Immobilization of horseradish peroxidase on Fe 3 O 4 magnetic nanoparticles

Mohamed, Saleh A.; Al-Harbi, Majed H.; Almulaiky, Yaaser Q.; Ibrahim, Ibrahim H.; El‐Shishtawy, Reda M.

doi:10.1016/j.ejbt.2017.03.010

Cited by 115 publications

(54 citation statements)

References 39 publications

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“…These results indicated that the immobilization of the enzyme did not affect the substrate's binding site in the enzyme. Similar findings were reported by Mohamed et al [20]. Using different concentrations of H2O2 (1.6-9.7mM) and guaiacol (20-58.8 mM) as the substrates, Using different concentrations of H 2 O 2 (1.6-9.7mM) and guaiacol (20-58.8 mM) as the substrates, the effect of substrates concentration was studied in terms of the rate of catalysis by the immobilized and free enzyme forms.…”

Section: Resultssupporting

confidence: 92%

“…These results indicated that the immobilization of the enzyme did not affect the substrate's binding site in the enzyme. Similar findings were reported by Mohamed et al [20].…”

Section: Resultssupporting

confidence: 92%

“…Besides the enhanced performance characteristics, the important behaviors of the nanoparticles also highlighted the interesting transition region between homogeneous and heterogeneous catalysis [18]. Magnetic nanomaterials were used in protein immobilization in various capacities [16,19]; for example, non-modified magnetic Fe 3 O 4 nanoparticles were physically immobilized on peroxidase, preserving 55% of original activity after being used 10 times [20]. Figure 1 shows a schematic illustration of HRP encapsulation onto a magnetic Fe 3 O 4 Np-PMMA film via casting.…”

Section: Resultsmentioning

confidence: 99%

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Encapsulation of HRP Enzyme onto a Magnetic Fe3O4 Np–PMMA Film via Casting with Sustainable Biocatalytic Activity

2020

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Horseradish peroxidase (HRP) enzyme was effectively encapsulated onto an Fe3O4 nanoparticle–polymethyl methacrylate (PMMA) film via the casting method. The HRP was immobilized on the 0.5% Fe3O4Np–PMMA film and characterized by Fourier transform infrared spectroscopy and field emission scanning electron microscopy. Moreover, the reusability, thermal stability, optimum pH, optimum temperature, the influence of metal ions, and the effects of detergent and organic solvent were investigated. After optimizing the immobilization conditions, the highest efficiency of the immobilized enzyme was 88.4% using 0.5% Fe3O4Np–PMMA. The reusability of the immobilized HRP activity was 78.5% of its initial activity after being repeatedly used for 10 cycles. When comparing the free and immobilized forms of the HRP enzyme, changes in the optimum temperature and optimum pH from 30 to 40 °C and 7.0 to 7.5, respectively, were observed. The Km and Vmax for the immobilized HRP were estimated to be 41 mM, 0.89 U/mL for guaiacol and 5.84 mM, 0.66 U/mL for H2O2, respectively. The high stability of the immobilized HRP enzyme was obtained using metal ions, a high urea concentration, isopropanol, and Triton X-100. In conclusion, the applicability of immobilized HRP involves the removal of phenol in the presence of hydrogen peroxide, therefore, it could be a potential catalyst for the removal of wastewater aromatic pollutants.

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Section: Resultssupporting

confidence: 92%

“…These results indicated that the immobilization of the enzyme did not affect the substrate's binding site in the enzyme. Similar findings were reported by Mohamed et al [20].…”

Section: Resultssupporting

confidence: 92%

Section: Resultsmentioning

confidence: 99%

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Encapsulation of HRP Enzyme onto a Magnetic Fe3O4 Np–PMMA Film via Casting with Sustainable Biocatalytic Activity

