Superoxide dismutases (SOD) are considered key factors in cellular protection against superoxide, representing the first line of defense to prevent oxidative damage, being the most powerful antioxidant in the cell. SOD catalyzes the dismutation of superoxide anion to hydrogen peroxide (H2O2), which is further transformed to water (H2O) and molecular oxygen (O2) by the accessory enzymes glutathione peroxidase (GPx) and catalase (CAT).
Given the critical function of SOD, these enzymes can be found in all taxonomic groups of living organisms, from prokaryotes (archaea and bacteria) to lower and higher eukaryotes, differing in the number of different enzymes they possess. All known SOD are metalloenzymes, that is, they require a metal cofactor for the activity, with iron (Fe), zinc (Zn), nickel (Ni), copper (Cu) and manganese (Mn) being those normally bound to SOD.
TetraSOD® exhibits the highest SOD activity found currently in nature. Under the production technology developed by Fitoplancton Marino, figures higher than 30,000 IU/g of biomass can be measured. A detailed bioinformatic analysis of the available genetic information for the microalgae T. chuii has allowed the identification of three genes encoding for SOD, each one potentially corresponding to either Mn, Cu-Zn, or Ni isoforms. The combined action of these three enzymes contributes to the extremely high global SOD activity displayed by TetraSOD®.