Despite the many advantages of enzymes, their stability remains a significant limitation inbiocatalytic applications. A systematic evaluation of stability is a critical first step towardsdeveloping effective stabilization strategies. enzyme stability can be broadly categorized intothree types: thermodynamic stability, kinetic stability, and operational stability. each categoryoffers distinct insights into enzyme performance. thermodynamic stability reflects the enzyme’sintrinsic tendency to maintain its folded structure under equilibrium conditions. Kinetic stabilityrefers to the rate of irreversible deactivation over time, while operational stability describes theenzyme’s ability to retain catalytic activity under actual process conditions, accounting for allrelevant deactivation mechanisms. this review compiles the key parameters, experimentalmethodologies, and tools to assess each stability type. to this end, we highlight case studies fromthe past decade that demonstrate the absence of a universal approach to evaluating enzymestability and we present examples of Ai- and Ml-driven tools for different types of stabilitypredictions. the specific application should guide the choice of method and metric, whether theobjective is to understand fundamental deactivation mechanisms or to optimize enzymeperformance under industrial conditions.