Insects are rich in proteins and obtained by environmentally friendly processes. As an alternative source of proteins, can be consumed directly or as an ingredient in food formulations. In recent years, there has been a great interest in the use of insect proteins as substrate to obtain bioactive peptides. Enzymatic hydrolysis is the most common method used to obtain these compounds; however, their bioactivity can be modified during digestion, being necessary to evaluate the bioaccessibility of the peptides. In this sense, the objective of this work was to evaluate how simulated digestion affects the bioactive properties of black cricket (Gryllus assimilis) protein hydrolysates obtained by the use of the commercial proteases Alcalase, Flavourzyme and Neutrase. For this, black cricket protein hydrolysates were evaluated for their antioxidant, antidiabetic and antihypertensive properties, before and after simulated digestion. In vitro digestion was performed according to the INFOGEST method, reproducing the oral, gastric and intestinal phases in terms of pH, temperature, presence of enzymes and bile salts. After simulated digestion, the hydrolysate increased by 17%, 246%, and 175% their ABTS- and DPPH- radicals scavenging activities, and the Ferric Reducing Antioxidant Power Assay (FRAP) , respectively. The α-amylase and α-glucosidase inhibitory activities (antidiabetic properties) of the hydrolysates after digestion were 47.87% and 12.73%, respectively, and did not differ from the undigested sample (p < 0.05). The angiotensin-converting enzyme (ACE) inhibitory activity (antihypertensive properties) reached 42.22%, but this property was completely lost after in vitro digestion. The results showed that simulated digestion of black cricket protein hydrolysates can modify their bioactive properties. While groups that confer antioxidant power are exposed, sequences of peptides necessary for the inhibitory activity of enzymes can be cleaved, requiring additional studies for the development of strategies to maintain these properties.