Catalase is one of the most important antioxidative enzymes. Its main function is the decomposition of hydrogen peroxide belonging to the group of reactive oxygen species. Disbalance in hydrogen peroxide metabolism in the skin associated with reduced catalase expression can result in the development of skin diseases, such as vitiligo, polymorphic light eruption, and xeroderma pigmentosum. For some of these conditions, the topical application of exogenous catalases was suggested to support the natural antioxidative system. The purpose of our work was to develop an in vitro method allowing for the investigation of H2O2 decomposition at controlled conditions where the antioxidative enzyme is residing in a realistic biological matrix and to assess the catalase activity and the apparent kinetics of catalase in keratinocytes and stratum corneum (SC) samples and to make a comparison with the corresponding catalase function in defatted algae biomass (DAB), which may serve as a potential source of catalase and other antioxidative enzymes or metabolites to be used in skin care applications.
Catalases are the only group of enzymes able to generate gaseous oxygen therefore measurements of enzyme activity were based on the Clark oxygen electrode, which was employed to determine the concentration of oxygen produced by the catalase in various biological samples related to the skin organ or potential green sources of catalase to be used as a skin care ingredient.
In conclusion, the results of our work illustrate the advantages of the simple and highly available oxygen electrode method, such as its versatility and ability to provide fast and accurate measurements with small sample amounts of various biological samples of varying complexity, such as keratinocytes, excised SC, and DAB. By using this method, we demonstrated that DAB, a byproduct from food supplement manufacturing, retains quantifiable and hopefully valuable catalase activity after oil extraction and prolonged storage time.