Optimization of Interfacial Properties Improved the Stability and Activity of the Catalase Enzyme Immobilized on Plastic Nanobeads.

The immobilization of catalase (CAT), a crucial oxidoreductase enzyme involved in quenching reactive oxygen species, on colloids and nanoparticles presents a promising strategy to improve dispersion and storage stability while maintaining its activity. Here, the immobilization of CAT onto polymeric nanoparticles (positively (AL) or negatively (SL) charged) was implemented directly (AL) or via surface functionalization (SL) with water-soluble chitosan derivatives (glycol chitosan (GC) and methyl glycol chitosan (MGC)). The interfacial properties were optimized to obtain highly stable AL-CAT, SL-GC-CAT, and SL-MGC-CAT dispersions, and confocal microscopy confirmed the presence of CAT in the composites. Assessment of hydrogen peroxide decomposition ability revealed that applying chitosan derivatives in the immobilization process not only enhanced colloidal stability but also augmented the activity and reusability of CAT. In particular, the use of MGC has led to significant advances, indicating its potential for industrial and biomedical applications. Overall, the findings highlight the advantages of using chitosan derivatives in CAT immobilization processes to maintain the stability and activity of the enzyme as well as provide important data for the development of processable enzyme-based nanoparticle systems to combat reactive oxygen species.