Pressure-temperature inactivation kinetics of two enzymatic model systems based on Bacillus subtilis alpha-amylase (BSA), previously determined under isobaric-isothermal conditions, were studied under more realistic, i.e. dynamic, process conditions. The proposed kinetic model was found to accurately describe non-isobaric/non-isothermal inactivation of BSA in absence as well as in presence of 15% glycerol. Furthermore the effect of pressure cycling on the inactivation of BSA (in absence of glycerol) was investigated. Multiple application of pressure seemed to exert a more pronounced inactivation effect as compared to a single-cycle process of the same total time. This additional effect, however, could be completely attributed to the more extensive temperature variation occurring during pressure cycling.