their removal.…”

Section: Introductionmentioning

confidence: 99%

Use of chitosan for removal of naphthols through tyrosinase‐catalyzed quinone oxidation

Kimura

Kashiwada

Matsuda

et al. 2012

J of Applied Polymer Sci

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In this study, the combined use of chitosan and mushroom tyrosinase was applied to remove 1‐naphthol and 2‐naphthol from aqueous solutions. In particular, the process parameters, such as the pH value, temperature, and enzyme dose, were discussed for tyrosinase‐catalyzed quinone oxidation of 1‐naphthol. The optimum conditions of enzymatic quinone oxidation of 1‐naphthol were determined to be pH 8.0 and 40°C. Under the optimum conditions, quinone oxidation of 1‐naphthol increased with an increase in the enzyme dose. Quinone derivatives enzymatically generated were chemisorbed on chitosan bead sand. The initial velocity of enzymatic quinone oxidation increased with an increase in the amount of added chitosan beads, since unfavorable interactions between quinone derivatives and tyrosinase in the solutions were restrained by quinone adsorption. 1‐Naphthol was completely removed for 8 h by quinone adsorption on chitosan beads (0.10 cm3/cm3) at 20 U/cm3. The removal time was shortened by increasing the enzyme dose or the amount of added chitosan beads. 2‐Naphthol was also completely removed by increasing the enzyme concentration and reaction time, since enzymatic quinone oxidation of 2‐naphthol was much slower than that of 1‐naphthol. The above results reveal that the procedure constructed in this study was an effective technique to remove naphthols. © 2012 Wiley Periodicals, Inc. J Appl Polym Sci, 2012

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Removal of α-naphthol and other phenolic compounds from polluted water by white radish (Raphanus sativus) peroxidase in the presence of an additive, polyethylene glycol

Cited by 17 publications

References 27 publications

Application of Diethylaminoethyl Cellulose Immobilized Pointed Gourd (Trichosanthes dioica) Peroxidase in Treatment of Phenol and α-Naphthol

Application of Diethylaminoethyl Cellulose Immobilized Pointed Gourd (Trichosanthes dioica) Peroxidase in Treatment of Phenol and α-Naphthol

Employing peroxidase from Thai indigenous plants for the application of hydrogen peroxide assay

Use of chitosan for removal of naphthols through tyrosinase‐catalyzed quinone oxidation

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