Extraction, partial purification and characterization of beta-amylase fromthe bulbs of G-klattianus

The bulbs of Gladiolus klattianus are used in Burkina Faso in food processi ng. Activities of alpha-amylase and beta-amylase were reported within those bulbs for the first time. The purification of the beta-amylase involved bu ffer extraction, ammonium sulfate precipitation and gel filtration chromato graphy. The enzyme was purified 47 fold with 75% yield, giving a final spec ific activity of 2360 U/mg. The beta-amylase from G. klattianus was shown t o be a heterodimer protein of 60 and 12 kDa subunits. Optimum pH and temper ature for the activity were 5.5 degrees C and 55 degrees C, respectively. T he abundance of beta-amylase in G. klattianus suggests its possible applica tion for biotechnological purposes. (C) 2000 Elsevier Science Ltd. All righ ts reserved.