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This study investigated the effect of heat treatment of edible insects on antioxidant and anti-inflammatory activities of peptides obtained by in vitro gastrointestinal digestion and absorption process thereof. The antioxidant potential of edible insect hydrolysates was determined as free radical-scavenging activity, ion chelating activity, and reducing power, whereas the anti-inflammatory activity was expressed as lipoxygenase and cyclooxygenase-2 inhibitory activity. The highest antiradical activity against DPPH• (2,2-diphenyl-1-picrylhydrazyl radical) was noted for a peptide fraction from baked cricket Gryllodes sigillatus hydrolysate (IC50 value 10.9 µg/mL) and that against ABTS•+ (2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) radical) was the highest for raw mealworm Tenebrio molitor hydrolysate (inhibitory concentration (IC50 value) 5.3 µg/mL). The peptides obtained from boiled locust Schistocerca gregaria hydrolysate showed the highest Fe2+ chelation ability (IC50 value 2.57 µg/mL); furthermore, the highest reducing power was observed for raw G. sigillatus hydrolysate (0.771). The peptide fraction from a protein preparation from the locust S. gregaria exhibited the most significant lipoxygenase and cyclooxygenase-2 inhibitory activity (IC50 value 3.13 µg/mL and 5.05 µg/mL, respectively).

The aim of this study was to determine the effect of heat treatment of edible insects on antioxidant and anti‐inflammatory activities of peptide fractions from hydrolysates obtained by in vitro gastrointestinal digestion thereof. Identification of bioactive peptides from the edible insects and their chemical synthesis were carried out as well. The highest antiradical activity against ABTS•+ and DPPH• was noted for the peptide fraction from the Gryllodes sigillatus protein preparation (EC50 value 2.75 and 6.91 μg mL−1, respectively). This fraction exhibited the strongest LOX and COX‐2 inhibitory activity (IC50 value 0.13 and 0.26 μg mL−1, respectively). The peptide fraction from the Tenebrio molitor protein preparation showed the highest Fe2+ chelating ability (EC50 value 2.21 μg mL−1) and the highest reducing power (0.198). The heat treatment process has a positive effect on the antioxidant and anti‐inflammatory properties of peptides. All identified and synthesised peptides from insect protein showed antioxidant and anti‐inflammatory activity.

Generally, bioactive peptides are natural compounds of food or part of protein that are inactive in the precursor molecule. However, they may be active after hydrolysis and can be transported to the active site. Biologically active peptides can also be synthesized chemically and characterized. Peptides have many properties, including antihypertensive, antioxidant, antimicrobial, anticoagulant, and chelating effects. They are also responsible for the taste of food or for the inhibition of enzymes involved in the development of diseases. The scientific literature has described many peptides with bioactive properties obtained from different sources. Information about the structure, origin, and properties of peptides can also be found in many databases. This review will describe peptides inhibiting the development of current diseases, peptides with antimicrobial properties, and new alternative sources of peptides based on the current knowledge and documentation of their bioactivity. All these issues are part of modern research on peptides and their use in current health or technological problems in food production.