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 692 bp with an open reading frame of 459 bp. Expression of the gene in Escherichia coli cells followed by purification yielded the enzyme with Km of 0.047 +/- 0.008 mu M and V-max of 1250 +/- 24 units/mg of protein. The enzyme functioned (i) across a temperature range of -10 to +80 degrees C with temperature optima at 20 degrees 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 degrees C for 180 min (k(d), 6.54 +/- 0.17 x 10(-3) min(-1); t(1/2), 106.07 +/- 1 2.68 min), and had midpoint of thermal transition (T-m) of 70.45 degrees C. The results suggested Ca-Cu,Zn SOD to be a kinetically stable protein that could be used for various industrial applications. (C) 2014 Elsevier Ltd. All rights reserved.