Rapid and simple purification of a novel extracellular β-amylase from Bacillus sp.

Abstract

Bacillus sp. KYJ 963,a local isolate, produced an extracellular amylase with Mr = 59 kDa. The amylase was easily purified by adsorption on soluble starch. The analyses of TLC and N-terminal amino acid sequence from the purified protein revealed that the enzyme was a novel β-amylase which could not hydrolyze maltose or α-cyclodextrin and its N-terminal amino acid sequence was A-V-N-G-Q-S-F-N-S-N-Y-K-T-Y-K-.