Effects of thermal and non-thermal processing on the structure and function of food proteins: A review.

Impact of Novel and Emerging Nonthermal Technologies on the Functionality and Digestibility of Poultry-Derived Proteins

Poultry meat and eggs are high-quality protein sources, but thermal processing alters their nutritional and functional attributes. Emerging non-thermal and novel processing methods, such as high-pressure processing, ultrasound, pulsed electric fields, cold plasma, moderate electric fields, magnetic fields, ozone treatment, and pulsed light, are increasingly popular as substitutes. This review examines the effects of nonthermal and novel processing technologies on poultry meat and egg proteins. The review focuses on the interrelationship among protein structure, functionality, and digestibility, with emphasis on the mechanism underlying structural modification, altered intermolecular interactions, and controlled protein unfolding. Under optimized conditions, nonthermal technologies can maintain protein integrity and improve functionality such as water-holding capacity, emulsification, gelation, and tenderness in poultry meat. In egg proteins, non-thermal technologies improve solubility, emulsification, foaming, and gelation through structural modification, intermolecular interactions, and controlled unfolding, thereby exposing enzymatic cleavage sites and enhancing digestibility. Evidence exists for enhanced proteolysis by peptide release and amino acid availability in nonthermal treatments, whereas studies on poultry meat remain limited. This review integrates existing evidence and critical gaps in interpreting structure–functionality–digestibility interrelation, and highlights the potential of nonthermal technologies for producing poultry-derived foods with higher functional quality and nutritional value.

Multiscale structural modulation of plant proteins via ultrasound and electro-physical processing: from extraction to functional food matrices

The transition toward sustainable food systems has increased interest in plant proteins as alternatives to animal-derived proteins due to their lower environmental impact, including reduced greenhouse gas emissions, land use, and resource demand. However, their broader application is constrained by structural characteristics that limit solubility, interfacial behaviour, digestibility, and sensory performance. Many plant proteins exhibit compact globular structures stabilized by strong intermolecular interactions, restricting their functionality in complex food systems. These structural constraints operate across a hierarchy of scales, from the molecular conformation of secondary and tertiary structures to the micro- and macro-structural organisation of protein aggregates, interfacial films, and gel networks, and it is this multiscale organisation that ultimately governs functional performance in complex food matrices. Non-thermal processing technologies, namely, ultrasound, pulsed electric fields (PEF), and cold plasma, together with the electro-thermal technique of ohmic heating, offer promising approaches for modifying protein structure without causing extensive thermal damage. These methods can induce partial unfolding, alter aggregation behaviour, and enhance the exposure of functional groups, thereby improving solubility, emulsification, and gelation properties. This review adopts an explicit multiscale framework to link molecular-level conformational changes to microstructural aggregation and macroscopic structure–property relationships. It summarizes the mechanisms, functional impacts, and industrial relevance of these technologies in plant protein processing. Building on this analysis, the review evaluates the principal technical bottlenecks, the economic and industrial scalability, and the priority directions for future research on non-thermal and electro-thermal processing of plant proteins.

Dual-Protein Systems in Foods: Structure-Function Relationships, Nutritional Impacts, and Applications.

Growing demand for sustainable, nutritious, and high-quality protein foods has highlighted limitations of single-source proteins and promoted interest in dual-protein systems (DPS). DPS are edible protein matrices intentionally formed from two distinct primary protein components, derived from different biological sources or complementary protein fractions, and processed within a shared physicochemical environment. This review integrates their definition, fabrication strategies, interaction mechanisms, functional properties, nutritional implications, and food applications. Protein-protein interactions, including electrostatic, hydrophobic, hydrogen-bonding, and disulfide-mediated interactions, regulate unfolding, aggregation, interfacial adsorption, and network formation. Processing methods such as blending, co-precipitation, ultrasound, microwave treatment, pH shifting, fermentation, germination, and enzymatic cross-linking further modify structure and functionality. These changes affect solubility, emulsification, foaming, gelation, rheology, digestibility, and storage stability. Nutritionally, DPS may improve amino acid complementarity, digestion behavior, and bioactive peptide release, but their benefits depend on protein source, ratio, processing conditions, and matrix. Applications in meat and seafood analogues, dairy-like systems, bakery products, beverages, and structured foods show potential for quality and sustainability improvement. However, sensory defects, allergenicity, limited digestibility evidence, and insufficient consumer studies remain challenges. This review provides a framework for designing stable, nutritious, sustainable, and acceptable dual-protein foods.

Methodological approaches to assess protein digestibility with an emphasis on plant-derived foods.

Physical Processing of Aquatic Gel Foods: From Protein Structure Regulation to Health, Sustainability, and Personalized Design.

This review synthesizes recent advances in physical processing of aquatic gel systems from a process-structure-function perspective, comparing the mechanisms, benefits, and limitations of major technologies.

Effects of cold plasma treatment on food bioactive compounds

Cold plasma technology has emerged as a promising non-thermal food processing approach due to its ability to enhance food safety while preserving or improving nutritional and functional quality. This review evaluates recent advances in the application of cold plasma for modulating food bioactive compounds, with particular emphasis on polyphenols, carotenoids, vitamins, and natural pigments. Cold plasma operates in a thermodynamically non-equilibrium state, generating reactive oxygen and nitrogen species that interact with food matrices through complex and matrix-dependent mechanisms. Evidence indicates a dual-effect behaviour under optimized conditions, cold plasma can disrupt cellular structures, promote macromolecule depolymerization, inactivate degradative enzymes, and enhance the release and bioaccessibility of bioactive compounds. Conversely, excessive treatment intensity or prolonged exposure may trigger oxidative degradation, leading to losses in sensitive constituents. Recent literature highlights the strong dependence of cold plasma outcomes on processing parameters, plasma generation methods, gas composition, and intrinsic food characteristics. In addition to compositional changes, cold plasma has been shown to influence antioxidant activity, pigment stability, and post-digestion bioaccessibility highlighting its relevance for functional food development. Despite its significant potential, challenges remain regarding process standardization, scalability, and regulatory acceptance. Overall, this review identifies critical knowledge gaps and future research directions necessary to facilitate the safe and effective industrial implementation of cold plasma technology in food systems.