The effect of hyperbaric storage (HS) on polyphenoloxidase activity (PPO) was studied in model solutions and apple juice. Model solutions containing increasing amounts of mushroom (Agaricus bisporus) PPO (up to 26 U) were stored at room temperature at pressure up to 200 MPa. During HS, samples were assessed for residual PPO activity. The enzyme was completely inactivated according to a first-order kinetic model that was used to calculate PPO decimal reduction time (Dp) and pressure sensitivity (zp = 140.8 MPa) in diluted model solutions (2 U PPO). The increase in enzyme concentration (6–26 U) nullified the effect of HS, probably due to protein structure stabilization by self-crowding. The application of HS at 100 and 200 MPa to apple juice promoted a decrease in total bacteria, lactic acid bacteria, yeasts, and molds. These changes occurred in concomitance with the inactivation of PPO (zp = 227.3 MPa). At 200 MPa, PPO inactivation followed a biphasic first-order kinetic, suggesting the presence of PPO isozymes with different pressure sensitivity. The inactivation of PPO was observed to occur more rapidly with increasing storage pressure and led to the maintenance of the original bright juice color. This study proves the capability of HS to control enzyme-related quality decay in fruit juices and, potentially, in many other food matrices suffering enzymatic alteration.
