The pectic enzymes of Aspergillus niger. A second exopolygalacturonase.
1. A second exopolygalacturonase was separated from a mycelial extract of Aspergillus niger with a 265-fold purification and a recovery of 1%. 2. Unlike the first exopolygalacturonase this enzyme showed no requirement for metal activators, nor was it inhibited by chelating agents. 3. The two exopolygalacturonases were also distinguished by their pH optima and stability. 4. The enzyme progressively removed the terminal galacturonic residues from alpha-(1-->4)-linked galacturonide chains, converting digalacturonic acid, trigalacturonic acid and tetragalacturonic acid into galacturonic acid. Galacturonic acid was also released from pectic acid but complete digestion was not achieved.
D001230:Aspergillus / Q000201:enzymology*; D055598:Chemical Phenomena; D002621:Chemistry; D002845:Chromatography; D004492:Edetic Acid; D006026:Glycoside Hydrolases; D006863:Hydrogen-Ion Concentration; D008628:Mercury
D004492:Edetic Acid; D006026:Glycoside Hydrolases; D008628:Mercury