Chia seed peptides (CSPs), liberated from defatted flour via strategic enzymatic hydrolysis, emerge as multifunctional ingredients that fundamentally transform food quality. Specifically, Alcalase and Flavourzyme proteases generate low molecular weight fractions possessing potent angiotensin‐converting enzyme (ACE) inhibition and broad pH solubility, thereby enabling clear beverage fortification and stable emulsion formation in dressings and analogs. Moreover, advanced extraction technologies amplify yield while preserving peptide integrity, and multiomics characterization links specific hydrophobic and aromatic residue sequences to interfacial stabilization and radical scavenging capacity. Furthermore, hydrolysis‐driven structural modulation governs solubility phase behavior across pH and ionic strength, while peptide backbone flexibility dictates emulsifying and foaming prowess. In parallel, in silico prediction tools accelerate the discovery of safe, bioactive sequences. This review uniquely delineates the translational framework that reconciles in vitro bioactivity with in‐matrix techno‐functional performance, providing a rigorous roadmap for overcoming sensory and stability hurdles. Consequently, CSPs enhance water holding in baked goods, delay lipid oxidation in meats, and replace eggs in mayonnaise, all while aligning with clean‐label demands. Finally, the review further evaluates regulatory pathways and bitterness mitigation strategies, cementing CSPs as a basis for sustainable, health‐promoting food architectures.
Joachim Matondo (Thu,) studied this question.