The current study addresses the thermodynamic and kinetic characterization of the protease from Bacillus sp. P45 in a submerged culture. The enzyme was mixed in ionic liquid and acetone to compare its effect to a solubilized enzyme in 100 mmol/L Tris-HCl buffer, pH 7.5 (trial control). Protease P45 was kinetically characterized from its half-life and thermodynamically by the parameters obtained in a first-order inactivation kinetic model at a temperature range of 40 to 55 ºC. As a resulted, protease was more stable than the control, which was verified by the increase half-life along with the temperature rise. Through this characterization, new potential applications may be further explored for this enzyme.