فصل ودراسة إنزيم اللاكتوبيروكسيديز من حليب الإبل والجاموس المحلي

The research included the separation of lactoperoxidase (LP) from camel and buffalo milk locality using different biochemical techniques. One proteinous band had been isolated by gel filtration using sephadex)G-50 and G-100) that produced by ammonium sulphate precipitation. The apparent molecular weight of the isolated protein as a source of enzyme using gel filtration chromatography (G-100) was (75219 + 900) Dalton for camel milk and (76493 + 1000) Dalton for buffalo milk.The results showed that the purified LP from camel and buffalo milk were at (70 µg/ml) of enzyme concentration using (0.08 mol/l) phosphate buffer at pH (7) act for (25) minutes at (45C) and (400 mmol/l) of pyrogallol as a substrate. Using Line Weaver-Burk plot, the values of maximum velocity (Vmax) and Michaelis constant (Km) were found to be (3.49 µmol/ min) and (26.3 mmol/l) respectively for camel milk and (4.44 µmol/ min) (45.4 mmol/l) for buffalo milk.Finally, the research was, also, involve the study of the effect of some chemicals and drugs on the enzyme activity. The results showed the sodium meta arsenite (NaAsO2) uncompetitive inhibitor while phenylphrine is noncompetitive inhibitor for the enzyme at different concentrations of inhibitor, but disodium ethylene diamine tetra acetic acid (Na2-EDTA) and tetracycline were activators to LP.