Identification, screening and taste mechanisms analysis of two novel umami pentapeptides derived from the myosin heavy chain of Atlantic cod ( Gadus morhua ).

Umami peptides are new ingredients for the condiment and seasoning industries, with healthy and nutrition characteristics, some of which were identified from aquatic proteins. This study aims to further explore novel umami peptides from Atlantic cod ( Gadus morhua ) by combining in silico , nano-HPLC-MS/MS, sensory evaluation, and electronic tongue analysis. Two novel peptides, Leu-Val-Asp-Lys-Leu (LVDKL) and Glu-Ser-Lys-Ile-Leu (ESKIL), from the myosin heavy chain of Atlantic cod ( Gadus morhua ), were screened and confirmed to have strong umami tastes with the thresholds of 0.427 mM and 0.574 mM, respectively. The molecular docking was adopted to explore the interactions between the umami peptides and the umami taste receptor T1R1/T1R3, which showed that the umami peptides interacted with T1R1/T1R3 mainly by electrostatic interaction, hydrogen bond interaction, and hydrophobic interaction. Furthermore, the physicochemical properties of the peptides were investigated by in silico methods and cell viability experiments. This study will provide a better understanding of the umami taste in Atlantic cod and will promote the development of condiments and seasonings.