title: Partial purification and properties of a bacterial isoamylase.
abstract: Isoamylase has been prepared by affinity chromatography of a commercial enzyme-preparation from a strain of Cytophaga (also known as a Flavobacterium or Polyangium). The enzyme was not very stable, but the stability could be improved by calcium ions. The enzyme had a very low but significant activity on pullulan and on alpha-dextrins having maltosyl side-chains. This observation, which is contrary to previous reports, has been related to the specificity of isoamylase and other bacterial debranching-enzymes.
mesh_terms: D000818:Animals; D002413:Cations, Divalent; D002846:Chromatography, Affinity; D003589:Cytophaga / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000378:metabolism*; D007517:Isoamylase / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008112:Liver Glycogen; D051381:Rats; D013379:Substrate Specificity
chemical_list: D002413:Cations, Divalent; D008112:Liver Glycogen; D006026:Glycoside Hydrolases; D007517:Isoamylase