PURIFICATION, THERMOSTABILITY AND INHIBITORS OF α-GLUCOSIDASE FROM Penicllium chrysogenum
HAMED M. EL-SHORA *
Department of Botany, Faculty of Science, Mansoura University, Egypt.
SALLY M. METWALLY
Department of Botany, Faculty of Science, Tanta University, Egypt.
METWALLY A. METWALLY
Department of Botany, Faculty of Science, Tanta University, Egypt.
ESSAM A. FADDA
Department of Botany, Faculty of Science, Tanta University, Egypt.
NESMA A. ELZAWAWY
Department of Botany, Faculty of Science, Tanta University, Egypt.
*Author to whom correspondence should be addressed.
Abstract
α-glucosidase (α-D-glucoside glucohydrolase, EC:3.2.1.20) was isolated from Penicillium chrysogenum Thom ATCC 10106. The enzyme was purified by ammonium sulphate precipitation (85%), DEAE-cellulose and Sephadex G-200. The final specific activity was 360 units/mg protein. The yield was 18 % and the purification fold was 52.9. Trehalose and different sugars offered appreciable protection of α-glucosidase against denaturation at 60 °C. The aqueous extracts from various plants including Trigonella foenum-grecum, Sinapis arvensis, Cucurbita moschata, Apium crispum and Lepidium sativum inhibited α-glucosidase activity with different rates. IC50 values of the tested plants extracts were 88.5, 65.3, 72.6, 84.7 and 97.9 μg/ml, respectively.
Keywords: P. chrysogenum, α-glucosidase, purification, dextrose, raffinose, trehalose