Interactions between dairy proteins and aroma compounds: A comprehensive review of mechanisms, processing effects, and analytical methods

Dairy aroma perception is largely governed by the interactions between dairy proteins (DP) and dairy aroma compounds (DAC), which together determine the binding, retention, and release behaviors of volatile molecules in complex dairy matrices. This review provides a comprehensive synthesis of recent advances in understanding DP-DAC interactions from molecular characteristics to processing-induced modulation and analytical evaluation. Current evidence demonstrates that hydrophobic forces, hydrogen bonding, electrostatic interactions, and van der Waals forces dominate non-covalent binding, whereas thermal processing, oxidation, and Maillard-derived reactions can introduce covalent modifications that markedly alter aroma stability. Processing variables, such as heat treatment, pH, ionic strength, fermentation, homogenization, and drying, dynamically reshape protein conformation and matrix microstructure, thereby regulating aroma retention and release kinetics. Advances in spectroscopic analysis, chromatographic-mass spectrometric quantification, calorimetric and kinetic measurements, molecular simulation, and machine learning have deepened mechanistic insights into interaction pathways and energetics. Despite substantial progress, challenges remain in quantifying covalent interactions, linking model-system observations to real dairy matrices, and predicting multi-scale aroma behavior under industrial conditions. Emerging integrated approaches combining multi-modal analytics, molecular dynamics, and kinetic modeling are expected to support the rational design of protein-based strategies for flavor stabilization, controlled aroma delivery, and sensory optimization in dairy products.