Isolation and partial characterization of a protease enzyme from Thaumatococcus daniellii waste

A protease enzyme was isolated and partially purified from the pulp ofThaumatococcus daniellii fruit by gel filtration on sephadex G-75 followed by ion-exchange column chromatography on DEAE-cellulose. 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 Km andVmax 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.   Key words: Protease, isolation, characterization, Thaumatococcus danielii.