Bioactivities of Mealworm ( L.) Larvae Hydrolysates Obtained from Artichoke ( L.) Proteases.

In this study, we aimed to obtain hydrolysates with bioactive peptides from mealworm (Alphitobius diaperinus L.) larvae using an artichoke (Cynara scolymus L.) enzyme extract. Two types of substrates were used: the raw larvae flour (LF) and its protein extract (PE). The hydrolysis yield, considering the peptide concentration of the hydrolysates, was higher in PE hydrolysates than in LF hydrolysates (6.39 ± 0.59 vs. 3.02 ± 0.06 mg/mL, respectively). However, LF showed a higher antioxidant activity against the DPPH radical than PE (59.10 ± 1.42 vs. 18.79 ± 0.81 µM Trolox Eq/mg peptides, respectively). Regarding the inhibitory activity of angiotensin-I-converting enzyme (ACE), an IC50 value of 111.33 ± 21.3 µg peptides/mL was observed in the PE. The identification of the peptide sequence of both hydrolysates was conducted, and LF and its PE presented 404 and 116 peptides, respectively, most with low molecular weight (<3 kDa), high percentage of hydrophobic amino acids, and typical characteristics of well-known antioxidant and ACE-inhibitory peptides. Furthermore, the potential bioactivity of the sequences identified was searched in the BIOPEP database. Considering the antioxidant and ACE-inhibitory activities, LF hydrolysates contained a larger number of sequences with potential bioactivity than PE hydrolysates.