An immobilized acarbose column selectively adsorbed most of glucoamylase components from a commercial glucoamylase preparation. The adsorbed enzyme was specifically eluted with maltose into a glucoamylase fraction free from α-amylase and α-glucosidase. The eluate was further fractionated into six subfractions by gel chromatography and subsequent anion-exchange chromatography. Each of the enzyme subfractions liberated β-glucose as the sole product from soluble starch and maltooligosaccharides. Thus, all the enzymes are glucoamylases, though the enzymes were apparently discriminated from one another on the basis of molecular weight and/or electrophoretic behavior. Furthermore, the enzyme subfractions were classified roughly into three groups on the structural resemblance implied by immunological cross-reactivity among them.

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