Phytase (myo-inositol-hexakisphosphate phosphohydrolase, (EC 3.1.3.8) has been purified from a novel isolated Bacillus cereus EME 48, from environmental samples based on their ability. The enzymes were purified and characterized, using a three-step purification procedure with 12.3-fold. The optimum pH for phytase activity was in the range of 4.0 to 5.0 and the optimum temperature was 40 to 60°C for 10 min. The metal ions MgCl₂, CoCl₂, NiCl₂ and KCl₂ did not show any inhibitory effect on the phytase activity of Bacillus cereus EME 48. Strongly inhibited by FeCl₂, Na Florida, EDTA, DTT, AlCl₃ and ZnCl₂ but significantly stimulated by MgCl₂, BaCl_2, MnCl₂ and CuCl₂. The enzymes were active in the pH range of 5.0 to 6.5 with pH optima at 5.5. The enzyme from Bacillus cereus EME 48 retained about 80% activity up to 75°C. It was highly specific to sodium phytate as the substrate. Km for phytate was estimated to be 0.23 mmol and especially for penta- and tri-phosphate esters of myo-inositol. Due to their relatively high specific activity, substrate specificity, good pH profile and thermostability, the enzymes could be interesting candidate for agricultural and feed application.