Lipid-protein interactions in food systems: Mechanisms, thermodynamics, and analytical approaches

This chapter provides a comprehensive overview of lipid-protein interactions in food systems, focusing on their physicochemical mechanisms, analytical techniques, and implications for food quality, nutrition, and functionality. These interactions, governed by hydrophobic, electrostatic, hydrogen bonding, and van der Waals forces, are influenced by multiple factors such as pH, temperature, and ionic strength during food processing. Both experimental techniques, including spectroscopy (fluorescence, CD, FTIR), calorimetry (ITC, DSC), microscopy (CLSM, SEM), and gel electrophoresis, as well as computational approaches such as molecular dynamics simulations and molecular docking are used to characterize the structural, thermodynamic, and dynamic properties of these interactions. Lipid-protein interactions affect key lipid characteristics such as chemical stability, solubility, and gastrointestinal behavior, while also modulating protein properties like digestibility, thermal stability, gelling, foaming capacity, phosphorylation, and aggregation. Moreover, these interactions can influence health-related outcomes, including lipid oxidation, cholesterol metabolism, and allergenicity. Understanding these interactions provides valuable insights for the development of novel and functional food products with enhanced stability and bioavailability. The dynamic nature of lipid-protein interactions necessitates continued research using integrated experimental and computational approaches to optimize their role in modern food systems.