Purification and properties of polygalacturonase associated with the infection process of Colletotrichum truncatum CP2 in chilli

Abstract—In this study, polygalacturonase enzyme produced by Colletotrichum truncatum CP2 was partially purified by aqueous two-phase system and the properties of this enzyme was characterized. The highest yield (57.4%) and purification fold (5.1) was obtained using 22% PEG 6,000/15% sodium citrate comprising crude load of 16% (w/w) at pH 7.0 with addition of 1.0% (w/w) sodium chloride. The partially purified PG remained active over a wide range of pH (2.5-6.0) and the optimum activity was obtained at pH 5.0. Incubation of the partially purified PG at 40 and 50 °C for 30 min caused the activity of PG to decrease up to 20% and 40%, respectively. However, no significant changes in the activity when the enzymes were incubated up to 4 h at 40 and 50 °C. The results from this study suggested that ATPS comprising of PEG and sodium citrate could be potentially used as an alternative method for purification of PG