Abstract
An extracellular beta amylase was induced in cultures of Bacillus subtilis isolated from the kolanut weevil, Balanogastris kolae grown in liquid medium that contained cocoyam starch as sole carbon source. The enzyme was partially purified by acid treatment with ice cold 1.0N HCl and gel filtration with Sephadex G 150. The enzyme had its optimal activity at pH 6.0 and exhibited maximal activity at temperature of 50 o C. The activity of the enzyme was enhanced by Na + , while ethylene diaminetetraacetic acid (EDTA), Hg 2+ and Ca 2+ acted as mild inhibitors and Fe 2+ was a strong inhibitor of its activity. The beta amylase had a molecular weight of 27.6 kDa and an apparent Michaelis constant Km of 4.6 mg/ml and maximum velocity (Vmax) of 47.62 U/mg proteins.
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