Oct 2026· Food Research International· Vol 242 Pt 4, pp.
120133
· 0 citations· 42 references
Medicine
Abstract
As a green non-thermal technology, plasma-activated water (PAW) generates reactive oxygen and nitrogen species (RONS) through plasma-liquid interactions and thereby affects the oxidation, conformation, and functionality of aquatic myofibrillar proteins (MPs). To investigate the regulatory effects of PAW on yellow croaker MPs, the original extraction buffer was replaced with plasma-activated buffer of different activation times, and the oxidation, conformation, and functional changes of MPs during chilled storage were evaluated. The results indicate that moderate PAW treatment induces mild oxidation and modulates protein conformation. PAW-30 s showed a lower bromophenol blue binding capacity (31.55 ± 0.95 μg), indicating limited intermolecular interactions and moderate aggregation that partially masked hydrophobic groups and improved structural stability. As the treatment time was extended to 60 s and 120 s, PAW further promoted the oxidation of thiol groups, altered surface hydrophobicity and intrinsic fluorescence characteristics, and enhanced the conformational rearrangement and intermolecular cross-linking of MP. SDS-PAGE results showed that the effects of PAW were primarily concentrated on the myosin heavy chain (MHC), as shown by MHC band weakening and increased high-molecular-weight aggregates, without obvious low-molecular-weight degradation. Molecular docking analysis further indicated that representative reactive oxygen species in PAW, H₂O₂ and O₃ can bind to specific regions on the MHC surface, thereby inducing local microenvironmental disturbances and oxidative modifications. Overall, PAW regulated yellow croaker MPs mainly through mild oxidation-induced conformational rearrangement and intermolecular cross-linking rather than extensive chain cleavage, with moderate activation being more favorable for maintaining MP structural stability and functional properties.
This study investigated the effects of air freezing (AF), liquid immersion freezing (LIF), and high hydrostatic pressure combined with liquid immersion freezing (HPP + LIF) on the structural and functional properties of myofibrillar proteins (MP) from bighead carp. Compared with AF and LIF, HPP + LIF significantly improved MP dispersion, with significant increases in protein solubility and absolute zeta potential, as well as significant reductions in turbidity and particle size, indicating reduced formation of large protein aggregates during freezing. Moreover, HPP + LIF induced conformational changes, enhancing surface hydrophobicity and exposure of aromatic residues, with decreased α-helix content and increased β-sheet content, and reduced conversion from ordered to disordered structures during freezing. In addition, this treatment enhanced thermal stability and modulated intermolecular interactions, including hydrogen bonds, hydrophobic interactions, and disulfide bonds. Microstructural observations further showed that HPP + LIF limited the formation of large aggregates while maintaining a relatively uniform distribution of protein particles. Overall, HPP + LIF alleviated freezing-induced structural deterioration and regulated aggregation behavior of MP during freezing, providing insights for improving the quality of surimi products from freshwater fish.
Tao Song, Yuyang Zhang, Xinxin Li et al.· Food Research International· 0 citations
Lipid peroxidation products can induce oxidative modification of myofibrillar proteins (MPs), thereby compromising their water-holding capacity (WHC), but the underlying molecular mechanism remains unclear. This study systematically investigated the mechanism of MDA-induced WHC deterioration in bovine myofibrillar proteins (MPs) using multispectral techniques, redox proteomics, and molecular docking. Results demonstrated that low MDA concentrations caused relatively limited water release. Structural alterations became evident at 2 mM, whereas pronounced WHC deterioration occurred at 5–10 mM. At these higher concentrations, centrifugal loss increased by up to 48.80%, and immobilized water migrated to free water (p < 0.05). This functional decline was accompanied by substantial structural remodeling, characterized by a transition from α-helix to β-sheet conformations, decreased hydrogen bonding, and enhanced disulfide-associated cross-linking. Furthermore, redox proteomics identified 581 differential cysteine redox sites, including 343 increased and 238 decreased sites. Among these sites, 57 markedly decreased sites associated with myofibrillar and cytoskeletal proteins were further characterized, including sites in actin, α-actinin, myosin, and LIM-domain-containing proteins. Motif analysis further revealed a characteristic cysteine-rich C-x-x-C-x-C sequence pattern surrounding responsive oxidation sites. Molecular docking of 12 representative cysteine sites supported the spatial feasibility of MDA pre-association near these cysteine-containing regions, with actin C258 exhibiting the most negative docking score among the examined sites (−3.3 kcal/mol). These findings reveal that cysteine redox remodeling was associated with structural reorganization and increased water mobility, thereby contributing to WHC deterioration.
