Abstract

An endopolygalacturonase (poly,α-1,4-galacturonide glycanohydrolase, EC 3.2.1.15) was purified 60-fold from the culture fluids of Verticillium albo-atrum by chromatography on columns of carboxymethyl cellulose and hydroxylapatite, gel filtration, and preparative electrophoresis. Final preparations were homogeneous on the basis of disc-gel electrophoresis, ion-exchange and gel-filtration chromatography, and sedimentation in the ultracentrifuge. The purified endopolygalacturonase had a molecular weight of about 30,000, was rich in basic amino acids, and contained 1.2% carbohydrate. The enzyme catalyzed the random hydrolysis of sodium polypectate to short-chain oligouronides and exhibited macerating activity on cucumber pericarp tissues. The endopolygalacturonase had a Michaelis constant and maximum velocity on sodium polypectate of 0.15% and 2150 μmoles galacturonate equivalents liberated/ min/mg protein, respectively, at 35 ° and at the optimum pH of 6.5. The enzyme was inhibited by heavy metals but not by classical sulfhydryl or serine antagonists.

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