Extraction and purification techniques of the bio-catalyst cabbage peroxidase enzyme to remove reactive dyes and bisphenol-A pollutants

Abdulwahhab Mohammed, Weam; M-Ridha, Mohanad J.

doi:10.1016/j.rineng.2024.101961

Cited by 2 publications

(2 citation statements)

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“…Although they have a structure similar to that of Class II peroxidases, they play a role in the hydroxylation of various chemicals, unlike the peroxidative cycle. The application areas of peroxidases in this class are specific in terms of their substrates and can successfully degrade various phenolic compounds, including pyrogallol, guaiacol, catechin, and catechol . It is a commercial enzyme used in many industrial fields due to its low molecular weight (44 kDa), broad substrate specificity, and high catalytic efficiency .…”

Section: Introductionmentioning

confidence: 99%

“…The application areas of peroxidases in this class are specific in terms of their substrates and can successfully degrade various phenolic compounds, including pyrogallol, guaiacol, catechin, and catechol. 16 It is a commercial enzyme used in many industrial fields due to its low molecular weight (44 kDa), broad substrate specificity, and high catalytic efficiency. 17 HRP is involved in many application areas such as the bioremediation of phenolic compounds, removal of synthetic dyes from industrial wastes, cancer treatment, and biosensors.…”

Section: Introductionmentioning

confidence: 99%

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Horseradish Peroxidase Immobilized onto Mesoporous Magnetic Hybrid Nanoflowers for Enzymatic Decolorization of Textile Dyes: A Highly Robust Bioreactor and Boosted Enzyme Stability

Bakar,

Akbulut,

Ulusal

et al. 2024

ACS Omega

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Recently, hybrid nanoflowers (hNFs), which are accepted as popular carrier supports in the development of enzyme immobilization strategies, have attracted much attention. In this study, the horseradish peroxidase (HRP) was immobilized to mesoporous magnetic Fe3O4–NH2 by forming Schiff base compounds and the HRP@Fe3O4–NH2/hNFs were then synthesized. Under optimal conditions, 95.0% of the available HRP was immobilized on the Fe3O4–NH2/hNFs. Structural morphology and characterization of synthesized HRP@Fe3O4–NH2/hNFs were investigated. The results demonstrated that the average size of HRP@Fe3O4–NH2/hNFs was determined to be around 220 nm. The ζ-potential and magnetic saturation values of HRP@Fe3O4–NH2/hNFs were −33.58 mV and ∼30 emu/g, respectively. Additionally, the optimum pH, optimum temperature, thermal stability, kinetic parameters, reusability, and storage stability were examined. It was observed that the optimum pH value shifted from 5.0 to pH 8.0 after immobilization, while the optimum temperature shifted from 30 to 80 °C. K m values were calculated to be 15.5502 and 7.6707 mM for free HRP and the HRP@Fe3O4–NH2/hNFs, respectively, and V max values were calculated to be 0.0701 and 0.0038 mM min–1. The low K m value observed after immobilization indicated that the affinity of HRP for its substrate increased. The HRP@Fe3O4–NH2/hNFs showed higher thermal stability than free HRP, and its residual activity after six usage cycles was approximately 45%. While free HRP lost all of its activity within 120 min at 65 °C, the HRP@Fe3O4–NH2/hNFs retained almost all of its activity during the 6 h incubation period at 80 °C. Most importantly, the HRP@Fe3O4–NH2/hNFs demonstrated good potential efficiency for the biodegradation of methyl orange, phenol red, and methylene blue dyes. The HRP@Fe3O4–NH2/hNFs were used for a total of 8 cycles to degrade methyl orange, phenol red, and methylene blue, and degradation of around 81, 96, and 56% was obtained in 8 h, respectively. Overall, we believe that the HRP@Fe3O4–NH2/hNFs reported in this work can be potentially used in various industrial and environmental applications, particularly for the biodegradation of recalcitrant compounds, such as textile dyes.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Horseradish Peroxidase Immobilized onto Mesoporous Magnetic Hybrid Nanoflowers for Enzymatic Decolorization of Textile Dyes: A Highly Robust Bioreactor and Boosted Enzyme Stability

Bakar,

Akbulut,

Ulusal

et al. 2024

ACS Omega

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Graphene Oxide Nanocomposites as a Promising Photocatalyst in the Degradation of Organic Dyes

Vishnu,

Pal,

Lawrence

2024

Advances in Chemical and Materials Engineering

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Globally, water pollution is a crucial environmental issue. Research has indicated the presence of chemicals in the aquatic environment, which includes dyes, antibiotics, and insecticides. Presently, there are numerous techniques available for the degradation of dyes which include physicochemical, chemical, biological, electrochemical, and membrane technologies along with sustainable techniques such as photocatalysis. The remarkable photocatalytic activity of graphene oxide nanocomposites is one of its most notable features. Graphene oxide's photocatalytic ability outperforms many traditional techniques, offering a quick and efficient way to remove dye. The detailed mechanism of graphene induced materials in the degradation of organic dyes was highlighted in the present study. Also, the current integration of graphene with plant sources and their usage as the photocatalysts are discussed. The present study could provide a nominal insight on the current trends in graphene-based bioremediation techniques and its efficacy as a pollutant removal system.

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Extraction and purification techniques of the bio-catalyst cabbage peroxidase enzyme to remove reactive dyes and bisphenol-A pollutants

Cited by 2 publications

References 25 publications

Horseradish Peroxidase Immobilized onto Mesoporous Magnetic Hybrid Nanoflowers for Enzymatic Decolorization of Textile Dyes: A Highly Robust Bioreactor and Boosted Enzyme Stability

Horseradish Peroxidase Immobilized onto Mesoporous Magnetic Hybrid Nanoflowers for Enzymatic Decolorization of Textile Dyes: A Highly Robust Bioreactor and Boosted Enzyme Stability

Graphene Oxide Nanocomposites as a Promising Photocatalyst in the Degradation of Organic Dyes

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