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Updated: May 12, 2026
11:16
Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
Published on: July 11, 2012
16.3K
Modulating ion migration realizes both enhanced and long-term-stable nanozyme activity for efficient microplastic
Pingping Wan1, Guanghui Chen1, Jinsong Fan1
1State Key Laboratory of Chemo and Biosensing, College of Chemistry and Chemical Engineering, Hunan University Changsha 410082 P. R. China kunli@hnu.edu.cn.
Chemical Science
|August 13, 2025
Summary
This study introduces manganese-doped lithium iron phosphate (LFMP) nanozymes to efficiently degrade microplastics. The engineered LFMP nanozymes show improved catalytic activity and stability, overcoming common nanozyme limitations.
Area of Science:
- Materials Science
- Environmental Science
- Catalysis
Background:
- Microplastic degradation is a critical environmental issue requiring advanced catalytic solutions.
- Nanozymes offer cost-effective, multi-enzyme mimicry but suffer from self-consumption, limiting practical applications.
- Improving nanozyme stability and activity is essential for effective environmental remediation.
Purpose of the Study:
- To engineer manganese-doped lithium iron phosphate (LFMP) nanozymes to enhance catalytic activity and stability for microplastic degradation.
- To investigate the role of Mn2+ doping in modulating ion migration and lattice structure for improved nanozyme performance.
- To address the self-consumption issue in nanozymes through lattice expansion strategies.
Main Methods:
- Density Functional Theory (DFT) calculations to analyze the effects of Mn2+ doping on LFP's electronic structure and ion migration.
- Synthesis and characterization of Mn-doped LFP (LFMP) nanozymes.
- Assessing the peroxidase-like activity and cycling stability of LFMP nanozymes in degrading polyamide 6, HDPE, and polypropylene microplastics.
Main Results:
- DFT calculations confirmed that Mn2+ doping expands the LFP lattice and narrows the bandgap, enhancing Li+ migration.
- LFMP nanozymes exhibited 3 times higher peroxidase-like activity compared to undoped LFP.
- LFMP demonstrated superior cycling stability, retaining 80% activity after 5 cycles versus 45% for LFP, enabling efficient microplastic degradation.
Conclusions:
- Lattice expansion via Mn2+ doping effectively enhances nanozyme catalytic activity and stability by modulating ion migration.
- LFMP nanozymes provide a promising bio-inspired strategy for efficient microplastic degradation, overcoming nanozyme self-consumption limitations.
- This approach offers a new paradigm for designing robust and highly active nanozymes for environmental applications.
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