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An homogeneous fraction of alpha-amylase from Aspergillus tamarii was obtained by means of a very easy purification procedure. The enzyme is a glycoprotein containing 32% saccharide and MW of 37.5 kDa. Optimal of pH and temperature with starch as substrate were 4.5-6.5 and 50-55 degrees C. The enzyme was stable for several hours at temperature up to 65 degrees C. Starch, amylose, and amylopectin were the substrates preferentially hydrolysed and maltose and maltotriose were the main end products. The values of K(M) and V(max) for starch were 2 g/l and 880 micromoles reducing sugars/min.mg of protein, respectively. The purified enzyme was remarkably insensitive to end product inhibition, being only slightly inhibited by maltose and glucose up to 1.0 M.

A strain of Aspergillus tamarii, a filamentous fungus isolated from soil, was able to produce both α-amylase and glucoamylase activities in mineral media supplemented with 1% (w/v) starch or maltose as the carbon source. Static cultivation led to significantly higher yields than those obtained using shaking culture. The production of amylases was tolerant to a wide range of initial culture pH values (from 4 to 10) and temperature (from 25 to 42 o C). Two amylases, one α-amylase and one glucoamylase, were separated by ion exchange chromatography. Both partially purified enzymes had optimal activities at pH values between 4.5 and 6.0 and were stable under acid conditions (pH 4.0-7.0). The enzymes exhibited optimal activities at temperatures between 50 o and 60 o C and were stable for more than ten hours at 55 o C.

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The use of α methyl-D-glucoside (αMG), a synthetic analogue of maltose, as carbon source and inducer of amylase synthesis to several species of Aspergillus was studied in submerged and solid-state fermentations. Among a group of ten species, A. tamarii, A. fumigatus and A. flavus were able to produce biomass and high specific amylolytic activity in submerged cultures containing αMG as the only carbon source. In solid state fermentation, the enrichment of basal wheat bran or corn cob medium with αMG increased up to 3 times the production of amylases. In both submerged and solid state fermentations, aMG was more effective inducer of amylases than maltose and starch.