Acid phosphatase and invertase activities of Aspergillus nigerindustries (Metwally 1998). They produce extracellular enzymes to degrade insoluble substrate into smaller fragments and fi nally into soluble units that are then absorbed by hyphae (Chaube and Singh 2000). The property of microorganisms to produce enzymes is vastly exploited for industrial purposes.Aspergillus niger, a cosmopolitan, widely distributed fungus, is an important industrial source for citric acid and enzymes, such as amylase, and enjoys a GRAS ("generally regarded as safe") status (Martens-Uzunova et al. 2006). The starch-degrading enzyme amyloglucosidase, which is an extracellular inducible enzyme from fi lamentous fungi (Aspergilli), is the second most widely produced enzyme worldwide after that of Bacillus protease (Metwally 1998). Thus, study of the stability of enzymes is an important aspect to consider in biotechnological processes as this can provide information on the structure of the enzymes and facilitate an economical design of continuous processes in bioreactors (Jurado et al. 2004).Acid phosphatases (EC 3.1.3.2, orthophosphoric monoester phosphohydrolase) are a group of enzymes that catalyze the hydrolysis of external phosphate esters (Joh et al. 1996). They play an important role in the mineralization of organic carbon, organic phosphate, and low levels of free inorganic ions (Pi) (Straker and Mitchell 1986). Orthophosphate anion ("inorganic phosphate" Pi) plays a vital functional role in energy transfer and metabolic regulation and is also an important structural constituent of many bio molecules (Ehsanpour and Amini 2003). Extracellular acid phosphatases hydrolyze external phosphate esters, and intracellular acid phosphatases are involved in the routine utilization of Pi. Acid phosphatases of Saccharomyces cerevisiae have been extensively studied (Schweingruber et al. 1992). They have also been studied in Aspergillus nidulans (Arst et al. 1980), ectomycorrhizal fungi (Straker and Mitchell 1986), lysing and growing fungal structure, and molds (Haas et al. 1992). Acid phosphatase is reported to be located in the cell wall and septa of hyphae as determined by cytochemical studies by transmission electron microscopy (TEM) (Gutiérrez-Miceli et al. 2005).