Partial Purification of ?-Glucosidase Enzyme from Soybean (Glycine max) and Determination of Inhibitory Effects two Quercetin Derivatives on Enzyme Activity

Abstract

Glucosidases are enzymes that catalyze the hydrolysis of the glycosidic linkage of glycosides, leading to the formation of a sugar hemiacetal or hemiketal and the corresponding free aglycon. Activity of glucosidases is crucial for several biochemical processes. Thus, discovery of new glucosidase inhibitors is crucially important owing to potential therapeutic applications of this enzyme in the treatment of diabetes, human immunodeficiency virus infection, metastatic cancer, lysosomal storage disease etc. In the current study, inhibitory potential of ‘quercetin’ and its isomeric form ’morin hydrate’ on the activity of ?-glucosidase enzyme, present in the extract of soybean (Glycine max L.) seeds, were investigated. The compounds exhibited moderate inhibitory action in low milimolar concentrations. I50 values were calculated as 0.188 and 0.138 mM for quercetin and morin hydrate, respectively. The results have confirmed that these compounds can be used as leads for designations of novel glucosidase inhibitors which would be used in medicinal biotechnology and food science and technology. © 2016, Eesti Pollumajandusulikool. All rights reserved.