Rhodanese, a cyanide detoxifying enzyme, was isolated from soldier termite using ammonium sulphate fractionation, reactive blue affinity chromatography and gel filtration on Sephadex G-150. The enzyme had a specific activity of 7.9 RU per milligram of protein. The K m values of the substrates (KCN and Na 2 S 2 O 3 ) were 7.0 mM and 5.3 mM respectively. The results of substrate specificity showed that the enzyme was specific for thiosulphate (S 2 O 3 2-) when compared with other sulphur compounds. The native and subunit molecular weight of the enzyme was found to be 37,154 and 32,210 dalton respectively. The optimum pH and temperature of the enzyme activity were 8.0 and 55 o C respectively. NH 4 + , Mn 2+ , and Ba 2+ had about 50 % effect on the activity of the enzyme. However, Hg 2+ , Zn 2+ and Mg 2+ inhibited the enzyme considerably (≤ 20 %). The half-life of the enzyme at 40 o C, 50 o C, 60 o C, 70 o C and 80 o C were found to be 150.7, 60.3, 43.0, 37.7 and 37.0 respectively.