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Keywords

Enzyme Kinetics, pH, Temperature, Polarimetry

Abstract

The purpose of this research is to study the factors that affect the enzymatic activity of invertase, extracted from baker’s yeast, on hydrolysis of sucrose in aqueous medium. Invertase, a glycoprotein, is an enzyme in the glycoside hydrolase family. It catalyzes the hydrolysis of sucrose producing equimolar mixture of a-D-glucose and b-D-fructose. Invertase shows high affinity for the substrate, and is capable of both cleaving the glycosidic linkage in sucrose and transferring ab-D-O-fructofuranoside residue to an acceptor substrate. (Toledo et al. 2019). A detailed mechanism of the action of invertase was postulated by Shall et al. (Shall et al. 1971). In this study, the effect of pH on enzymatic activity of invertase at constant temperature of 16.5 ± 0.5 oC was examined. In addition, the optimum temperature for invertase activity was determined. We found that a combination of pH ~4.7 and ~50 oC temperature was the optimum condition for invertase activity. Lastly, we have studied the effect of decreasing sucrose concentration under optimum conditions of pH and temperature.  The results of our study show asymptotic relationship of product-to-initial substrate concentration ratio versus time at optimal conditions. Polarimetry was extensively applied to perform these experiments.

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