An immobilized acarbose column selectively adsorbed most of glucoamylase components from a commercial glucoamylase preparation. The adsorbed enzymewas specifically eluted with maltose into a glucoamylase fraction free from a-amylase and a-glucosidase. The eluate was further fractionated into six sub fractions by gel chromatography and subsequent anion-exchange chromatography. Each of the enzyme sub fractions liberated /^-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 enzymesub fractions were classified roughly into three groups on the structural resemblance implied by immunological cross-reactivity among them.
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 a-amylase and a-glucosidase. The eluate was further fractionated into six subfractions by gel chromatography and subsequent anion-exchange chromatography.Each of the enzyme subfractions liberated f3-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.
A commercial preparation of glucoamylase from Aspergillus niger consisted of at least six species (A-II~IV and B-I-III), five forms of which were fully characterized. They were apparently different in molecular weight, sedimentation constant feo,w)» isoelectric point (pi), chemical composition, kinetic parameters (k0, molecular activity; kint, intrinsic rate constant), and other enzymatic properties. Whencompared with enzymological characteristics as well as serological ones, B-I was found to be a peculiar enzyme among them. Furthermore, A-II was significantly discriminated from the other enzymesin respect of molecular weight and composition of amino acid, suggesting that A-II might be the product of transcription of a different DNAsite.
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