In almost all studies on the role of solvent in the binding of the ligand to a receptor, the focus had always been on the thermodynamic stability of the complex formed. Hardly any attempt has been made to quantify the number of solvent molecules released in the course of ligand (e.g., substrate, pathogen, drug, etc.) and receptor (enzymes, cell membrane, antibodies, etc.) binding interaction in recent times. The goal of the study was to determine how to calculate the amount of solvent molecules displaced from reactant species using nonequilibrium binding energy (NEBE), since desolvation is a prerequisite for the development of a stable complex. Deriving relevant energy equations, such as the one for calculating the number of molecules of desolvation, was one of the objectives. The methods are solely theoretical, experimental (Bernfeld), and computational. According to the study's findings, the water of hydration ranged from 338 to 400 water molecules, which corresponded to substrate (gelatinized potato starch) concentrations between 5 and 10 g/L. The translational entropy gains, the corresponding thermodynamic component, ranged from 91.4 to 133.1 J/mol K. The comparable values were 526.316 and 216.129 J/mol K, respectively, at the highest hydrolysis velocity. In conclusion, the equation of NEBE can be explored for the computation of water of desolvation in support of the observation that desolvation is part of the driving forces that propel ligand-receptor binding. Further thermodynamic characterization of ligand-receptor binding on the basis of desolvation needs to be done at different temperatures in the future.