The Partial Purification and Properties of Endopolygalacturonase and -L-Arabinofuranosidase secreted by Sclerotinia fructigena

Abstract

SUMMARY An endopolygalacturonase (PG) and an α-l-arabinofuranosidase (AF) in culture filtrates of the fungus Sclerotinia fructigena were partially purified by ion-exchange chromatography on CM-Sephadex and Ecteola-cellulose columns, and characterized. Molecular weight estimations by gel-filtration and electrophoresis on cellulose acetate strips indicated that both enzymes existed in multiple forms. The PG showed unusual stability to extreme pH values, to classical inhibitors, and to proteolytic enzymes; in the crude filtrate a bimodal temperature/stability curve was obtained.