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A catechol biosensor based on immobilizing laccase to Fe3O4@Au core-shell nanoparticles
Changiz Karami1, Mohammad Ali Taher1
1Department of Chemistry, Faculty of Sciences, Shahid Bahonar University of Kerman, Kerman, Iran.
International Journal of Biological Macromolecules
|February 9, 2019
Summary
Researchers synthesized magnetic core-shell nanoparticles with immobilized laccase (Fe3O4@Au@Lac) for biosensing applications. The developed biosensor showed sensitive and linear detection of catechol.
Area of Science:
- Nanotechnology
- Biochemistry
- Biosensor development
Background:
- Magnetic nanoparticles offer unique properties for immobilization and separation.
- Gold shells provide a stable platform for enzyme attachment.
- Laccase is a versatile enzyme for oxidation-based biosensing.
Purpose of the Study:
- To synthesize and characterize Fe3O4@Au@Lac core-shell nanoparticles.
- To develop a biosensor for catechol detection using the synthesized nanoparticles.
- To optimize biosensor performance and evaluate its kinetic parameters.
Main Methods:
- Synthesis of Fe3O4@Au@Lac core-shell nanoparticles.
- Characterization using TEM, SEM, DLS, zeta potential, UV-Vis, and TGA.
- Biosensing assay based on catechol oxidation monitored by UV-Vis spectroscopy.
Main Results:
- Successful synthesis and characterization of Fe3O4@Au@Lac nanoparticles.
- Optimized biosensor activity at pH 5.0, 40 min reaction time, and 35 mg enzyme loading.
- Linear response to catechol from 5.0-70.0 μM with a limit of detection of 2 μM.
- Apparent Michaelis-Menten constant (Km) determined to be 15 μM.
Conclusions:
- Fe3O4@Au@Lac core-shell nanoparticles are effective platforms for laccase immobilization.
- The developed biosensor demonstrates high sensitivity and a wide linear range for catechol detection.
- This biosensor shows potential for practical applications in environmental monitoring or diagnostics.
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