Identification of novel salty peptides in Tenebrio molitor by a combination of computer analysis and sensory evaluation: exploring the underlying mechanism of saltiness formation

Abstract Edible insect protein is an ideal source of new salty peptides. In this study, 55 polypeptides were identified from Tenebrio molitor protein though virtual hydrolysation and 12 of them were predicted to have a salty taste. Four novel salty peptides (ADYYL, ADHPF, SYHESPEL, and VVDHPF) were selected after sensory prediction. All of them were found to form stable complexes with receptor protein TMC4. Among which, SYHESPEL exhibited the best affinity energy (−8.3 kcal/mol) and binding ability, being the most stable complex. The results of sensory and electronic tongue analysis of synthesised peptides showed that all the four peptides had good saltiness, and the saltiness of SYHESPEL peptide was the strongest (threshold 0.0938 ± 0.054 mmol/L). The study has established a rapid screening method for salty peptides and elucidated the binding mechanism of salty peptides derived from T. molitor with their receptors, providing a theoretical reference for the development and application of edible insect proteins.