The enzyme linamarase (E. C. 3.2.1.21) has been purified from cassava cortex (Manihot caculenta) by techniques involving acetone precipitation, ammonium sulfate fractionation, gel filtration and ion-exchange chromatography. Two peaks of linamarase activity (A & B) were eluted by linear gradient on DEAE-Sephadex column. Both forms of the enzyme were found to catalyze similar reactions, however, at different rates. Double reciprocal plots from initial velocity data gave Km of 1.47 mM & 1.44 mM for linamarase A & B, respectively, with linamarin as substrate. The Km values with the artificial substrate para-nitrophenyl glucoside (PNP-G) were 0.48 mM, Both enzyme forms exhibited maximal activity at pH 6.0 and 30°C. Arrhenius plots gave activation energy (Ea) as 49 KJ/mole (11.72 Kcal mole−1) and 36.5 KJ/mole (8.72 Kcal mole−1) for linamarase A & B, respectively. Analysis of cyanide levels in cassava and its products with the crude enzyme showed the leaves to contain high levels of the toxic factor.