Alpha-amylase was purified from freeze-dried pear fruit by extraction at pH 7.40 with Tris, Acetate and Imidazole buffer followed by differential ammonium sulfate precipitation and desalting column. The specific activity of the enzyme was increased 5.68 fold during purification. The optimum pH was 5.64 in Acetate buffer. The difference in the time course of alpha-amylase was observed between freeze-dried and fresh samples.
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