Purification and characterization of polygalacturonase from Aspergillus fumigatus MTCC 2584 and elucidating its application in retting of Crotalaria juncea fiber

Polygalacturonases represents an important member of pectinases group of enzymes with diverse industrial applications and is widely distributed among fungi, bacteria, yeasts, plants and some plant parasitic nematodes. An endo-polygalacturonase from a new fungal source Aspergillus fumigatus MTCC 2584 was produced under solid-state fermentation conditions and was purified simply by acetone precipitation and gel-filtration chromatography technique. The approximate molecular weight of the purified PG was found to be 43.0 kDa as revealed by SDS-PAGE. The pH optimum of the purified enzyme was found to be 10.0 and was stable in the pH range of 7-10. The optimum temperature of purified PG was found to be 30 °C. The Km and Kcat of the purified enzyme were 2.4 mg/ml and 44 s-1, respectively, and the metal ions Cu2+ and K+ were found to enhance the enzyme activity while Ag+, Ca2+ and Hg2+ were inhibitory in nature. Based on its alkaline nature, the potential of purified PG in retting of natural fiber Crotalaria juncea was elucidated in the absence of EDTA. This is probably the first report of alkaline PG from Aspergillus fumigatus.