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Research Article
Abeer A. Khamis
Tanta University Faculty of Science
Corresponding Author
ORCiD: https://orcid.org/0000-0001-5216-2712
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This work is licensed under a CC BY 4.0 License. Read Full License
To enhance the removal of dye, horseradish peroxidase (HRP) was immobilized onto amine-functionalized superparamagnetic iron oxide and used as a biocatalyst for the oxidative degradation of Acid black-HC dye. The anchored enzyme was characterized by sets of techniques such as vibrating sample magnetometer, Fourier transform infrared, X-ray diffraction, thermogravimetric, scanning electron microscopy, BET and BJH methods, nitrogen adsorption-desorption measurements , Zeta potential, energy dispersive X-ray (EDX), and transmission electron microscopy. The Michaelis constant (K m ) values of free peroxidase and immobilized horseradish peroxidase were determined that equal 4.5 and 5 mM for hydrogen peroxide; 12.5 and 10 mM for guaiacol, respectively. Besides, the free peroxidase is thermally stable at 40°C however, the immobilized enzyme was up to 60°C. In the catalytic experiment, the immobilized HRP showed superior catalytic activity compared with free HRP for the oxidative decolorization and removal of Acid black-HC dye. The impacts of experimental parameters for instance catalyst dosage, pH, H 2 O 2 concentration, and temperature, were investigated. The reaction followed second-order kinetics and the thermodynamic activation parameters were determined.
Keywords
Horseradish peroxidase, immobilization, Enzymatic kinetic, 3- aminopropyl trimethoxysilane.
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This preprint is under consideration at Environmental Science and Pollution Research. A preprint is a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Learn more about In Review
Research Article
Abeer A. Khamis
Tanta University Faculty of Science
Corresponding Author
ORCiD: https://orcid.org/0000-0001-5216-2712
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
Peer Review Timeline
CURRENT STATUS: Under Review
Version 1
Posted 22 Mar, 2021
No community comments so far
Review #? received
Received 13 Apr, 2021
Reviewers invited
Invitations sent on 17 Mar, 2021
Editor invited
On 16 Mar, 2021
Editor assigned
On 07 Mar, 2021
First submitted
On 04 Mar, 2021
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
License:
This work is licensed under a CC BY 4.0 License. Read Full License
To enhance the removal of dye, horseradish peroxidase (HRP) was immobilized onto amine-functionalized superparamagnetic iron oxide and used as a biocatalyst for the oxidative degradation of Acid black-HC dye. The anchored enzyme was characterized by sets of techniques such as vibrating sample magnetometer, Fourier transform infrared, X-ray diffraction, thermogravimetric, scanning electron microscopy, BET and BJH methods, nitrogen adsorption-desorption measurements , Zeta potential, energy dispersive X-ray (EDX), and transmission electron microscopy. The Michaelis constant (K m ) values of free peroxidase and immobilized horseradish peroxidase were determined that equal 4.5 and 5 mM for hydrogen peroxide; 12.5 and 10 mM for guaiacol, respectively. Besides, the free peroxidase is thermally stable at 40°C however, the immobilized enzyme was up to 60°C. In the catalytic experiment, the immobilized HRP showed superior catalytic activity compared with free HRP for the oxidative decolorization and removal of Acid black-HC dye. The impacts of experimental parameters for instance catalyst dosage, pH, H 2 O 2 concentration, and temperature, were investigated. The reaction followed second-order kinetics and the thermodynamic activation parameters were determined.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
Figure 7
Figure 8
Figure 9
Figure 10
Figure 11
Figure 12
Figure 13
Figure 14
Figure 15
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