This study details on cloning and characterization of Cu,Zn superoxide dismutase (Ca–Cu,Zn SOD) from a medicinally important plant species Curcuma aromatica. Ca–Cu,Zn SOD was 692bp with an open reading frame of 459bp. Expression of the gene in Escherichia coli cells followed by purification yielded the enzyme with Km of 0.047±0.008μM and Vmax of 1250±24units/mg of protein. The enzyme functioned (i) across a temperature range of −10 to +80°C with temperature optima at 20°C; and (ii) at pH range of 6–9 with optimum activity at pH 7.8. Ca–Cu,Zn SOD retained 50% of the maximum activity after autoclaving, and was stable at a wide storage pH ranging from 3 to 10. The enzyme tolerated varying concentrations of denaturating agent, reductants, inhibitors, trypsin, was fairly resistant to inactivation at 80°C for 180min (kd, 6.54±0.17×10−3 min−1; t1/2, 106.07±2.68min), and had midpoint of thermal transition (Tm) of 70.45°C. The results suggested Ca–Cu,Zn SOD to be a kinetically stable protein that could be used for various industrial applications.