The Impact of Low-Temperature Inactivation of Protease AprX from Pseudomonas on Its Proteolytic Capacity and Specificity: A Peptidomic Study

The destabilization of UHT milk during its shelf life can be promoted by the residual proteolytic activity attributed to protease AprX from Pseudomonas. To better understand hydrolysis patterns AprX, and evaluate feasibility using low-temperature inactivation (LTI) for release peptides through on proteins was examined an LC-MS/MS-based peptidomic analysis. Milk samples were either directly incubated hydrolyzed or preheated under LTI conditions (60 °C 15 min) then incubated. Peptides parent (the which originated) identified quantified. mapped cleavage frequency amino acids in P1/P1′ positions analyzed, after influence potential bitterness formed determined. Our results showed that a total 2488 48 proteins, with most abundant originating κ-casein β-casein. may also non-specifically hydrolyze other milk. Except decreasing skim milk, did not significantly reduce AprX-induced proteins. Therefore, feasible production.