Homodimeric glucose oxidase (GOX) from Aspergillus niger is a prominent enzyme used for a number of applications in biotechnology and clinical diagnostics. For robust and long-term functional applications of GOX, the stability of the protein is of utmost importance. In vitro, GOX is irreversibly inactivated over time by a mechanism that is poorly understood, and hence, it presents a significant drawback for the development of strategies to stabilize the enzyme. We show that the nonequilibrium stability of GOX is fully described by a one-step conformational unfolding kinetics. To explore the strategies for improving GOX nonequilibrium stability, the effect of salts of the Hofmeister series is examined using microcalorimetry. We obtain activation energies Ea and inactivation temperatures Tk (at which the irreversible step is 1.0 min-1) as a function of the salt types and concentrations. Based on the analysis by the extended Langmuir model, we find that at high salt concentrations (>1 M) the Hofmeister effect on inactivation temperature is determined by the universal ion-specific effect on the protein/water interface, which apparently does not depend significantly on a particular amino-acid sequence and 3D protein structure. Our findings identify protein/water interfacial tension as a critical physicochemical attribute of excipients that is crucial for increasing enzyme kinetic stability.