Isolation, purification and characterization of a protease from the seeds of Artocarpus heterophyllus

Proteases are being widely used in various industries like detergent, leather, food and pharmaceuticals.Protease was purified to homogeneity from the seeds of Artocarpus heterophyllus. The enzyme found be a tetramer having molecular mass 74 kDa. Gelatin zymography showed clear band proteolysis. isolated serine protease, as indicated by its inhibition with PMSF. stable at broad pH temperature ranges optima 8.5 50°C, respectively. presence some divalent ions enhanced activity. With addition calcium, change absorption emission spectra observed spectrofluorometric analysis. Km Vmax for 0.229 µM 0.014 min-1, respectively, using BAPNA substrate. consisted 4.44% alpha helix 44.17% beta sheets when measured CD spectra. Dynamic light scattering protease particle size distribution revealed mono-dispersity sample. Easy purification paramount stability makes it good candidate industrial pharmaceutical applications.