The study included the selection of the best methods to extract the enzyme among nine methods. The protein content was concentrated and precipitated by cold acetone among other five methods of concentration (partial purification). The purification stages were achieved by using ion exchange column chromatography (DEAE – Sephadex A 50 column). Followed by gel filtration chromatography using sephacryl S-300. The active parts were lyophlizated (free drying) to obtain Lipoxygenase with 43.18% yield and 8.16 folds of purification and specific activity of 1162.9 unit / mg. The purity of enzyme was confirmed by poly acryl amide gel electrophoresis under non denaturing conditions, with the appearance a single band .