Studies on Carbohydrate Metabolising Enzymes. Part XXVI. The Limit Dextrinase from Germinated Barley

Limit dextrinase was isolated from an extract of freshly germinated barley by precipitation with ammonium sulphate followed by continuous electrophoresis. Enzyme activity was assayed using pullulan as substrate. The purified enzyme can release α‐(1→6)‐linked maltosyl and maltotriosyl units from both oligosaccharide and polysaccharide substrates (e.g. amylopectin β‐limit dextrin). It had no action on substrates containing α(1→6)‐linked glucosyl residues, or on amylopectin, glycogen, or glycogen β‐limit dextrin. The enzyme also synthesised branched oligosaccharides from maltose and various maltosaccharides; glucose was not a substrate for these condensation reactions.