*3.1. Mealworm Protein Degradation during Enzymatic Hydrolysis*

Figure 1 presents the degradation of mealworm soluble proteins that were recovered at the beginning, during, and at the end of the enzymatic hydrolysis for control and pressurized conditions (pretreated and simultaneous). Regarding protein profiles during Alcalase® hydrolysis (Figure 1A), a band, whose intensity increased as a function of hydrolysis duration, was detected in wells for control, pretreated, and simultaneous conditions. Whatever the condition, three distinctive bands that corresponded to proteins with molecular weights (MW) close to 10, 20, and 50 kDa were observed. The protein degradation profiles for hydrolysates after 10 and 120 min of Alcalase® hydrolysis for control, pretreated, and simultaneous conditions were similar. More specifically, the same bands, as listed for control at t = 0 min (10, 20, and 50 kDa), were detected, but heavy bands close to 10 kDa were observed after 10 and 120 min of hydrolysis, resulting in mostly peptide fragments. A band with MW between 150 and 250 kDa observed after 10 min of hydrolysis, and whose intensity was increasing at 120 min of hydrolysis, was detected for control and pretreatment conditions but was absent at t = 0 min. When compared to Alcalase®, non-distinctive bands were observed for the pepsin control at t = 0 min except for the band at 20 kDa (Figure 1B). However, while peptides with molecular weights close to 10 kDa MW were detected for all conditions, the bands were more intense for simultaneous conditions after 10 and 240 min of hydrolysis as compared to the pretreatment condition. Under the control conditions, peptides with molecular weight close to 10 kDa MW were more concentrated after 10 min of hydrolysis as compared to 240 min.

**Figure 1.** Protein degradation of mealworm proteins during enzymatic hydrolysis by Alcalase® (**A**) and pepsin (**B**) for control (0.1 MPa) and pressurization conditions (pretreated and simultaneous at 380 MPa for 1 min).
