Abstract
An improved purification procedure preserved high levels of α-amylase activity, and revealed and separated other starch-degrading activities from endosperm of germinating maize ( Zea mays L.). Amylases were partially purified by hydroxylapatite chromatography, and separated by chromatofocusing and affinity chromatography on cycloheptaamylose. Chromatofocusing resolved eight protein peaks with amylase activity. The binding of amylase activity to cycloheptaamylose ranged from 0 to 90% for these peaks. Isoelectric focusing and analysis of substrate specificities showed two major groups of α-amylase with five subgroups, two pullulanase enzymes, and one β-amylase. This procedure is a significant improvement over the use of protein precipitation and affinity chromatography which results in large, and possibly selective, losses of amylase activity.
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