Protease stability in bovine milk under combined thermal-high hydrostatic pressure treatment

At atmospheric pressure, inactivation of protease from B. subtilis in raw milk and pasteurized milk (with and without homogenization) was studied in a temperature range of 50–80 °C. Thermal inactivation followed a first order kinetic model in the temperature range tested. Temperature dependence of the first order inactivation rate constants could be accurately described by the Arrhenius equation, allowing Ea values to be calculated. Different milk systems did not show differences in enzyme thermo stability.The combined thermal (40, 50 and 60 °C)-high hydrostatic pressure (300–450 and 600 MPa) effect on protease activity was studied. Protease was very resistant to high pressures. Pressure stability was higher in raw milk than in pasteurized milk; homogenization appeared to have a protective effect on the enzyme. The separate effects of pressure and temperature on enzyme inactivation were related to changes in L?-values and milk appearance.A very pronounced antagonistic effect between high temperature and pressure was observed, i.e. at temperatures where thermal inactivation at atmospheric pressure occurs rapidly, application of pressure up to 600 MPa exerted a protective effect.Industrial relevanceHigh hydrostatic pressure (HHP) is an emerging technology that has been successfully applied as a minimal process for a variety of foods. Although the potential for the use of HHP treatment as an alternative method to heat treatment of milk was proposed almost a century ago, the suitability of this innovative technology to extend the shelf-life of milk hinges not only on its ability to inactivate pathogenic vegetative microorganisms but also on its effectiveness to inactivate indigenous and endogenous enzymes. This work examines the combined effects of temperature, pressure and homogenization on the protease (exogenous enzyme from B. subtilis) activity in milk. Inactivation of protease could extend the shelf life of milk.