Purification and characterization of α-glucosidase from Penicillium chrysogenum.

α-glucosidase (EC: 3.2.1.20) was isolated and purified fromPenicillium chrysogenum Thom ATCC 10106 by ammonium sulphate precipitation (75%), DEAE-cellulose and Sephadex G-200. The specific activity was 140 units (U) mg-1 protein. The enzyme expressed a single band using SDS-PAGE and the molecular weight of the enzyme was nearly 43KDa. The optimal pH and temperature were 8 and 40 ºC. The activation energy was 17.94 k J mol-1. The optimal incubation time was 40 min. Glutamine, glutamic acid, cysteine, alanine, phenylalanine, glycine, methionine, asparagine enhanced the enzyme activity and cysteine was the best enhancer. However, cystine and arginine inhibitedα-glucosidase activity. The Vmax values were 48 and 38.1 U mg-1 protein with and without of cysteine, respectively. However, Km values were 0.21 and 0.25 mM in absence and presence of cysteine, respectively.

Source: International Journal of Phytomedicine - January 7, 2019 Category: Science Authors: Hamed M El-Shora Source Type: research