Aug 2026· Food Chemistry· Vol 526, pp.
150716
· 0 citations· 52 references
Medicine
Abstract
Mixed-protein gel systems have emerged as an effective strategy for tailoring textural and structural properties in sustainable food systems. In this study, the effects of varying ratios (1:1, 2:1, 4:1) and thermal pretreatment (75, 85, 95 °C) of soy protein isolate (SPI) on the gelation behavior of transglutaminase (TGase)-crosslinked fish gelatin (FG) were systematically investigated. The results showed that TGase-induced FG-SPI complexes exhibited strengthened intermolecular interactions. However, the globular structure of native SPI constrained the formation of a dense and continuous porous microstructure characteristic of TGase-crosslinked FG, thereby reducing the gel strength of the mixed gels. Preheating SPI at 75 °C promoted partial unfolding of the protein, generating additional TGase-accessible reactive sites and intensifying hydrophobic interactions and disulfide bonding, which collectively improved the gel strength and textural properties of the FG-SPI gels. These findings provide a robust framework for designing tunable, sustainable mixed-protein gels for diverse food applications.
The textural properties of food colloidal systems are highly dependent on the gelling characteristics of animal-derived proteins (such as egg protein, EP) and polysaccharides (such as starch, pectin, and gums). The development of plant-based protein alternatives faces challenges such as insufficient gel strength and poor structural stability. This study focused on purified Chlorella protein extract (PCPE). To address the insufficient gel performance of PCPE, a synergistic optimization strategy of "modification combined with calcium ion regulation" was proposed. Results revealed that alkali treatment strengthened ionic interactions while weakening hydrogen bonds and hydrophobic interactions, promoting protein molecular rearrangement and resulting in a narrower and more concentrated particle-size distribution. This increased the initial storage modulus to 136 Pa, comparable to that of EP. TGase treatment catalyzed protein-protein and protein-polysaccharide covalent cross-linking, forming a dense network structure and significantly increasing gel hardness to approximately 1.5 times that of EP. Furthermore, the addition of calcium ions synergistically enhanced gel strength via salt bridge formation, further elevating the initial storage modulus to 297 Pa. However, a high calcium concentration (25 mM) led to an approximately 20% reduction in water-holding capacity for TGase-treated PCPE gels. This study elucidates the multidimensional regulatory mechanisms underlying enhanced plant-protein gelation and provides a strategy for developing sustainable plant-based gelled foods.
Hao Chen, Qun Gao, Ruoyu Wu et al.· International Journal of Bio...· 0 citations
Myofibrillar protein (MP) gels with desirable textural properties are highly favored by customers. In the present study, the effects of different charged polysaccharides, including neutral dextran (DX), anionic κ-carrageenan (KC) and cationic chitosan (CS), on modulating the thermal gelation properties of microbial transglutaminase (MTGase)-mediated MP were investigated. The results suggested that the thermal gelation characteristics of composite gel systems formed by combining MTGase with three polysaccharides respectively were improved, regardless of polysaccharide ion types. Furthermore, cationic CS was the most effective in increasing water-holding capacity (WHC), texture properties, and viscoelastic characteristics of composite gels, followed by neutral DX and then anionic KC. Based on the results of water state and distribution, the incorporation of three polysaccharides strengthened the water entrapment effect of MTGase-mediated MP gel network. Additionally, cationic CS displayed the greatest effect on driving the generation of β-sheet structures, facilitating the formation of disulfide bonds and enhancing hydrophobic interactions, thereby contributing to the formation of a uniform and well-organized gel matrix network. These findings provide theoretical support for formula optimization and quality improvement of meat products by modulating MP during thermal processing.
Xiaomin Zhang, Shuxia Wu, Cheng Tang et al.· International Journal of Bio...· 0 citations
The reconstituted soybean protein isolate (SPI) was constructed by adjusting the ratios of its main components, namely lipophilic protein (LP), glycinin (11S), and β-conglycinin (7S). The effects of different LP/11S/7S ratios on stability and delivery function of transglutaminase-induced emulsion gel were investigated. The reconstituted SPI with a high proportion of LP had lower particle size, higher surface charge and excellent interface affinity, which helped to strengthen microstructure of emulsion gel. The reconstituted SPI emulsion gels exhibited higher viscoelasticity and water holding capacity, and the freeze-thaw, thermal and pH stability were enhanced. Furthermore, reconstituted SPI emulsion gels increased encapsulation efficiency of quercetin to 92.2%, which facilitated its chemical stability and promoted bioaccessibility to 61.78%. Therefore, reconstituted SPI emulsion gel can be improved by regulating ratios of LP, 7S and 11S, thus promoting quercetin delivery, which provides a theoretical basis for construction and application of stable SPI-based emulsion gel carriers.
Jiannan Yan, Fangxiao Xing, Pan Liu et al.· Food Chemistry· 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
Soy protein isolate (SPI) is widely used as a plant protein ingredient. This study modified SPI by ultrasound-assisted laccase treatment (U + La; 150, 300, 450, and 600 W), evaluated its functional properties, and further analyzed the related physicochemical and structural changes. SPI treated with 300 W ultrasound and laccase (UL3) showed the best overall functionality, with the highest water-holding capacity (93.39%), emulsion stability index (42.60 ± 2.24 min), and foaming capacity (169.29%). UL3 also showed a relatively small particle size (362.80 nm) and the highest absolute zeta potential (27.78 mV). Electrophoretic and chromatographic analyses indicated increased high-molecular-weight aggregates after U + La treatment. Spectroscopic and microstructural results suggested that moderate U + La treatment was associated with SPI conformational changes and a compact gel network. Overall, UL3 improved SPI model functionality and showed application potential as a modified plant protein ingredient.
Jiaxin Guo, Qinggang Xie, Yilin Sun et al.· Food Research International· 1 citation
Structural and functional modifications of common bean (Phaseolus vulgaris L.) protein were investigated using cold atmospheric plasma (CAP) and Maillard reaction (MR) with pectin. CAP treatment (20 kV, 1–5 min) significantly enhanced protein solubility and emulsifying activity. Conversely, MR (90 °C, 0.5–3 h) reduced solubility and foaming properties but improved gelling capacity, achieving the lowest gelation concentration (LGC) at 2–3 h of heating. Conformational shifts in secondary structures (α-helix, β-turn, and β-sheet) were confirmed by FTIR and correlated with protein unfolding and structural modifications, as characterized by SDS-PAGE. Zeta potential measurements indicated that CAP improved colloidal stability, whereas extended MR heating decreased stability. These findings demonstrate that CAP is an effective nonthermal tool for enhancing protein functionality, while MR is better suited for developing stable gel-based food matrices, lowering the LGC from 8% to 5%.
Rukiye Gundogan, T. Dissanayake, A. C. Karaça et al.· ACS Food Science & Techn...· 0 citations
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