Endopolygalacturonase, an extracellular pectic enzyme of Rhizoctonia fragariae.
A pectolytic enzyme from culture filtrates of Rhizoctonia fragariae was purified approx. 29-fold. The enzyme exhibited maximal depolymerizing activity on Na-polypectate rather than pectin at pH 5.0 and was inhibited at different extent by divalent cations Mg++, Mn++, Ca++. The analysis by paper chromatography of the products of enzyme hydrolysis suggested that the enzyme attacks the substrate by a random mechanism. The absorption spectrum of the chromogen formed by the hydrolysis products and thiobarbituric acid suggested that the enzyme is a hydrolytic enzyme. On the basis of these results the enzyme is classifiable as endo-polygalacturonase (poly alpha-1,4-galacturonide glycanohydrolase E.C. 3.2.1.15).
D002118:Calcium / Q000494:pharmacology; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D003904:Mitosporic Fungi / Q000201:enzymology*; D010368:Pectins / Q000378:metabolism; D011096:Polygalacturonase / Q000302:isolation & purification / Q000378:metabolism*; D012232:Rhizoctonia / Q000201:enzymology*
C014767:polypectate; D008345:Manganese; D010368:Pectins; D006026:Glycoside Hydrolases; D011096:Polygalacturonase; D008274:Magnesium; D002118:Calcium