An ${alpha}$-glucosidase enzyme produced by the fungus Thermoascus aurantiacus CBMAI 756 was purified by ultra filtration, ammonium sulphate precipitation, and chromatography using Q Sepharose, Sephacryl S-200, and Superose 12 columns. The apparent molecular mass of the enzyme was 83 kDa as determined in gel electrophoresis. Maximum activity was observed at pH 4.5 at $70^{circ}C$. Enzyme showed stability stable in the pH range of 3.0-9.0 and lost 40% of its initial activity at the temperatures of 40, 50, and $60^{circ}C$. In the presence of ions $Na^+$, $Ba^{2+}$, $Co^{2+}$, $Ni^{2+}$, $Mg^{2+}$, $Mn^{2+}$, $Al^{3+}$, $Zn^{2+}$, $Ca^{2+}$ this enzyme maintained 90-105% of its maximum activity and was inhibited by $Cr^{3+}$, $Ag^+$, and $Hg^{2+}$. The enzyme showed a transglycosylation property, by the release of oligosaccharides after 3 h of incubation with maltose, and specificity for short maltooligosaccharides and ${alpha}$-PNPG. The $K_m$ measured for the ${alpha}$-glucosidase was 0.07 ${mu}M$, with a $V_{max}$ of 318.0 ${mu}mol/min/mg$.