Aug 2026· Food Chemistry· Vol 526, pp.
150765
· 0 citations· 31 references
Medicine
Abstract
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.
This study compared the effects of ultrasonic (US) and ultra-high pressure (UHP) treatments at varying intensities on the multi-scale structure and physicochemical properties of goat liver protein (GLP), and evaluated their potential to enhance emulsified pork sausage quality. US treatment at two selected durations (600 W, 20 kHz, 2 and 15 min) induced different structural and functional responses in GLP, including partial protein unfolding, exposure of sulfhydryl and hydrophobic groups, and moderate oxidation. UHP treatment elicited distinct pressure-level-dependent differences in volumetric compression and conformational rearrangement between the selected pressure levels. Moderate UHP improved water retention, heating stability, and gel network formation, whereas extreme pressure caused excessive aggregation, leading to less favorable instrumental texture parameters and electronic-nose response patterns. Comparative analysis revealed that US primarily enhanced dynamic structure-function coupling, while UHP optimized structural stability and processing performance. These findings elucidate distinct mechanistic pathways for US and UHP in protein modification and provide guidance for non-thermal strategies to improve protein functionality and meat product quality.
Xiangxi Yan, Jiamin Shen, Changyu Zhou et al.· International Journal of Bio...· 0 citations
Understanding and modulating myofibrillar protein (MP) gelation is essential for the rational design of processed meat products. This study investigated the effects of high internal phase Pickering emulsions (HIPPEs) stabilized by pea protein (PP) and different ionic celluloses, cationic (PQC), non-ionic (HPMC), and anionic (CMC), on the gel properties and underlying mechanisms of MP composite gels. HIPPEs were incorporated into MP gels at a 30% substitution level (w/w, based on total gel formulation), and their effects on water retention, texture and color, physicochemical properties, rheological behavior, secondary structure, water distribution, and microstructure were systematically evaluated. Results indicated that all HIPPEs significantly improved gel properties, with PP-PQC HIPPEs exhibiting the most pronounced enhancements: smallest particle size, highest water-holding capacity (WHC), superior texture, and most compact gel network. The incorporation of HIPPEs promoted protein unfolding, increased surface hydrophobicity, facilitated the conversion of α-helices to β-sheets, and encouraged disulfide bond formation, leading to a denser and more uniform gel structure. These findings demonstrate that ionic cellulose-based HIPPEs, especially those stabilized by cationic cellulose, can effectively modulate MP gelation, offering a promising strategy for developing high-quality, reduced-fat meat products.
This study examined the influence of quinoa protein modified by high-pressure homogenization (HQP) on the gelation behavior, water mobility, rheological attributes, and microstructure of chicken breast batters. Cooking yield and gel strength of batter gels increased progressively from 88.93% and 859.56 g to 95.35% and 1467.34 g, respectively, with elevated HQP supplements. Concurrently, L⁎ and a⁎ values dropped gradually, whereas the b⁎ value elevated evidently (P < 0.05). Textural indicators all displayed an ascending-descending trend, reaching optimal values at 12% HQP incorporation. Rheological assessment demonstrated that HQP markedly enhanced the G' value throughout thermal and frequency scan analyses. Low-field nuclear magnetic resonance (LF-NMR) data indicated that HQP significantly elevated the immobilized water fraction while concomitantly reduced the free water proportion. Fourier transform infrared (FTIR) spectroscopy indicated a marked decline in α-helix fraction paired with elevated β-sheet formation. SEM imaging confirmed that HQP supplementation facilitated the formation of a smoother and more compact gel architecture. Collectively, HQP demonstrates strong potential as a functional ingredient for enhancing emulsified chicken systems.
Yanyan Zhao, Xin Yao, Qi-Zhao Han et al.· Food Chemistry: X· 0 citations
This study conducts a scientific elucidation of the traditional ice-cooking technique for lamb. Compared with conventional water-cooking, the ice-cooking established a distinct thermal process: an initial low-temperature holding phase (below 20 °C for approximately 120 s) followed by a more gradual and uniform heating. Analysis of spatial structure and rheological properties indicated that this gentle heating effectively suppressed excessive protein aggregation and hydrophobic groups exposure, promoting an ordered, continuous gel network (exhibiting higher storage modulus). The muscle fibers in ice-cooked lamb were more tightly arranged, and the ionic and hydrogen bonds that stabilize protein structure were sufficiently preserved, thus retaining more immobile water. Consequently, ice-cooked lamb demonstrated notably improved (P < 0.01) water-holding capacity and tenderness compared to water-cooked lamb, along with superior digestibility and inhibited lipid oxidation. This study decodes the traditional cooking practice by modern food science principles, providing a theoretical foundation for quality optimization in meat cooking.
Zichun Jin, Lei Zhang, Yani Yin et al.· Food Chemistry· 0 citations
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.
Fangqi Yuan, Quanyou Guo, Zuofeng Shi et al.· Food Research International· 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.
