*3.2. Profiles and Characterization of Proteins in Meals and Protein Extracts*

Figure 2 presents the protein profiles of TMI, TMD, HDSP, and NDSP fractions obtained after 2D SDS-PAGE analysis. The 11 main spots (#1 to #11) visualized in 2D gels were excised for protein characterization by proteomic tools (Table 2). As observed for 2D gels (Figure 2), proteomic results confirmed that *T. molior* fractions (TMI, TMD, HDSP, and NDSP) have very similar protein profiles consisting of muscular (e.g., actin-87E-like protein) and hemolymph proteins (e.g., hexamerin 2, 12 kDa hemolymph protein b) as well as proteins associated with various metabolic activities (e.g., α-amylase, chitinase, arginine kinase). However, some differences in spot intensities were observed between gels. While the cockroach allergen-like protein (spot #2) and the 28 kDa desiccation stress protein (spot #9) were present in all fractions with similar relative intensities, spot #3, identified as a cockroach allergen-like protein, was present at high intensity for each *T. molitor* fraction except for TMI. Similarly, the actin-87E-like protein (spot #1) was present in all fractions, except for NDSP where the intensity of the protein spot was low. Furthermore, 12 kDa hemolymph protein b (spot #4 and #5), α-amylase (spot #8), the melanin-inhibiting protein (spot #10), as well as chitinase (spot #11) were predominantly abundant in soluble protein extracts NDSP and HDSP. Conversely, an arginine kinase fragment (spot #7) could only be found in whole meals TMI and TMD. Finally, the 86 kDa early-staged encapsulation inducing protein and hexamerin 2 (spot #6) were only abundant in HDSP. It is worth noting that some identified proteins were associated only with other insects from the *Tenebrionidae* family, such as *Tribolium castaneum*, since they were absent from the Uniprot database for *T. molitor* (Table 2).
