THE PROPERTIES OF AN OLIGO-1,4 → 1,4-GLUCANTRANSFERASE FROM ANIMAL TISSUES

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Abstract
An oligo-l,4[forward arrow]1,4-glucantransferase has been discovered in rabbit muscle as a contaminant of amylo-l,6-glucosidase preparations. The transferase acts to move preferentially maltotriosyl and, to a lesser extent, maltosyl residues from donor oligosaccharides, including glycogen, to acceptor linear and branched oligosaccharides. The enzyme has no detectable action in moving single glucose residues. With a branched 7-unit dextrin of suitable structure, it has been possible to observe intramolecular transfer from the side branch to the main chain as well as intermolecular transfer of a maltosyl residue.