Some species of the genus Aspergillus are excellent producers of industrial enzymes, such as amylases. The aim of this work was to study some properties of the amylases produced by Aspergillus phoenicis. The enzymatic assays were carried out with starch or maltose as substrates. The reducing sugars released were quantified using acid 3', 5' dinitrosalicilic acid. The best amylolytic levels were obtained when the fungus was grown at 30ºC in modified Khanna medium, initial pH 5.0, during four days, under standing conditions. Carbon sources, such as wheat bran, sugar cane bagasse, starch, maltose, mannose, penetrose maize, among others, were used as inducer. The highest extracellular enzyme levels were obtained in cultures supplemented with 1% starch or maltose. Rapidly assimilable sugars such as mannose or glucose repressed the amylolytic activity. The optimum pH for extracellular and intracellular amylases oscillated between 4.5 – 5.5 independently of the inducers and substrates used, but Mcllvaine buffer improved the enzymatic activity (49.9%), as compared with those in sodium acetate buffer. Considerably stability was observed between 30 - 65ºC. Approximately 68% of the extracellular amylolytic activity, obtained from starch-cultures, was stable in the range of pH 3.0 to 8.0, however the enzyme obtained from maltose-cultures was less stable (54%, in the range 3.0 to 6.5). The amylolytic activity was increased in the presence of 0.25 to 20.0mM Co⁺⁺, Cu⁺⁺, Na⁺, PO4⁺⁺, Ba⁺⁺, Ca⁺⁺, Mn⁺⁺ and NH₄F. The analysis on TLC of hydrolysis products on maltose or starch revealed glucose and maltooligosaccharides (triose, tetraose, pentaose), suggesting the activities of a-amylase and glucoamylase. Interestingly, it was observed when the assay was carried on maltose as substrate, also the formation of maltooligosaccharides larger than maltose (maltotriose and maltotetraose). This result suggested that the amylase was able of transglicosylation activity.