Abstract
α-Amylase was purified and prepared in good yield from sorghum malt by procedures based on ultracentrifugation, salt fractionation, and adsorption on starch granules. The purified enzyme had a specific activity comparable to crystalline barley α-amylase. The enzyme had a pH optimum of 4.6 and was inactivated at pH's below 3.5. It exhibited a minimum solubility in ammonium sulfate solutions at pH 5.8 and required Ca ++ ions for stabilization.
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