He Li, Zhen-Yu Fang, Qin Wu et al.· Foods· 0 citations
This study established a refined plasma activated water (PAW) system to distinguish the effects of acidification and H2O2 from the broader effects of PAW-derived reactive species on gelatin gelation. Acidification altered surface charge and resulting in an increased in β-turn content (38.90%) and ionic bonding (15.23%). H2O2 treatment induced oxidative modification, leading to sulfhydryl oxidation, increased hydrophobic interactions and decreased gelation temperature, but partially disrupted triple-helix-based crosslinking. Notably, PAW exerted unique enhanced effects, significantly enhancing gelling properties by strengthening hydrogen bonding and lowering the eutectic point. Molecular docking further suggested that PAW-derived reactive species promoted hydrogen bonding and hydrophobic interactions with gelatin. These improvements highlight the potential of PAW-modified gelatin for functional gelled foods and gelatin-based packaging requiring enhanced structural and moisture stability, although validation in complex food matrices and practical processing systems remains necessary.
Mengzhe Li, Ruichang Gao, Xin Wang et al.· Food Chemistry: X· 0 citations
In this study, we evaluated how varying concentrations of two exogenous proteins, egg white protein (EWP) and whey protein isolate (WPI) influence heat‐induced aggregation and gelation of cod myofibrillar proteins (MPs). Addition of exogenous proteins enhanced the MP solubility and surface hydrophobicity while reducing the turbidity and total sulfhydryl levels. These physicochemical changes occurred during heating in three kinetic phases, an initial rapid phase (0–30 min), a slower transitional phase (30–60 min), and a second rapid aggregation phase (70–90 min) until equilibrium was reached. Dynamic rheology revealed that EWP enhanced G′ at moderate concentrations but reduced it at higher levels, while WPI caused a progressive decline in G′ with increasing concentration. Gel property analysis showed that EWP‐M (MP:EWP = 2:14) produced the highest gel strength, whereas WPI‐L (MP:WPI = 1:15) resulted in the lowest cooking loss and highest water‐holding capacity (WHC). WPI‐containing systems exhibited slightly lower gel strength but showed improved water retention and a uniform microstructure. Notably, a 1:1 EWP‐WPI combination showed synergistic network solubility, hydrophobic exposure, and uniform microstructure, leading to high gel strength with minimal cooking loss and maximum WHC. Mechanistically, EWP acted as a structural enhancer, promoting gel network strengthening and increased rigidity, whereas WPI functioned primarily as a filler, enhancing water retention and reducing structural heterogeneity. These findings offer key insights into MP/EWP‐WPI interactions and support the optimization of composite protein gel systems.
Safia Aslam, Jinjin Xing, Hui Tao et al.· Journal of texture studies· 0 citations
This study evaluated the effects of low-frequency alternating magnetic field (AMF) on mass transfer, myofibrillar protein (MP) structure, and quality of beef during marination. AMF significantly enhanced NaCl and moisture diffusion, reducing marination time by over 50%. The improvement was linked to AMF-induced MP conformational unfolding, increased surface hydrophobicity, reduced solubility, and promoted protein aggregation via strengthened hydrophobic interactions. Unlike conventional treatments, AMF-driven aggregation widened inter-myofibrillar spaces, facilitating ion and water migration. Additionally, AMF reduced cooking loss while maintaining shear force and texture, indicating improved water-holding capacity without compromising tenderness. These effects were attributed to microstructural remodeling that preserved myofibrillar integrity. Overall, AMF-assisted marination enhances processing efficiency and technological quality, representing a promising non-thermal strategy for meat processing.
Lixin Du, Qihan Liu, Guanghong Zhou et al.· Food Chemistry· 0 citations
This study investigated the effects of controlled thermal modification (95 °C, 10-60 min) on the structural and foaming properties of soybean lipophilic protein (SLP). Results indicated that moderate heating (10-30 min) triggered structural unfolding, increased hydrophobic group exposure and free sulfhydryl content, and reduced aggregation. Notably, compared to individual protein samples, a 1:1 (w/w) mixture of native and moderately heat-treated SLP jointly promoted protein adsorption at the interface, and facilitated the conformational evolution of the modified protein to form a mechanically robust and dense composite film, thereby substantially improving overall foaming capacity and stability. Conversely, 60-min heat treatment induced large, ordered aggregates that hindered interfacial adsorption and the development of a stable film, compromising the overall foaming performance. These findings offer new insights into the strategic application of SLP in aerated food systems.
