Purification and Properties of Polysaccharide Depolymerase Associated with Phage-infected Pseudomonas aerugiuosa*

A polysaccharide depolymerase was puritied 1,688-fold from crude lysates produced by the propagation of a specitic bacteriophage in Pseudomonas aeruginosa. Conventional methods of protein fractionation were employed, namely, salting out with ammonium sulfate, Sephadex gel filtration, and high speed centrifugation. The purified depolymerase behaves as a single entity when tested by electrophoresis in acrylamide gel. On the basis of gel filtration data the molecular weight was estimated to be 180,000. Maximal enzymatic activity was found at pH 7.5.