Immobilization of peroxidase from fresh horseradish extract for anthraquinone dye decolorization

Šekuljica, Nataša Ž.; Prlainović, Nevena Ž.; Lukić, Nevena M.; Jakovljević, Aleksandra M.; Grbavčić, Sanja; Mijin, Dušan Ž.; Knežević‐Jugović, Zorica

doi:10.5937/zasmat1503335s

Cited by 5 publications

(5 citation statements)

References 12 publications

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“…This was an indication that the immobilized peroxidase was more stable under alkaline conditions (Darwish et al, 2019). Sekuljica et al (2015), obtained 94.7% color removal efficiency at pH 4 and a reaction time of 15 min using horseradish peroxidase enzyme. Han F. et al (2020) observed in their activities that the pepsin enzyme had max.…”

Section: Effect Of Ph On Cod and Color Removalmentioning

confidence: 97%

The Effect of Immobilized Enzyme on Textile Wastewater

AYRANPINAR,

KOZAK,

GÖÇER

et al. 2024

Kahramanmaraş Sütçü İmam Üniversitesi Mühendislik Bilimleri Dergisi

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Textile wastewater has a complex composition characterized by high dye content and chemical oxygen demand. Therefore, textile wastewaters have serious environmental impacts, such as aesthetic degradation, and carcinogenic properties. Treatment and the recovery of textile wastewater are important due to their high volume and toxicity. The effects of peroxidase enzyme immobilized on magnetic chitosan-clay beads of synthetic textile wastewater were investigated in a batch reactor. System performance was determined by chemical oxygen demand (COD) and color. The batch reactor was operated in three different pH (5, 7, 10), temperatures (25, 35, 45 °C), and reaction times (0-5-10-20-30 min.) with synthetic textile wastewater. As a result, COD and color removal efficiencies were determined as 44% and 56%, respectively, corresponding effluent concentrations are 1442 mg/L, 450 Pt-Co. The results of this study show that using the enzyme immobilization process is an effective method to remove color and COD concentration from textile wastewater.

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Section: Effect Of Ph On Cod and Color Removalmentioning

confidence: 97%

The Effect of Immobilized Enzyme on Textile Wastewater

AYRANPINAR,

KOZAK,

GÖÇER

et al. 2024

Kahramanmaraş Sütçü İmam Üniversitesi Mühendislik Bilimleri Dergisi

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“…After that, the sample was centrifuged (at 10,000 rpm for 10 min), and the absorbance was measured. Equation 5 was used to compute the % decolorization [21].…”

Section: Decolorization Of Dyes With Citrus Lemon Peroxidase (Clp)mentioning

confidence: 99%

“…Similar experiments were conducted to optimize temperature (25 °C-95 °C), enzyme dose (0.05-0.2), and H 2 O 2 concentration (0.05-0.2 mM). The incubation time (5-60 min) was calculated [21]. All the studies were carried out in test tubes with a shaking water bath.…”

Section: Optimization Of Peroxidase Activity For Dye Decolorizationmentioning

confidence: 99%

“…The contact duration between the catalyst and the substrate is a key factor in dye degradation. So, investigations were carried out to determine the optimal contact time required for Citrus limon peroxidase to decolorize 1847 Colafx Blue P3R and 621 Colafx Blue R. Time of incubation (5-60 min) was observed [21]. The incubation effect on both selected dyes is demonstrated in Fig.…”

Section: Parameters Optimization For Optimal Dye Degradation Percentagementioning

confidence: 99%

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Citrus limon peroxidase-assisted biocatalytic approach for biodegradation of reactive 1847 colfax blue P3R and 621 colfax blue R dyes

Riaz

Kalsoom

Bhatti

et al. 2022

Bioprocess Biosyst Eng

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One of the big environmental problems in today’s world is dye-contaminated toxic waste. Peroxidase is known as highly efficient for the degradation of various pollutants, including dyes. Environmental contamination caused by the discharge of dyes into water bodies is an onerous challenge that poses both human and ecological hazards. In the current studies, biocatalysts used for enzyme decolorization (1847 Colafx Blue P3R and 621 Colafx Blue) are regarded as an eco-friendly method utilizing commonly available low-cost material lemon peels (Citruslimon peroxidase). Peroxidase was extracted in a phosphate buffer of pH 7.0 and partially purified by 20–80% ammonium sulfate precipitation technique from Citruslimon peels. The soluble enzyme was characterized in terms of kinetic and thermodynamic parameters. The values of Km and Vmax (23.16 and 204.08 μmol/ml/min) were determined, respectively. The enzyme showed maximum activity at pH 5.0 and a temperature of 55 °C. Citruslimon efficiently degraded 1847 Colafx Blue P3R and 621 Colafx Blue R dyes with maximum degradation of 83 and 99%, respectively, with an initial dye concentration of 200 ppm at pH 4 and 35 °C temperature within 5–10 min of incubation time. The effect of the redox mediator on the degradation process was examined. Results showed that the peroxidase HOBT system efficiently enhanced the degradation of dyes from water. Hence, Citruslimon peroxidase is an efficient biocatalyst for the treatment of effluents.

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“…The obtained enzyme-clay complex was used for the treatment of wastewater polluted with phenol. Fumed silica served as the support for the adsorp-tion of HRP and immobilized biocatalyst was successfully applied in the AV 109 dye removal [16].…”

Section: Introductionmentioning

confidence: 99%

The oxidation of anthraquinone dye using HRP immobilized as a cross-linked enzyme aggregates

Sekuljica¹,

Prlainovic²,

Stefanović³

et al. 2016

Adv techn

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Finding a sustainable and ecofriendly methods for recalcitrant synthetic dyes removal is a researchers` major challenge. A carrier-free technique for commercial HRP immobilization is a focus of the present study. The immobilized biocatalyst, HRP-CLEAs with 580 U g-1 of the activity was obtained under the following immobilization conditions: precipitation reagent 80% ammonium sulphate, cross-linking reagent 1% of glutaraldehyde and protein-fedder, bovine serum albumin (BSA) concentration 5 mg ml-1. The obtained HRP-CLEAs showed great affinity towards model anthraquinone dye, C. I. Acid Violet 109. 88.4% of the dye was oxidized under the reaction conditions: pH 4, dye concentration 40 mg l-1 , H 2 O 2 concentration 1 mM and 0.1 U of HRP-CLEAs. The possibility of the immobilized biocatalyst application in five and eight oxidation cycles of the dye and pyrogallol (retained activity ~ 80%), respectively, indicates that HRP-CLEAs is an efficient and environmentally friendly biocatalyst with great potential in aromatic compounds removal from wastewater. This paper is a continuation of our earlier research related to HRP from horseradish extract immobilization in the form of CLEAs and the application in the wastewater colored with a synthetic anthraquinone dye treatment.

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Immobilization of peroxidase from fresh horseradish extract for anthraquinone dye decolorization

Abstract: ABSTRACT

Cited by 5 publications

References 12 publications

The Effect of Immobilized Enzyme on Textile Wastewater

The Effect of Immobilized Enzyme on Textile Wastewater

Citrus limon peroxidase-assisted biocatalytic approach for biodegradation of reactive 1847 colfax blue P3R and 621 colfax blue R dyes

The oxidation of anthraquinone dye using HRP immobilized as a cross-linked enzyme aggregates

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