title: Purification and characterisation of limit dextrinase from Pisum sativum L.
abstract: 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.
mesh_terms: D002846:Chromatography, Affinity; D006026:Glycoside Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D010944:Plants / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D006026:Glycoside Hydrolases; C100181:pullulanase