Cultures of Colletotrichum lindertmuthianum (Saccardo and Magnus) Scribner have been induced to secrete an endopolygalacturonase (polygalacturonide glyeanohydrolase EC3.2. 1.15). This enzyme has been brought to a high state of purity bv ion exchange, gel filtration, and agarose affinity chromatography. The enzyme has optimal activity at pH 5, has an apparent molecular weight as determined bv gel filtration of about 70,000, and prefers polygalacturonic acid to pectin as its substrate. The enzymne, while hydrolyzing only 1% of the glycosidic bonds, reduces the viscosity of a polygalacturonic solution by 50 %. Nevertheless, the initial as well as the final products of polygalacturonic acid hydrolysis are predominantly tri-and digalacturonic acid and, to a lesser extent, monogalacturonic acid. The purified enzyme catalyzes the removal of about 80% of the galacturonic acid residues of cell walls isolated from suspension-cultured sycamore cells (Acer pseudoplatanus) as well as from the walls isolated from 8-day-old Red Kidney bean (Phaseolus vulgaris) hypocotvls.Most polysaccharide-degrading enzymes are unable to attack effectively their substrates within isolated cell walls. Evidence has been presented which suggests that the "wall-modifying enzyme" purified from the culture filtrate of Aspergillus niger is a polygalacturonic acid-degrading enzyme (13). Treatment of walls with the wall-modifying enzyme permits other enzymes to degrade their substrates within the wall. Additional evidence that polygalacturonic acid-degrading enzymes are probably able, without assistance, to degrade cell walls comes from numerous efforts to demonstrate that these enzymes macerate plant tissues (2,4,5,7,12,18,20