Stable SOD and Catalase for Cosmetic Formulations

Superoxide dismutase and catalase work as a two-step antioxidant cascade, converting superoxide and the hydrogen peroxide it generates into water and oxygen. The revision addresses the stability gap that limits conventional enzyme actives during cosmetic manufacturing.


Superoxide dismutase and catalase work as a two-step antioxidant cascade, converting superoxide and the hydrogen peroxide it generates into water and oxygen.

Why oxidative stress matters to skincare formulators

Skin is continuously exposed to reactive oxygen species (ROS) generated by mitochondrial metabolism, inflammation, UV radiation, and pollution. Among environmental stressors, UV exposure is the most relevant for cosmetic R&D: UVA penetrates deeply into the dermis and generates ROS through photosensitization, while UVB causes direct epidermal injury and further stimulates ROS production (Pandel et al., 2013). Accumulated ROS oxidize lipids, proteins, and nucleic acids, and contribute to photoaging and extracellular matrix degradation (Pandel et al., 2013). This rationale is why enzyme antioxidants such as SOD and catalase are among the most studied active candidates for serums, creams, and protective formulations (Addor, 2017; Zheng et al., 2023).

The two-enzyme antioxidant cascade

The skin uses two enzymatic steps to defuse reactive oxygen. Superoxide dismutase (SOD) dismutates the superoxide radical into hydrogen peroxide (H₂O₂) and oxygen. Catalase then decomposes that peroxide into water and oxygen (Zheng et al., 2023). Without the second step, the system would simply exchange one reactive species for another, leaving peroxide to accumulate in the local environment. This is why SOD and catalase are positioned as a two-step catalytic antioxidant system rather than as two interchangeable radical scavengers (Nascimento et al., 2024).

Why conventional enzyme actives lose activity in cosmetic manufacturing

If the mechanism is well established, why do so many finished products underperform? The bottleneck is not the chemistry, it is the fragility of the protein. Conventional SOD and catalase preparations from mesophilic sources are prone to denaturation from temperature excursions, shear, non-neutral pH, and incompatible excipients during processing and storage (Bouziani et al., 2026). Classic SOD formulation studies reached the same conclusion: physical and chemical instability limits the practical window of topical SOD (Di Mambro et al., 2004).

The result is a familiar dilemma for development departments: an active that shows high activity on the supplier’s certificate of analysis but loses much of it after the production line. The relevant quality parameter is formulation stability, measured as retained enzymatic activity after emulsification, filling, and accelerated storage, not the nominal amount added (Bouziani et al., 2026).

The advantage of extremozymes in topical formulations

Enzymes from organisms adapted to extreme environments, cold, heat, or high salinity, generally maintain their structure and catalytic function under thermal and chemical stress better than mesophilic counterparts (Sarmiento et al., 2015). In a cosmetic formulation this is a relative advantage: an extremozyme is not immune to denaturation, but it can give the formulator a wider process window, particularly during warm emulsification and storage (Bouziani et al., 2026; Sarmiento et al., 2015).

SwissAustral’s complementary SOD/catalase system

SwissAustral offers a complementary enzymatic antioxidant system for evaluation in cosmetic formulations: a thermotolerant SOD (ENZ_SOD_010) and a cold-active catalase (ENZ_CAT_001), both produced recombinantly in non-pathogenic E. coli.

  • Thermotolerant SOD: Origin: thermophilic bacterium. Maintains over 50% of its activity after 64 hours at 50 °C.
  • Cold-active catalase: Origin: psychrotolerant bacterium. Maintains over 50% of its activity after 7 hours at 50 °C, and stays active at below-freezing temperatures .
  • pH tolerance: The SOD operates between pH 5 and 10 (optimum 7–8); the catalase between pH 4 and 11 (optimum 7), covering most cosmetic formulation ranges.
  • Storage: The SOD retains its reported activity at least for 1 year at −20 °C; the liquid catalase at least 2 years at 20 °C.

As a two-step catalytic antioxidant system, the combination helps neutralize superoxide and removes the secondary hydrogen peroxide, complementing the enzymatic antioxidant defences of the skin (Zheng et al., 2023). Both enzymes originate from SwissAustral’s extremophile collection, the platform described in our previous article on The Collection.

Technical evaluation for R&D teams and laboratories

For formulation laboratories and ODM manufacturers, the decision criterion is not the theoretical antioxidant capacity of the ingredients, but the activity retention of the system after the entire manufacturing process. The recommended validation follows the same logic as the published formulation-stability literature (Bouziani et al., 2026; Di Mambro et al., 2004):

  • Measure catalytic activity before and after each process step (emulsification, filling, pasteurization where applicable).
  • Run real-time and accelerated storage under the final packaging conditions.
  • Test in the actual matrix: representative preservatives, surfactants, and excipients.
  • Compare SOD alone, catalase alone, and the combination against a vehicle control.

This workflow demonstrates whether the two-step neutralization remains intact in the finished product and gives the formulation team the data needed to make supported claims (Nascimento et al., 2024).

Is your formulation team evaluating antioxidant actives for a new cosmetic line? Learn more about SwissAustral’s thermotolerant SOD or its cold-active catalase, and contact the technical team to request samples, the technical dossier, and a stability-testing proposal.

References

Addor, F. A. S. (2017). Antioxidants in dermatology. Anais Brasileiros de Dermatologia, 92(3), 356–362. https://doi.org/10.1590/abd1806-4841.20175697

Bouziani, A., Özel, R., & Güngör, Ö. (2026). Cosmetic enzymes as formulation-integrated actives: Mechanisms, delivery, and functional evidence. Journal of Cosmetic Dermatology, 25(7), Article e71085. https://doi.org/10.1111/jocd.71085

Di Mambro, V. M., Maia Campos, P. M. B. G., & Fonseca, M. J. V. (2004). Physical and chemical stability of different formulations with superoxide dismutase. Pharmazie, 59(10), 786–790. https://pubmed.ncbi.nlm.nih.gov/15544058/

Nascimento, N. S., Torres-Obreque, K. M., Oliveira, C. A., Rabelo, J., Baby, A. R., Long, P. F., Young, A. R., & Rangel-Yagui, C. O. (2024). Enzymes for dermatological use. Experimental Dermatology, 33(1), Article e15008. https://doi.org/10.1111/exd.15008

Pandel, R., Poljšak, B., Godic, A., & Dahmane, R. (2013). Skin photoaging and the role of antioxidants in its prevention. ISRN Dermatology, 2013, Article 930164. https://doi.org/10.1155/2013/930164

Sarmiento, J. E., Peralta, G., & Blamey, K. (2015). Cold and hot extremozymes: Industrial relevance and current trends. Frontiers in Bioengineering and Biotechnology, 3, Article 148. https://doi.org/10.3389/fbioe.2015.00148

Zheng, M., Liu, Y., Zhang, G., Yang, Z., Xu, W., & Chen, Q. (2023). The applications and mechanisms of superoxide dismutase in medicine, food, and cosmetics. Antioxidants, 12(9), Article 1675. https://doi.org/10.3390/antiox12091675


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