Bitter taste receptor 14(T2R14) is one of the most widely regulated bitter taste receptors (T2Rs) and plays a vital role in the research of T2R blockers. In this study, potential T2R14 blockers were identified from the myosin of Mizuhopecten yessoensis. Myosin was hydrolyzed in silico by gastrointestinal proteases, and the peptides were obtained. The peptides' biological activity, solubility, and toxicity were predicted, and the potential T2R14 blocking peptides were docked with T2R14. Subsequently, the in vitro T2R14 blocking activity of the selected peptide was verified by an electronic tongue. The results showed that QRPR had T2R14 blocking activity with an IC50 value of 256.69 ± 1.91 μM. Molecular docking analysis suggested the key role of the amino residues Asp168, Leu178, Asn157, and Ile262 in blocking T2R14, and revealed that the amino acid residues of T2R14 bound with the peptide QRPR via electrostatic interaction, hydrophobic interaction, conventional hydrogen bond, and hydrogen bond. The novel T2R14 blocking peptide QRPR is a potential candidate for suppressing bitterness.