ISSN: 0973-7510
E-ISSN: 2581-690X
Polygalacturonases (PG) are enzymes that degrade pectic substances and are widely used in juice and fruit beverages to improve the quality of the process. The PG isolated from Aspergillus niger RBF96 was partially purified and characterized. It was purified upto 7 folds with an yield of 14.04 % and specific activity of 83.06 U/ìg, by gel filtration using sephadex G100. The SDS-PAGE revealed the presence of multiple bands in the crude enzyme, while a single band in the purified fractions. The molecular weight of the PG protein was 37 kDa. The Km and Vmax of the enzyme were 0.155 U/mL and 38.57 U/mL respectively. The PG was found to be relatively more stable to temperature and pH changes. The optimum temperature and optimum pH of the enzyme were 50° C and 4.5 respectively.
Aspergillus niger RBF96, Polygalacturonase, SDS-PAGE, Purification, Km and Vmax
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