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Nanomaterials can regulate the stability and activity of enzymes at the nano-bio interface, providing multifunctional carriers for biocatalysis. However, strong interfacial interactions often disrupt enzyme structures, leading to significant activity loss; at the same time, assembling enzyme-nanomaterial complexes usually relies on trial and error, making rational design difficult. This study proposes a rational strategy to control enzyme activity: constructing amphiphilic enzymes that self-assemble into stable nanoparticles (NPs) in water. Using 4-piperidinyl-1,8-naphthalimide-functionalized glucose oxidase (PPNI–GOx) as a model system, the degree of glutaraldehyde crosslinking is systematically regulated to control nanoparticle size and catalytic performance. The optimized PPNI–GOx nanoparticles exhibit catalytic efficiency comparable to, or even better than, natural glucose oxidase in solution; compared to previously reported glucose oxidase nanoparticles, their catalytic activity increases by up to 66 times. Applying these optimized amphiphilic enzyme nanoparticles to electrochemical glucose sensors results in sensors with high sensitivity, a wide linear range (up to 24 mM), a low detection limit (53.3 μM), and excellent anti-interference selectivity against common interferents. The sensors also show outstanding operational stability, retaining 92% of the initial response after 7 days of long-term testing. In summary, this study demonstrates that nano amphiphilic enzymes are an efficient and tunable platform, capable of enhancing enzyme activity, stability, and sensor performance, providing a groundbreaking new strategy for developing high-performance biocatalysts and next-generation biosensing systems.
Summary
This AFM study introduces Nanoamphizymes, which use amphiphilic units and enzymes to self-assemble, creating enzyme-based nanomaterials. Free natural enzymes usually suffer from poor stability, difficulty in recovery, and low environmental tolerance. In this study, the self-assembled structures help protect enzyme molecules and maintain their protein conformation. This material system achieves both high-performance biocatalysis and biosensing by adapting its amphiphilic structure to complex biological environments while balancing catalytic activity and signal output.
Enzyme immobilization has always been a hot topic in biocatalysis and sensing. This self-assembling amphiphilic strategy avoids the need for complex carrier synthesis, making the preparation process simpler. The approach can be extended to applications like bio-detection, microfluidic sensing, and biomedical probes. Compared to traditional enzyme immobilization methods, the self-assembly strategy offers advantages in simplifying preparation and preserving enzyme activity. Future work could explore combining this system with flexible sensors or in vivo microenvironment detection to uncover more application potential.
Reference:
DOI: 10.1002/adfm.78924
