Aug 2026· Frontiers in Soft Matter· Vol 6· 0 citations· 58 references
Abstract
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.
Aquatic gel foods, including surimi, minced crustacean products, and algal gels, are important platforms for aquatic protein valorization. However, their production is constrained by uneven thermal gelation, endogenous enzyme-driven deterioration, nutrient loss, additive dependence, and limited flexibility for 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. The central premise is that physical energy delivery can regulate protein conformation, intermolecular interactions, water mobility, and gel network assembly, thereby affecting texture, nutritional quality, safety, and consumer acceptance. Rather than presenting technologies separately, the review groups them into non-thermal physical fields, thermally assisted volumetric heating, and additive manufacturing. Their roles in remodeling aquatic protein and polysaccharide matrices are discussed alongside matrix-dependent responses and implementation constraints. Available evidence suggests that, under optimized and matrix-specific conditions, these technologies may contribute to gel network reinforcement, salt and fat reduction, nutrient retention, improved digestibility, shelf-life extension, by-product valorization, and personalized product development. However, overprocessing, nonuniform energy delivery, and matrix-specific responses can offset these benefits. Reported outcomes vary with processing intensity, treatment duration, raw-material composition, ionic conditions, and product geometry, limiting direct generalization across aquatic gel systems. Industrial translation is further constrained by fragmented mechanisms, limited quantitative structure-function relationships, insufficient scale-up validation, inconsistent evaluation metrics, and limited life-cycle, techno-economic, and consumer evidence. Future work should integrate standardized assessment, online monitoring, multi-field design, predictive modeling, and sustainability evaluation to support healthy, sustainable, and personalized aquatic gel foods.
Yantong Li, Cewen Yang, Xinyi Zhang et al.· Comprehensive Reviews in Foo...· 0 citations
The growing demand for sustainable, ethical, and healthier foods has generated interest in plant‐based proteins as alternatives to animal proteins. Although promising, these proteins often face limitations due to inherent characteristics that restrict their application diverse food products. These include low solubility, foaming, emulsification, and gelation, which collectively impede their utilization in food systems. To overcome this, cold plasma, a nonthermal and eco‐friendly technology, has recently emerged as a promising strategy to enhance protein functionality without compromising nutritional quality. This review examines the mechanisms, functional outcomes, and food applications cold plasma in plant‐based proteins, with focus on comparison with conventional and emerging protein modification technologies. Rigorous literature search was conducted to obtain relevant information from databases used to develop the review. The results revealed that plasma treatments usually generate reactive oxygen and nitrogen species, ultraviolet photons, and charged particles that can unfold protein structures, promote cross‐linking, and alter surface properties like charge and hydrophobicity. These modifications improve hydration, dispersion, and stability, and enhance performances in emulsions, foams, and gels in plant protein products. Cold plasma offers advantages in terms of energy efficiency and versatility, despite challenges of reproducibility, oxidation, scalability, and consumer acceptance. Combining cold plasma with other processing techniques like ultrasound or fermentation, while applying advanced omics approaches could offer better understanding and open opportunities for food applications. Overall, cold plasma offers a valuable approach to enhance functionality of plant proteins, with strong potential to support innovation, sustainability, and nutrition in the food industry.
Aishat O. Adejoh, Linda A. Kpomblekou, F. Ekezie et al.· International journal of foo...· 0 citations
Food proteins play important roles in determining the nutritional quality and functional properties of food systems. However, many native proteins exhibit limited solubility, digestibility, and bioactivity, restricting their industrial applications and nutritional utilization. Although numerous studies have investigated the effects of thermal and non-thermal processing on protein modification, current understanding remains fragmented, and systematic comparisons of the underlying structure-function relationships across different processing technologies are still limited. This review provides a comparative and mechanistic perspective on how thermal treatments (e.g., traditional heating methods, ohmic heating, microwave and radio frequency) and non-thermal technologies (e.g., high hydrostatic processing, cold plasma, pulsed electric fields, ultrasound and irradiation) regulate the structural evolution and functional properties of food proteins. Particular emphasis is placed on the relationships between processing-induced changes in secondary and tertiary structures and the consequent alterations in protein solubility, digestibility, and bioactivity, thereby providing insights for the rational design of protein modification strategies.
Understanding the interaction between proteins and polysaccharides is fundamental for designing food structures, yet the potential of ultrasound to precisely modulate these interactions has not been systematically reviewed. This review critically examines the mechanistic role of acoustic cavitation and its associated physical and chemical effects in driving the formation of protein-polysaccharide complexes. We highlight how ultrasound-induced shear forces, micro-turbulence, and free radical generation not only accelerate covalent conjugation via the Maillard reaction but also reinforce non-covalent forces, such as hydrophobic interactions, hydrogen bonding, and electrostatic contacts, by inducing conformational changes in biopolymers. These ultrasound-mediated structural modifications result in significantly improved techno-functional properties, including solubility, emulsification, and foaming performance. We further discuss how these enhanced complexes are enabling innovations across emulsion stabilization, gel fabrication, bioactive compound encapsulation, and edible film formation. Finally, we identify critical research priorities, particularly the correlation between ultrasonic parameters and molecular interaction mechanisms, the structural characterization of conjugates, and the evaluation of their safety for food applications. By providing a comprehensive framework that bridges fundamental sonochemistry with food material science, this review positions ultrasound as a versatile and sustainable tool for engineering advanced food systems.
Qiufang Liang, Panpan Cao, Yunxia Du et al.· Ultrasonics sonochemistry· 0 citations
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.
Xue Bai, Kai Zhou, Ranran Pang et al.· Journal of Food Science· 0 citations
Pectin-protein complexes have emerged as promising functional ingredients in texture-modified foods (TMF) due to their multifunctional roles in gelation, emulsification, and water retention. These properties enable the design of customized textures for applications such as dysphagia-friendly products, plant-based meat analogs, and 3D food printing. However, their broader utilization remains limited by an incomplete understanding of formation mechanisms, regulatory factors, and challenges related to stability and industrial scalability. This review summarizes the formation mechanisms of pectin-protein complexes, including phase behavior, preparation approaches, interaction forces, and key factors influencing texture development. Their functional properties and applications in five representative areas (dysphagia-oriented foods, 3D printing structures, encapsulation systems, plant-based analogs, and fat replacers) are discussed. Recent advances highlighting structure-function relationships between molecular interactions and macroscopic textural properties are critically evaluated, along with the translational gap between fundamental research and scalable production. The formation of pectin-protein complexes is mainly governed by intermolecular forces such as electrostatic interactions, hydrophobic interactions, hydrogen bonding, and covalent cross-linking. These interactions can be regulated by adjusting pH, ionic strength, temperature, enzymatic treatment, and processing conditions, thereby controlling supramolecular structure, stability, and sensory attributes. Although pectin-protein complexes offer significant potential for texture engineering, industrial application is hindered by raw material variability, limited processing control, and economic considerations. Future research should focus on clarifying molecular mechanisms, establishing selection criteria for pectin, and developing sustainable extraction strategies to facilitate large-scale implementation.
Jin Xie, Jing-Xuan Wang, Xiaoxian Liu et al.· Comprehensive Reviews in Foo...· 0 citations