The bulbs of Gladiolus klattianus are used in Burkina Faso in food processing. Activities of α-amylase and β-amylase were reported within those bulbs for the first time. The purification of the β-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 β-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°C and 55°C, respectively. The abundance of β-amylase in G. klattianus suggests its possible application for biotechnological purposes.

Extraction , partial purification , characterization of β-amylase