Superoxide dismutases (SODs) from thermoacidophilic organisms have industrial relevance because of their unique biochemical properties in comparison to their bacterial homologues. In this study, the Ta0013 orf from the thermoacidophilic archeon Thermoplasma acidophilum genome was cloned, expressed and the recombinant protein characterized. The yield of purified recombinant T. acidophilum SOD (TaFeSOD) was 43.51 mg/l and identified as an iron-containing protein by inductively coupled plasma optical emission spectrometry (ICP-OES). Electrophoretic analysis resulted in a single band of 25 kDa and native form of the enzyme was confirmed as a homotetramer. The specific activity of the purified enzyme was 118.5 U/mg at 23 °C and active at a temperature range between 15-60 °C and pH range 2-10. We found 100% thermostability at 50 ºC for 60 min. The enzyme was inactivated by 10 mM hydrogen peroxide after 15 min incubation at 25 °C and pH 7.8. Due to the characteristics presented here we propose TaFeSOD as a potential product for biotechnological applications as a reagent in the preparation of drugs, cosmetics, and/or biochemical substances.