Antioxidant cascade reactions detoxifying reactive oxygen species are of significance to control oxidative stresses-triggered diseases. In the present work, the antioxidant catalysts were prepared through the confinement of dual metalloenzymes in liposomes. The amino groups of superoxide dismutase (SOD) were conjugated to the carboxyl groups-bearing liposomes encapsulated with the catalase (CAT) to formulate a spatially organized antioxidant reaction network. The activity of SOD and CAT in the liposomal system was evaluated in detail on the basis of the prolonged xanthine oxidase/xanthine reaction producing superoxide anion radicals (O2̇–) and hydrogen peroxide (H2O2) coupled with redox reactions of cytochrome c. The liposome-confined SOD and CAT molecules were clearly demonstrated to catalyze the sequential disproportionation of O2̇– and H2O2 at 25 °C in a potassium phosphate buffer solution (pH = 7.8) under moderate transfer resistance with respect to the intermediate product (H2O2) within the liposomes. Furthermore, the liposomal catalysts were modified with the poly­(ethylene glycol) (PEG)-conjugated lipids with the molecular mass of the PEG moiety of about 5000 through the post-PEGylation approach. The mean hydrodynamic diameter of the PEGylated liposomal catalysts was 140–150 nm. The dual enzyme activity in liposomes and the thermal stability of the encapsulated CAT were practically unaffected by the PEGylation. The above liposome-based antioxidant catalysts are highly biocompatible, PEG-modifiable, and reactive, thereby making the catalysts potentially applicable to therapeutic materials exhibiting functionality similar to cellular peroxisomes.

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