Abstract
Culture filtrates of Cladosporium resinae ATCC 20495 contain a mixture of enzymes able to convert starch and pullulan efficiently into d-glucose. Culture conditions for optimal production of the pullulan-degrading activity have been established. The amylolytic enzyme preparation was fractionated by ion-exchange and molecularsieve chromatography, and shown to contain α- d-glucosidase, alpha-amylase, and two glucoamylases. The glucoamylases have been purified to homogeneity and their substrate specificities investigated. One of the glucoamylases (termed P) readily hydrolyses the (1→6)-α- d linkages in pullulan, amylopectin, isomaltose, panose, and 6 3-α- d-glucosylmaltotriose. Each of the glycoamylases cleaves the (1→6)-α- d linkage in panose much more readily than that in isomaltose.
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