2020

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“…Peroxidases are implicated in various applications in detoxification of recalcitrant organopollutants, decolourization of textile effluents, in bioremediation, polymer synthesis, paper and pulp industry, in development of biosensor, diagnosis kits, etc. (Lavery et al 2010;Bhatti et al 2012;Kalsoom et al 2013;Sarvamangala 2014;Nouren et al 2015;Tabassum et al 2015;Mohamed et al 2017;Moubasher et al 2017).…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of cationic peroxidase from ginger (Zingiber officinale)

et al. 2020

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Background: Due to versatility in reaction catalyzed by peroxidases, they have potential applications in different areas in the health sciences, food industry, and diagnostic purposes. Therefore, the aim of this study is to investigate the properties of peroxidase from ginger to be meeting the perquisites of several applications. Results: The cationic peroxidase (GPII) was purified to homogeneity by anion exchange chromatography using DEAE-Sepharose column followed by cation exchange chromatography using CM-Sepharose column and finally Sephacryl S-200 column. The molecular mass of GPII was 42 kDa. GPII shows oxidizing activity with several phenolic compounds by using H 2 O 2 as the second substrate. The natural plant phenolic compounds as pyrogallol, catechol, and guaiacol were found to be excellent electron donors for the enzyme compared to other phenolic compounds. GPII exhibited K m values of 3.1 and 7.1 mM and V max values of 0.6 and 0.31 units/assay using H 2 O 2 and guaiacol as substrates, respectively. The enzyme exhibited maximal peroxidase activity at broad pH's 6.0-7.5 and 50°C. GPII was thermal stable up to 50°C and retained 66% of its activity at 70°C after 1 h incubation. The GPII activated by most divalent cations tested and inhibited by Hg 2+ and Cu 2+ cations. Conclusion: PGII could be used in several applications due to its catalytic properties, thermal stability, broad pH, and acting on several phenolic compounds.

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“…In this work we present a competitive electrochemical assay in which the measured current values (related to WOR, being catalyzed by the presence of IrO2 NPs) are inversely proportional to the concentration of BDE-47 in liquid sample. We take advantage of magnetic beads (MBs) coated with anti-PBDE antibodies to capture BDE-47 and horseradish peroxidase (HRP)-PBDE conjugate to link IrO2 NPs to PBDE (HRP can be conjugated on IrO2 NPs surface, as has been reported on other nanomaterials: Cui et al, 2008;Mohamed et al, 2017). Then, in absence of BDE-47, the conjugate MBs/PBDE-IrO2NPs will be formed, leading to a high electrocatalytic signal.…”

Section: Introductionmentioning

confidence: 99%

Iridium oxide (IV) nanoparticle-based electrocatalytic detection of PBDE

Quesada-González

Baiocco

Martos

et al. 2019

Biosensors and Bioelectronics

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Polybrominated diphenyl ethers (PBDEs) are a type of flame retardants which are currently banned in EU and USA due their hazardousness for humans and mammals. However, these compounds were highly used during more than 30 years and still persist in the environment since they are resistant to degradation. Herein we present a biosensor for the detection of PBDEs using screen printed carbon electrodes (SPCEs) based on the electrochemical monitoring of water oxidation reaction (WOR) catalyzed by iridium oxide (IV) nanoparticles (IrO2 NPs). Our assay shows a limit of detection of 21.5 ppb of PBDE in distilled water. We believe that such an IrO2 NPs-based electrocatalytic sensing system can lead to a rapid, sensitive, low cost and miniaturizable device for the detection of PBDEs.

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Immobilization of horseradish peroxidase on Fe 3 O 4 magnetic nanoparticles

Cited by 115 publications

References 39 publications

Encapsulation of HRP Enzyme onto a Magnetic Fe3O4 Np–PMMA Film via Casting with Sustainable Biocatalytic Activity

Encapsulation of HRP Enzyme onto a Magnetic Fe3O4 Np–PMMA Film via Casting with Sustainable Biocatalytic Activity

Purification and characterization of cationic peroxidase from ginger (Zingiber officinale)

Iridium oxide (IV) nanoparticle-based electrocatalytic detection of PBDE

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