The bulbs of Gladiolus klattianus are used in Burkina Faso in food processing. Activities of alpha-amylase and beta-amylase were reported within those bulbs for the first time. The purification of the beta-amylase involved buffer extraction, ammonium sulfate precipitation and gel filtration chromatography. The enzyme was purified 47 fold with 75% yield, giving a final specific activity of 2360 U/mg. The beta-amylase from G. klattianus was shown to be a heterodimer protein of 60 and 12 kDa subunits. Optimum pH and temperature for the activity were 5.5 degrees C and 55 degrees C, respectively. The abundance of beta-amylase in G. klattianus suggests its possible application for biotechnological purposes.