Abstract:Purification of pectin lyase (PL), polygalacturonase (PG), and pectin esterase (PE) from the fermentation culture supernatant of Aspergillus niger YY-22 was investigated. All the three enzymes PL, PG and PE were precipitated by ammonium sulfate precipitation (0~65%). PE was further purified by hydrophobic interaction chromatography using Phenyl-Sepharose FF, while PG and PL were purified by Q-Sepharose HP ion exchange chromatography. The highest recovery of PL was obtained with 65% ammonium sulfate saturation precipitation. After three steps of separation, PL was purified 13.30 folds with a recovery of 33.05% and a specific activity of 79.37 U/mg.
