The total turnover number (ttn) of an enzyme is a quantity which combines the deactivation behavior of the enzyme with its specific activity to express the moles of product made by one mole of enzyme over its lifetime. TEM-1 beta-lactamase was expressed in E. coli and its deactivation behavior was characterized with respect to salt concentration and temperature. The unfolding mechanism was determined by differential scanning calorimetry (DSC) experiments and verified with circular dichroism (CD) and was then fit to a Lumry-Eyring model. The operational stability for TEM-1 beta-lactamase was determined in a variety of ammonium salt solutions and the results were used to verify that ttn = kcat/(KkD) under Lumry-Eyring mechanisms. The correlation of short-term biochemical measurements to the accurate prediction of the productivity of an enzyme over its useful life has only recently been mentioned in the literature and has not yet been proven. Furthermore, the investigation of beta-lactamase activity and stability in salt solutions helps to elucidate the feasibility of enzymatic catalysis in low-water environments.