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

Küçük Resim Yok

Tarih

2025

Dergi Başlığı

Dergi ISSN

Cilt Başlığı

Yayıncı

Elsevier

Erişim Hakkı

info:eu-repo/semantics/closedAccess

Özet

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. © 2026 Elsevier Inc. All rights reserved.

Açıklama

Anahtar Kelimeler

Binding kinetics, Electrostatic forces, Hydrogen bonding, Lipids, Protein, Thermodynamic analysis

Kaynak

Interaction of Food Macromolecules: The Matrix of Future Foods

WoS Q Değeri

Scopus Q Değeri

Cilt

Sayı

Künye