BACKGROUND: Lactoperoxidase is an enzyme of the oxidoreductase family. Lactoperoxidase is an important antimicrobial agent. Applications of lactoperoxidase are being found as a preservative in food and cosmetics. Immobilized LPO provides several significant benefits such as: easily separated from the reaction products, reducing production costs by efficient recycling and control of the process. Objectives: Purification and immobilization of lactoperoxidase extracted from camel milk using sodium alginate polymer. Methods: The lactoperoxidase was purified from camel milk by using sephadex G-100 gel filtration CM and sephadex C-50 ion-exchange chromatography. Encapsulation was carried out by using LPO, sodium alginate, glycerol and Tween 80. Afterward, the microcapsules were stablized by calcium ion (1%). Efficiency of encapsulation was calculated. The particle size and distribution were measured with particle size analyzer. Morphology and formation of the particles were studied  using Scanning Electron Microscope (SEM). Stability of encapsulated and uncapsulated  LPO was studied at 4 °C during 70 days. Results: After purification and purity measurement by SD-SPAGE, concentration of 0/28 micrograms per liter for each of the fractions was obtained. Microencapsulation efficiency was 84% and microcapsules  less than 200 nm were formed. Observation by SEM confirmed the formation of microparticles. Microcapsules have a relatively smooth surface, spherical with low tenacity as well. Stability of encapsulated enzyme at 70 days was obtained 81%. Conclusions: Immobilization of Lactoperoxidase extracted from camel milk  using sodium alginate is a good method to increase performance of the enzyme.