Purification and characterization of beta-amylase from Curculigo pilosa

Curculigo pilosa is traditionally used in the manufacture of sorghum beer i n West Africa. beta-Amylase was purified 100-fold with 38% yield from a cru de extract, giving final specific activities of 4850 U/mg and 5650 U/mg usi ng soluble starch and p-nitrophenyl maltopentaoside, respectively, as subst rates. The molecular mass of the monomeric enzyme was 64 kDa and its pI 4.2 . Both activity and thermostability are higher than reported for other plan t beta-amylases. The catalytic efficiency was lower for amylose than for st arches and amylopectin. In contrast to other plant amylases, the beta-amyla se from C. pilosa is able to degrade raw starches from wheat, corn, potato and rice. In this respect, it resembles beta-amylases from microbial origin . This property, and its high activity and stability, explain its tradition al use in the manufacture of infant food and sorghum beer in Burkina Faso a nd could make it applicable for other biotechnological purposes.