Peroxidase extraction from jicama skin peels for phenol removal

Chiong, Tung; Lau, Sie Yon; Khor, Ee Huey; Danquah, Michael K.

doi:10.1088/1755-1315/36/1/012048

Cited by 10 publications

(4 citation statements)

References 32 publications

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“…The peroxidases from agricultural waste are heme proteins that are able to catalyze the oxidation of a large variety of substrates through a reaction with hydrogen peroxide 11 . The peroxidase enzyme has attracted much demand recently due to its wide applicability in various processes such as the removal of phenolic contaminants and related compounds, decolorization of synthetic dye, peroxidase biosensor, analysis and diagnostic kit, enzyme immunoassay, deodorization of swine manure, application in paper pulp industries, and so forth 12–17 . In the literature, various sources other than wheat bran have also been used for the extraction of peroxidase enzymes, such as soya bean, horse radish root, and peanuts 18,19 .…”

Section: Introductionmentioning

confidence: 99%

“…11 The peroxidase enzyme has attracted much demand recently due to its wide applicability in various processes such as the removal of phenolic contaminants and related compounds, decolorization of synthetic dye, peroxidase biosensor, analysis and diagnostic kit, enzyme immunoassay, deodorization of swine manure, application in paper pulp industries, and so forth. [12][13][14][15][16][17] In the literature, various sources other than wheat bran have also been used for the extraction of peroxidase enzymes, such as soya bean, horse radish root, and peanuts. 18,19 Among the possible sources, horse radish root was considered to be the main commercial source of extraction of peroxidase enzyme.…”

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confidence: 99%

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Simple and efficient method for the extraction, isolation, and purification of peroxidase enzyme from wheat bran

Kumar,

Vasishta,

Pawar

2024

Biofuels Bioprod Bioref

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Peroxidase is an industrially important enzyme with a broad range of applications. In this study, the extraction, isolation, and purification of peroxidase was conducted with wheat bran as a feedstock. Several commercially available buffers (K2HPO4, Na3PO4, CH3COONa, and Tris‐base) were explored for the extraction of peroxidase from wheat bran. Of the tested media, sodium acetate buffer gave an excellent performance and displayed maximum protein (0.44 mg mL−1) and enzyme activity (28 U mL−1). A process optimization study was also conducted to obtain the maximum protein concentration and enzyme activity. The intensified process provided 1.39 mg mL−1 protein concentration with 90 U mL−1 enzyme activity with specific enzyme activity of 135.8 U mg−1. Crude enzyme was purified using a three‐step process: (a) precipitation, (b) ultrafiltration, and (c) chromatographic purification. Commercially available strong and weak ion exchange resins, with different surface properties, were tested for purification. The weak anion exchange resin showed an excellent performance for maximum binding of peroxidase. Adsorption study investigated the best fit model of Freundlich isotherm with maximum binding capacity of 54 mg mL−1. Overall, purification provided peroxidase with a protein concentration of 1.24 mg mL−1 and 727.58 U mg −1 specific enzyme activity with purity increased by around ~6.6 fold. The reported process provides a simple and efficient method for the extraction and purification of peroxidase enzyme from wheat bran for its efficient valorization.

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Section: Introductionmentioning

confidence: 99%

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confidence: 99%

Simple and efficient method for the extraction, isolation, and purification of peroxidase enzyme from wheat bran

Kumar,

Vasishta,

Pawar

2024

Biofuels Bioprod Bioref

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“…Peroxidases (EC 1.11.1.7) are heme-containing oxidoreductases that use hydrogen peroxide as an oxidant to catalyze the oxidation of a wide range of substrates like phenols, aromatic amines, sulfonates, and indoles [11,12]. They have a wide variety of industrial and biotechnological applications, one of which includes biodegradation of toxic and carcinogenic phenolic contaminants and related compounds in industrial effluents [13]. The horseradish peroxidase (HRP) and other plant peroxidases have been extensively used to bioremediate phenolic compounds from industrial wastewater [10,14].…”

Section: Introductionmentioning

confidence: 99%

“…The horseradish peroxidase (HRP) and other plant peroxidases have been extensively used to bioremediate phenolic compounds from industrial wastewater [10,14]. However, the high cost of purified HRP and other commercially available peroxidases has made it necessary to search for other cheap and local sources of peroxidases with comparable or better stability that can be explored for efficient biodegradation of phenolic pollutants from industrial effluents [13]. This approach for searching peroxidase and other useful products from local bioresource with the potential to remediate organic pollutants arising from petroleum effluent Plants are a well-known source of some biotechnologically important enzymes.…”

Section: Introductionmentioning

confidence: 99%

Characterization of Calotropis procera root peroxidase and its potential to mediate remediation of phenolic pollutant from petroleum refinery effluent

Banbilbwa¹,

Gabriel²,

Adams³

et al. 2021

J App Biol Biotech

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Peroxidases are oxidoreductive enzymes that have the potential to oxidize recalcitrant organic compounds like phenol, reducing their toxicity. Calotropis procera root peroxidase (CPrP) was isolated, characterized, and evaluated at the laboratory scale for its ability to oxidatively degrade phenol in petroleum refinery effluent. Ammonium sulfate precipitation, ion exchange, and gel filtration chromatography were used to purify CPrP 79-fold. Purified CPrP revealed a single polypeptide band with a molecular weight of 46.5 kDa in a single peak. The biochemical characterization revealed that the CPrP is a thermostable enzyme, active on both tested substrates (o-dianisidine and guaiacol) with optimum activity at 50°C and pH 6.0. The kinetic data show that o-dianisidine is the most preferred substrate. Apart from acetone, ethylenediaminetetraacetic acid, and Hg 2+ which act as inhibitors of CPrP, all other tested metal ions (Mg2+, Zn2+, Cu2+, and Mn2+) exhibited slight activation. The CPrP exhibits high efficiency to bioremediate phenol from petroleum effluent. In conclusion, this study revealed the possibility of obtaining peroxidase from locally available bioresources with the ability to bioremediate phenolic contaminants from petrochemical industry effluents.

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Immobilized enzymes and cell systems: an approach to the removal of phenol and the challenges to incorporate nanoparticle-based technology

Escobedo‐Morales

Hernández‐Beltrán

Balagurusamy

et al. 2022

World J Microbiol Biotechnol

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Peroxidase extraction from jicama skin peels for phenol removal

Cited by 10 publications

References 32 publications

Simple and efficient method for the extraction, isolation, and purification of peroxidase enzyme from wheat bran

Simple and efficient method for the extraction, isolation, and purification of peroxidase enzyme from wheat bran

Characterization of Calotropis procera root peroxidase and its potential to mediate remediation of phenolic pollutant from petroleum refinery effluent

Immobilized enzymes and cell systems: an approach to the removal of phenol and the challenges to incorporate nanoparticle-based technology

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