From in silico screening to experimental verification: Identification of novel umami peptides from tamarind (Tamarindus indica L.) seed proteins and their validation in enzymatic hydrolysates.

Umami peptides are key contributors to food flavor enhancement. In this study, novel umami peptides from tamarind seed proteins were identified using an integrated strategy combining in silico screening and experimental validation. A virtual peptide library was screened based on physicochemical properties and bioactivity, yielding six candidates (VSDY, DGIDF, AKNVSDYL, YNDPHC, VPPD, and NDPHCQY). Molecular docking and dynamics simulations revealed stable binding to the umami receptor T1R1/T1R3 via hydrogen bonding and hydrophobic interactions, with binding affinities of -7.9 to -8.8 kcal/mol. Among them, AKNVSDYL exhibited the strongest interaction and highest stability. Sensory evaluation and electronic tongue analysis confirmed the umami characteristics of all peptides, with AKNVSDYL showing the highest intensity, consistent with computational results. Enzymatic hydrolysis followed by UHPLC-ESI-HRMS/MS verified the presence of all predicted peptides. This study provides an efficient strategy for discovering natural umami peptides and supports the valorization of tamarind seed byproducts.