Purification and characterization of L-asparaginase extracted from local Iraqi green beans (Phaseoulus vulgaris)

The most prevalent metabolite for the storage and transport of nitrogen used in protein production is L-asparagine; earlier studies, L-asparaginase enzyme derived from microorganisms was utilized to treat cancer cells; therefore, this study aimed purify describe Iraqi green bean seeds rather than microbial sources. enzymes were partially purified beans by short steps, including centrifugation crude enzyme, dialysis Diethylaminoethyl Sepharose Column, equilibrated using 20 mM Tris-HCl buffer, pH 8.0, then applied a sephacryl S-200. Coulometric methods measured enzymatic activity at 450 nm, unit calculated comparing it standard curve. Purification yielded 5 percent yield, 2.7 fold increase activity, 43 unit/ml activity. asparaginase optimal 8.0. After one-day incubation period, became more stable levels ranging 7.5 9.5. This had same temperature thermal stability 40°C, but temperatures allowing retain its maximal