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Updated: May 12, 2026

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
Published on: July 11, 2012
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.
Abstract:
Degradation of microplastics represents a significant global environmental challenge, necessitating the development of bio-inspired catalysts with superior activity and stability, capable of mimicking natural plastic-degrading enzymes. Although nanozymes possess advantages such as low cost, ready availability, and multienzymatic activities, issues of self-consumption often hinder their practical application. Here, motivated by the acceleration of Li+ migration for improving the electrochemical reactivity and cycling stability of lithium iron phosphate (LFP), we engineered LFP by introducing Mn2+ to expand the lattice structure, resulting in Mn-doped LFP (LFMP) that modulates ion migration in nanozymes. Density functional theory (DFT) calculations reveal that Mn2+ doping expands the lattice structure of LFP while narrowing its bandgap, thereby significantly enhancing Li+ migration rates. Leveraging this design, LFMP exhibits enhanced peroxidase-like activity (3 times higher than that of LFP) and cycling stability (80% activity retention after 5 cycles versus 45% for LFP), enabling efficient degradation of microplastics made from polyamide 6, high-density polyethylene, and polypropylene. By exemplifying that the degradation efficiency achieved using LFMP nanozymes significantly exceeds that of traditional methods, we affirm that lattice expansion-driven ion migration may inspire future strategies to circumvent the self-consumption issue while maintaining high catalytic activity in nanozymes.
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