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Partial Purification and Properties of a Bacterial Isoamylase
Authors:Richards M. Evans  David J. Manners  J.Roger Stark
Affiliation:Department of Brewing and Biological Sciences, Heriot-Watt University, Edinburgh EH1 1HX Great Britain
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 barterial debranching-enzymes.
Keywords:To whom enquiries should be addressed.
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