A protease enzyme was isolated and partially purified from the pulp of Thaumatococcus daniellii fruit by gel filtration on sephadex G-75 followed by ion-exchange column chromatography on DEAEcellulose. The enzyme showed a specific activity of 4.75 × 10 -1 unit/mg protein and 6.93 × 10 -1 unit/mg protein, respectively after each purification procedure. The purified enzyme had a K m and V max of 2.0 × 10 -4 M and 1.53 mol/min, respectively, using casein as substrate. The enzyme had an optimum temperature of 35°C and functioned best at pH 7.0 with some residual activity at alkaline pH.