Previously, an extracellular ${alpha}$-amylase (BKA) had been purified from the culture of Bacillus sp. KR8104. Subsequently, the crystal structure of the active enzyme revealed a 422 amino acids polypeptide. In this study, the bka was cloned into E. coli, which encoded a polypeptide of 659 amino acids including two additional fragments: one 44 residues N-terminal fragment and another 193 residues C-terminal fragment. In order to investigate the role of the C-terminal fragment, two constructs with and without this region [$BKA{Delta}$(N44) and $BKA{Delta}$(N44C193)] were designed and expressed in E. coli BL21. The optimum pH, thermal stability, and the end-products of starch hydrolysis were found to be similar in both constructs. The $K_m$ and $V_{max}$ values for $BKA{Delta}$(N44) were lower than $BKA{Delta}$(N44C193), using either starch or ethylidene-blocked 4-nitrophenylmaltoheptaoside as a substrate.