Purification and Properties of Two Polygalacturonases from Trichoderma koningii

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Abstract
SUMMARY: Two inducible polygalacturonases (PG-1 and PG-2) from culture filtrates of Trichoderma koningii were purified to homogeneity by CM-cellulose chromatography and isoelectric focusing in a narrow pH range (pH 6 to 8). They were both hydrolytic enzymes classifiable as endopolygalacturonases [poly(1,4-α-D-galacturonide) glycanohydrolase; EC 3.2.1.15]. PG-1 and PG-2, focusing at pH 6-41 and 6-57 respectively, each consisted of a single polypeptide chain having an apparent molecular weight of 32000 as determined by gel filtration on Sephadex G-100; they were both glycoproteins and had carbohydrate contents of 0-033 and 0-062 mg sugar (mg protein)-1 respectively. When the isoenzymes were incubated with different plant tissues, they were not absorbed by any of them.