A gene encoding human intestinal maltase (HMA) was successfully expressed in Pichia pastoris under the control of the methanol-induced alcohol oxidase (AOX1) promoter. The secreted recombinant HMA fused with a $His_6$-tag was produced (150 U/L) and was easily purified from culture supernatants in a 3-step diafiltration, ultrafiltration, and affinity column chromatography protocol. The specific activity of the purified HMA was 16.8 U/mg. Endoglycosidase H digestion of the protein showed that the recombinant HMA was N-glycosylated. The purified HMA was maximally active at pH 6.5 and stable (${geq}$90%) up to $65^{circ}C$. The kinetic parameters $K_m$ and $V_{max}$ were $3.3{pm}0.25$ mM maltose and $61.9{pm}2$ U/mg, respectively.