PURIFICATION AND CHARACTERIZATION OF AN ENDOPOLYGALACTURONASE FROM PHYSALOSPORA-PIRICOLA

An endopolygalacturonase from Physalospora piricola was purified to apparent homogeneity by column chromatographies. The molecular weight was estimated to be 38,000 by SDS-PAGE, and the isoelectric point was around pH 7.6. The amino acid composition was similar to those of endo PGs from other fungi. The enzyme was most active at pH 4.9 and stable from pH 5 to 7. Oligogalacturonic acids with a degree of polymerization higher than three were readily hydrolyzed by the enzyme, but trigalacturonic acid only slightly.