Abstract
An extracellular amylase from a bacterium, Bacillus megaterium strain No, 32, was purified over 2600-fold by precipitation with ammonium sulfate, column chromatography with SE-Sephadex and gel-filtration with Sephadex G–100. The enzyme was most active at pH values around 6.5, and was stable in pH range between 5 and 7.5. The enzyme activity was inhibited by p-chloromercuribenzoate and was restored completely by the addition of cystein. The isoelectric point of the enzyme was pH 9.1. Results of experiments in which maltooligo-saccharides terminated at the reducing end by radioactive glucose were used as substrates for the enzyme, showed that the enzyme removed two glucose unit (maltose) from the nonreducing end. From these results, the enzyme resembled the higher plant β-amylase in the action.
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