An α-amylase capable of producing exceptionally high levels of maltose (74%) from starch has been identified from a strain of Penicillium expansum. The enzyme is produced extracellularly and was purified to homogeneity by starch adsorption and Sephadex gel filtration chromatography. P. expansum α-amylase has a pH optimum of 4.5 and is stable in the pH range of 3.6–6.0. Other properties include a temperature optimum of 60° C, a molecular weight of 69 000 and an isoelectric point of 3.9. The most outstanding feature of the P. expansum enzyme is its ability to yield 14% more maltose and 17.1% less maltotriose than a currently used commercial enzyme. This may be partly explained by the greater affinity of this new enzyme for maltotriose (K m=0.76 mM) relative to the commerical enzyme, Fungamyl (K m=2.9 mM). The enzyme reported here is unique among fungal α-amylases in being able to produce such high levels of maltose and its physicochemical properties suggest that it has potential for commercial development.