The current study aimed to isolate and purify the Beta Casein (β-CN) protein from Iraqi Camel milk by urea, and ion exchange chromatography using a DEAE-Cellulose column, and gel filtration by using a Sephadex-G100 column, determining the molecular weight (M.wt) of protein isolate by polyacrylamide gel electrophoresis in the presence of the denaturant Sodium Dodecyl Sulphate (SDS). Enzymatic hydrolyzates were prepared using both pepsin and trypsin enzymes and their mixture (1:1), then the degree of hydrolysis (DH) was estimated after incubation for 8 h. and compared with bovine protein and standard proteins, the elution of β-CN using a DEAE-Cellulose column showed the appearance of two separate peaks, and their molecular weight was 24 KDa and 20 KDa Respectively. The Sephadex-G100 gel filtration technique also showed the appearance of a single peak whose molecular weight was 24 KDa compared to β-CN, which weighed 23 KDa. The results showed that the highest degree of decomposition was 52.32% by using a mixture of pepsin and trypsin. The results indicate that the protein β-CN separated from camel milk can be highly purified using ion exchange chromatography and gel filtration techniques, and peptide hydrolysates can be prepared from it.