Enzyme β-glucosidase is a glycoside hydrolase that hydrolyzes β-glucosidase into water and alcohol. The research focuses on exploring the topology of the active site of sweetalmondβ-glucosidase (EC 3.2.1.21) by testing the kinetics of the enzyme with and without inhibitors using a spectrophotometer. By comparing the activity of the enzyme with the presence of various inhibitors, information about how structural differences of inhibitors interfere with the binding of the inhibitor to the active site of the enzyme can be obtained. To achieve better understanding of the active site topology, pH profile of the enzyme and pH profile of the binding will be constructed by monitoring reaction kinetics under different pH. Through the pH profile, the binding form of both the inhibitor and the enzyme at the active site can be inferred. The research provides inspiration of designing inhibitors of other related enzymes including some disease-relating glycoside hydrolases.