Phosphatases are enzymes present in eukaryotic and prokaryotic organisms and hydrolyze esters and anhydrides of phosphoric acid. These enzymes are classified in: i) alkaline phosphatases, ii) high molecular mass acid phosphatases, iii) low molecular mass acid phosphatases, iv) purple acid phosphatases and v) protein phosphatases. Phytase is an acid phosphatase which converts phytate into inositol and phosphoric acid. Addition of this enzyme to animal feed results in better digestibility, reduced feed cost and environmental protection. In this work, Rhizopus microsporus var. rhizopodiformis, a filamentous fungus isolated from Brazilian soil in our laboratory, produced and secreted the highest levels of phytase, and also amylases, xylanases, and invertases. Optimal conditions for solid state and submerged fermentation for phytase production were tested. Phytase activity was determined using 1mM phytic acid as substrate in succinic acid buffer 100 mM, pH 5.0. The enzymatic activity was expressed by Pi/min/mL, and growth by mg of total protein. When we compared liquid (SbmF) and solid state fermentation (SSF), the highest levels of extracellular phytases were produced after 24-48 hours of growth, using wheat bran and soy bean mixtures in water (1:1:2 p/v), with 70% relative humidity, at 45^oC. The results suggested that the optimal conditions of SSF and SbmF were pH 5.0 and optimum temperature was around 80^oC during 1 h. These enzymes were activated by Mn⁺⁺ and Mg⁺⁺ ions. The extracellular phytase was partially purified using DEAE-Cellulose chromatography, followed by a Concanavalin A-sepharose affinity chromatography, resulting in 62% recuperation. These results suggested that phytase could be useful for biotechnological and industrial applications, had its easy production, purification and recuperation (using half of culture of low cost). E also for its great resistance to pH and temperature.