Partial Purification of Metalloprotease from Acacia farnesiana

Not previously studied metalloprotease was tested in four species of leguminosae, purified and characterized from Acacia farnesiana which have maximum specific activity 25.01 U/mg. Precipitation by 50% ammonium sulfate referred to increase of specific activity (35.84) U/mg while loading on DEAE-Cellulose exchanger pointed out elevation of specific activity and purification fold, 51.39 unit/mg and 2.06 respectively. Molecular mass, pH and temperature optima of purified metalloprotease were 55.11kDa, 7.5 and 50oC respectively. All metal ions were decreased enzyme activity except the zinc showed the increasing about 16%. EDTA was inhibiting the activity in otherwise other inhibitor not affected on enzyme activity. Optimum substrate for activity was BSA and has Km and Vmax 1.11mM and 625 mM/ min respectively.