Invertase (b-D-fructofuranoside fructohydrolase, EC.3.2.1.26) catalyzes the hydrolysis of the  b- fructofuranoside residues non - reducing terminal in  b- fructofuranosides.  When the sucrose is hydrolyzed by invertase an equimolar mixture of glucose and fructose is generated. This mixture of monosaccharides is called invert sugar. This enzyme is mainly used in the food industry where fructose is preferred over sucrose because it is sweeter and does not crystallize as easily. This work purposes the production, purification and characterization of extracellular invertase from Aspergillus terreus. For enzyme production, spores from the microorganism were transferred to liquid medium with 1% cane pulp as carbon source. After incubation under constant shaking for 72 h, at 28⁰C, culture supernatants were collected by filtration through filter paper and kept frozen until use. Invertase activity was assayed with the dinitrosalicylic acid method to determine the sugar reducing. This enzyme has been purified by successive chromatographies on CM-Sepharose and Phenyl-Sepharose. This enzyme showed apparent molecular mass of 57.2 kDa on SDS-PAGE. The optimum pH and temperature were found to be 4.0 and 60 - 65⁰C, respectively. MnCl₂ increased invertase activity while EDTA, KCl, NaCl and CaCl₂ decreased moderately. SDS showed strong inhibitory effects on enzyme activity. The K_m and V_max values were determinate to be 11.6mM and 9.24mM.min^-1, respectively, for hydrolysis of sucrose. This enzyme lost 66% of its initial activity after 60min at 60⁰C. The purification and the characterization of this enzyme are necessary steps to improve the understanding of its mode of action and the nature of the hydrolytic activity. In addition, the carbon source utilized in this work is inexpensive and induces significantly the invertase activity showing that this enzyme may be candidate for industrial application.