Dismutation of superoxide by superoxide dismutase (SOD) generates hydrogen peroxide, which may be reduced to hydroxyl radical. The generated H₂O₂ during the catalysis can have an oxidative damage to SOD. Hydrogen peroxide decomposition by catalase (CAT) can help circumvent the problem. Mn-superoxide dismutase (herein referred to as SOD) and CAT are dimeric and tetrameric proteins, respectively. Herein, through intein-mediated in vivo subunit splicing, the C-terminus of the CAT subunit (CAT^S) has been specifically ligated to the N-terminus of the SOD subunit (SOD^S) with a peptide bond. Thus, the splicing product SOD&CAT combines the superoxide anion (•O₂⁻) scavenging ability and the ability of decomposing H₂O₂. The in vivo subunit splicing has little effect on the secondary structures of the enzymes as confirmed by circular dichroism (CD) spectra. Fluorescence spectra showed that the splicing product SOD&CAT has a higher stability than SOD. In the splicing product SOD&CAT, the SOD subunits are in close proximity to the CAT subunits, facilitating immediate transfer of H₂O₂ between the enzymes and enabling efficient decomposition of H₂O₂. SOD&CAT exhibited a superoxide anion (•O₂⁻) scavenging ability 244% higher than that of SOD and 46% higher than that of the mixed enzymes SOD+CAT.