Isolation of Lactoperoxidase Enzyme from Camel's Milk and Survey Its Antibacterial Effects against Staphylococcus aureus

Lactoperoxidase enzyme is present in various mammalian glands and in their secretions. The lactoperoxidase system is a natural anti-microbial system in milk which results from the interaction between three components; the enzyme lactoperoxidase، thoicyanate ion and hydrogen peroxidase. Hydrogen peroxidase catalyzes the oxidation of thiocyanate to turn it into the antibacterial hypotiocyanate that، in turn، inhibits the growth of bacteria. Lactoperoxidase enzyme was extracted from the milk of camel. Camel milk was centrifuged at 2500 rpm at 4°C for 15 min to remove fat. Camel lactoperoxidase was extracted from raw milk using CM sepHadex C-50 ion exchange chromatography٫ and sephadex G-100 gel filtration chromatography. The activity of lactoperoxidase was measured by using tetramethylbenzidin as achoromogenic substrate. The determination of molecular weight for the extracted enzyme was controlled with SDS-PAGE. Km value for lactoperoxidase was 0. 268 mM. Vmax value was 0/000149 µmol/ ml min. The antibacterial system was prepared. The complete system constituted lactoperoxidase٫ H2O2٫ and tiocyanate. The antibacterial complete system effect was measured on the Staph aureus bacteria. For this purpose، the bacteria were incubated under complete system condition for 360 min. The findings indicated that the antibacterial complete system effect on Staph aureus was 70%. These results showed a significant difference as compared to the control.