Biocatalytic degradation of reactive blue 221 and direct blue 297 dyes by horseradish peroxidase immobilized on iron oxide nanoparticles with improved kinetic and thermodynamic characteristics

Kalsoom, Umme; Khalid, Nasira; Ibrahim, Affaf; Ashraf, S. Salman; Bhatti, Haq Nawaz; Ahsan, Zainab; Zdarta, Jakub; Bilal, Muhammad

doi:10.1016/j.chemosphere.2022.137095

Cited by 27 publications

(7 citation statements)

References 35 publications

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“…For instance, Weber et al reported that immobilized HRP on calcium alginate-starch hybrid support achieved around 30% color elimination from a solution of 100 mg/L of PR after 8 cycles. In another work, HRP isolated from fresh leaves of Moringa Oliefera on iron oxide NPs degraded reactive blue 221 and direct blue 297 dyes by 0.6 and 12%, respectively, after the fifth cycle . Based on the result obtained in the present study, HRP@Fe 3 O 4 –NH 2 /hNFs show great promise in environmental applications, including wastewater treatment and enzymatic water purification.…”

Section: Resultssupporting

confidence: 66%

“…In another work, HRP isolated from fresh leaves of Moringa Oliefera on iron oxide NPs degraded reactive blue 221 and direct blue 297 dyes by 0.6 and 12%, respectively, after the fifth cycle. 60 Based on the result obtained in the present study, HRP@Fe 3 O 4 −NH 2 / hNFs show great promise in environmental applications, including wastewater treatment and enzymatic water purification.…”

Section: ■ Introductionsupporting

confidence: 62%

“…Unlike free HRP, HRP@Fe 3 O 4 –NH 2 /hNFs showed the highest activity at 80 °C. A shift in optimum temperature was observed due to hydrophobic and other secondary interactions between the enzyme and the supporting environment . Although free HRP exhibited high relative activity at lower temperatures, it did not show activity at temperatures higher than 60 °C.…”

Section: Resultsmentioning

confidence: 95%

“…This phenomenon occurs due to conformational changes in the enzyme, electrostatic interaction between the enzyme and the environment, the nature of the microenvironment, and the supporting environment . Various works involving the immobilization of peroxidase enzymes in different supports have reported similar changes in kinetic parameters after immobilization, such as those of Weber et al, Kalsoom et al, Bilal and Asgher …”

Section: Resultsmentioning

confidence: 97%

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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: Resultssupporting

confidence: 66%

Section: ■ Introductionsupporting

confidence: 62%

Section: Resultsmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 97%

See 2 more Smart Citations

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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“…The expansion of the global industry has resulted in a significant increase in the presence of a variety of pollutants in the environment that can negatively impact both human health and the environment. Biocatalytic systems based on HRP immobilized onto nanomaterials have remarkable potential for purifying surface waters and wastewaters of a wide range of impurities, such as dyes, pharmaceuticals, pesticides, phenols, and everyday products [26][27][28][29]. A study by Aldhari et al [26] demonstrated that HRP immobilized on copper oxide nanosheets is an efficient means of degrading a variety of dyes (crystal violet, methyl green, malachite green).…”

Section: Introductionmentioning

confidence: 99%

Support Materials of Organic and Inorganic Origin as Platforms for Horseradish Peroxidase Immobilization: Comparison Study for High Stability and Activity Recovery

Bilal,

Degorska,

Szada

et al. 2024

Molecules

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In the presented study, a variety of hybrid and single nanomaterials of various origins were tested as novel platforms for horseradish peroxidase immobilization. A thorough characterization was performed to establish the suitability of the support materials for immobilization, as well as the activity and stability retention of the biocatalysts, which were analyzed and discussed. The physicochemical characterization of the obtained systems proved successful enzyme deposition on all the presented materials. The immobilization of horseradish peroxidase on all the tested supports occurred with an efficiency above 70%. However, for multi-walled carbon nanotubes and hybrids made of chitosan, magnetic nanoparticles, and selenium ions, it reached up to 90%. For these materials, the immobilization yield exceeded 80%, resulting in high amounts of immobilized enzymes. The produced system showed the same optimal pH and temperature conditions as free enzymes; however, over a wider range of conditions, the immobilized enzymes showed activity of over 50%. Finally, a reusability study and storage stability tests showed that horseradish peroxidase immobilized on a hybrid made of chitosan, magnetic nanoparticles, and selenium ions retained around 80% of its initial activity after 10 repeated catalytic cycles and after 20 days of storage. Of all the tested materials, the most favorable for immobilization was the above-mentioned chitosan-based hybrid material. The selenium additive present in the discussed material gives it supplementary properties that increase the immobilization yield of the enzyme and improve enzyme stability. The obtained results confirm the applicability of these nanomaterials as useful platforms for enzyme immobilization in the contemplation of the structural stability of an enzyme and the high catalytic activity of fabricated biocatalysts.

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Porous Nanomaterials for Enzyme Immobilization and Bioremediation Applications

Hussain,

Shahbaz,

Malik

et al. 2024

Microbes Based Approaches for the Management of Hazardous Contaminants

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Biocatalytic degradation of reactive blue 221 and direct blue 297 dyes by horseradish peroxidase immobilized on iron oxide nanoparticles with improved kinetic and thermodynamic characteristics

Cited by 27 publications

References 35 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

Support Materials of Organic and Inorganic Origin as Platforms for Horseradish Peroxidase Immobilization: Comparison Study for High Stability and Activity Recovery

Porous Nanomaterials for Enzyme Immobilization and Bioremediation Applications

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