High hydrostatic pressure stabilized galactose oxidase (GaOx) at 70.0-80.0°C against thermal inactivation. The pseudo-first-order rate constant of inactivation k decreased by a factor of 8 at 80°C and by a factor of 44 at 72.5°C. The most pronounced effect of pressure was at the lowest studied temperature of 70.0°C with an activation volume of inactivation ΔV of 78.8 cm mol. The optimal pressure against thermal inactivation was between 200 and 300 MPa. Unlike other enzymes, as temperature increased the ΔV of inactivation decreased, and as pressure increased the activation energy of inactivation E increased. Combining the results for GaOx with earlier research on the pressure-induced stabilization of other enzymes suggests that ΔV of inactivation correlates with the total molar volume of cavities larger than ~100 Å in enzyme monomers for enzymes near the optimal pH and whose thermal unfolding is not accompanied by oligomer dissociation.
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