Abstract
Umami peptides are an important component of food flavoring agents and have high nutritional value. This work aimed to identify umami peptides from tuna skeletal myosin using a new model method of computer simulation, explore their umami mechanism, and further validate the umami tastes with sensory evaluation. Umami peptides LADW, MEIDD, VAEQE, and EEAEGT were discovered, and all of them bound to taste type 1 receptor 1 and receptor 3 via hydrogen bonds and van der Waals forces to form stable complexes. LADW exhibited the best affinity energy and binding capability. Sensory evaluation and electronic tongue confirmed that all peptides possessed an umami taste, and LADW exhibited the strongest umami intensity. This study not only explored four novel umami peptides to improve the value of tuna skeletal myosin but also provided a new method for the rapid discovery of umami peptides.
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