Abstract
Sclerotium rolfsii (isolate 14) was shown to produce at least two polygalacturonases. Both of these enzymes exhibited maximal activity on polygalacturonic acid substrates near pH 4·0 and had isoelectric points near pH 5·2. The two enzyme fractions were resolved by gel-filtration in Sephadex G-75 and sucrose density gradient centrifugation. The larger enzyme component had an estimated molecular weight of 46, 000 to 48, 000 and exhibited exopolygalacturonase activity. The smaller enzyme fraction had an estimated molecular weight of 28, 000 to 31, 000 and exhibited both endopolygalacturonase and exopolygalacturonase activities. Polygalacturonic acid substrates were readily converted to oligogalacturonides by endopolygalacturonase action and the oligomers were converted to galacturonic acid by exopolygalacturonase. The pectic enzyme complex produced by S. rolfsii would appear to function in tissue maceration, as well as provide a means of converting the pectic polymers of the host plant to a utilizable substrate for pathogen growth during pathogenesis.
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