PURIFICATION AND PARTIAL CHARACTERISATION OF A PROTEASE INHIBITOR FROM Mimosa diplotricha

Search for inhibitors to insect proteases is one of many strategies control pests. Previous work has demonstrated successful purification effective from plant origin. Thus, the current study attempted purify protease locally available medicinal plants. The that ethanolic extracts Mimosa diplotricha leaves caused a significant 80% reduction in bovine trypsin activity. inhibitory property proteinaceous nature extract was reconfirmed through qualitative analysis using detection on SDS-PAGE technique. ammonium precipitated inhibitor purified Hi-Trap G25 and resolved into single band with molecular weight approximately 20.8 kDa. By Dixon plot competitive Ki value 2.16 × 10-4 mM. protein inhibited Chrysomya megacephala at IC50 28 μg/mL. results highlighted presence its potential as pest agent.