Purification and characterisation of limit dextrinase from Pisum sativum L.

A limit dextrinase has been purified 2,700-fold from ungerminated pass by affinity chromatography. The enzyme hydrolyses (1 yield 6)-alpha-d-glucosidic linkages in alpha-limit dextrins containing at least one alpha-1(1 in alpha 4)-linked d-glucose residue on either side of the susceptible linkage. The limit dextrinase also hydrolyses the polysaccharides amylopectin, amylopectin beta-limit dextrin, glycogen beta-limit dextrin, and pullulan, but has no activity towards glycogen.