BACKGROUND: Future applications of high-internal-phase emulsions (HIPEs) are highly regarded, but poor freeze-thaw stability limits their utilization in frozen products. This study aimed to characterize the structure of chickpea protein microgel particles (HCPI) induced by NaCl and to assess its impact on the freeze-thaw stability of HIPEs.
RESULTS: The results showed that NaCl induction (0-400 mmol L-1) increased the surface hydrophobicity (175.9-278.9) and interfacial adsorbed protein content (84.9%-91.3%) of HCPI. HIPEs prepared with HCPI induced by high concentration of NaCl exhibited superior flocculation index and centrifugal stability, and their freeze-thaw stability was better than that of natural chickpea protein. The increase in NaCl concentration reduced the droplet aggregation and coalescence index of the freeze-thaw emulsions, diminishing the precipitation of oil from the emulsion. Linear and nonlinear rheology showed that the strengthened gel structure (higher G\' values) restricted water flow and counteracted the damage to the interfacial film by ice crystals at 100-400 mmol L-1 NaCl, thus improving the viscoelasticity of the freeze-thaw emulsions. Finally, the thawing loss of surimi gel with HCPI-200 HIPE was reduced by 2.04% compared to directly adding oil.
CONCLUSIONS: This study provided a promising strategy to improve the freeze-thaw stability of HIPEs and reduce the thawing loss of frozen products. © 2024 Society of Chemical Industry.

Myofibrillar protein (MP) gels are susceptible to oxidation, which can be prevented by complexing with hydrophilic polyphenols, but may cause gel deterioration. Sodium metabisulfite (Na2S2O5) has been used to induce self-assembly of MP and analyze the impact of self-assembly on the quality of composite gels containing high amounts of (-)-epigallocatechin gallate (EGCG). Hydrophobic forces were confirmed as the main driver of self-assembly. Self-assembly reduced the size of the MP-EGCG complex to approximately 670 nm and increased the gel\'s hydrophobic force by approximately 3.6-fold. The maximum hardness of the Na2S2O5-treated MP-EGCG composite gel was 52.43 g/kg, which was approximately 49% greater than pure MP gel. After oxidative treatment, the Na2S2O5-treated MP-EGCG composite gel had considerably lower carbonyl and dityrosine levels (2.47-μmol/g protein and 450 a.u.) than the control (8.37-μmol/g protein and 964 a.u.). Therefore, Na2S2O5 shows potential as a cost-effective additive for alleviating MP limitations in the food industry.

κ-Carrageenan (CG) was employed to mask the bitterness induced by 50% KCl in surimi gels to achieve salt reduction and gel performance improvement. The combination of KCl and CG (KCl + CG) yielded the increased textural characteristics and water-holding capacity (WHC) of surimi gels and facilitated the transition of free water to immobilized water. In addition, the KCl + CG supplement increased the turbidity and particle size of myofibrillar protein (MP) sols but decreased the surface hydrophobicity in a dose-dependent manner. The hydrophobic interactions and disulfide bonds played crucial roles in maintaining the stability of MP gels. The specific binding of potassium ions to the sulfate groups of CG limited the release and diffusion of potassium ions from the surimi gels during oral processing, effectively masking the bitterness perception and maintaining the saltiness perception. This study provides a promising strategy to reduce the utilization of sodium salt in surimi products.

The gel prepared using Nemipterus virgatus (N. virgatus) surimi alone still has some defects in texture and taste. Complexing with polysaccharides is an efficient strategy to enhance its gel properties. The main objective of this study was to analyze the relationship between the gel quality and molecular interaction of N. virgatus surimi gel after complexing with tapioca starch. The results make clear that the gel strength, hardness, and chewiness of surimi gel were increased by molecular interaction with tapioca starch. At the appropriate addition amount (12%, w/w), the surimi gel had an excellent gel strength (17.48 N), water-holding capacity (WHC) (89.01%), lower cooking loss rate (CLR) (0.95%), and shortened T2 relaxation time. Microstructure analysis indicated that the addition of tapioca starch facilitated even distribution in the gel network structure, resulting in a significant reduction in cavity diameter, with the minimum diameter reduced to 20.33 μm. In addition, tapioca starch enhanced the hydrogen bonding and hydrophobic interaction in the gel system and promoted the transformation of α-helix to β-sheet (p < 0.05). Correlation analysis showed that the increased physicochemical properties of surimi gel were closely related to the enhanced noncovalent interactions. In conclusion, noncovalent complexation with tapioca starch is an efficient strategy to enhance the quality of surimi gel.

The effect of soybean oil (SO) on freeze-thaw (F-T)-treated surimi was investigated and its related mechanism was revealed by molecular dynamics (MD) simulations. The results displayed that SO has a disrupting effect on the structure of fresh samples. However, in the F-T-treated samples, surimi gels supplemented with SO had a more uniform microstructure. Simultaneously, when SO was added from 0% to 7% in the F-T-treated samples, the gel strength increased from 46.66 to 51.86 N · mm $$ 46.66\\ \\mathrm{to}\\ 51.86\\;\\mathrm{N}\\cdotp \\mathrm{mm} $$ (p < .05), the physically bound water was increased from 92.90% to 94.15% (p < .05), and storage modulus was increased from 5939 to 6523 Pa. Triglycerides of SO generated hydrophobic interactions with myosin mainly in carbon chains. Computational results from MD simulations illustrated that the structure of myosin combined with triglycerides was more stable than that of myosin alone during temperature fluctuations (-20 to 4°C). During ice crystal growth, triglycerides absorbed on the myosin surface inhibited the growth of surrounding ice crystals and mitigated the ice crystal growth rate (from 7.54 to 5.99 cm/s). The addition of SO during the F-T treatments allowed myosin to be less negatively affected by ice crystal formation and temperature fluctuations and ultimately contributed to the formation of a more uniform network gel structure.

Grass carp (Ctenopharyngodon idella) are used as raw material for conventional surimi products in Southern China. However, endogenous serine proteases deteriorated the texture of the surimi gel. To unlock the mechanism behind, the present study isolated the crude myofibril-bound serine protease (cMBSP) in grass carp and studied its effects on surimi gel. The cMBSP activity was the highest at 40 °C and pH 8.0, and it remained stable at 20-55 °C neutral pH. Additionally, it was susceptible to serine protease inhibitors and high concentrations of Na+. The maximum degradation of myosin heavy chain by cMBSP was observed at 50 °C. Protein unc-45 homolog B (a myosin chaperone) is one of the apparent degradation products according to mass spectrometry. The cMBSP caused lower water holding capacity and deteriorated texture in the surimi gel. This study expanded insights about the mechanism of surimi gel degradation by cMBSP, which provided theoretical basis for enhancing surimi quality.

BACKGROUND: The present study aimed to investigate the effects of large yellow croaker roe phospholipids (LYCRPLs) on the physical properties of surimi gels and to clarify their interaction mechanism with myofibrillar proteins (MPs) in terms of chemical forces and the spatial conformation.
RESULTS: LYCRPLs could improve the gel strength, textural properties, rheological properties and water-holding capacity of surimi gels. Moreover, the interaction mechanism between LYCRPLs with MPs was revealed through intermolecular forces, Fourier transform infrared spectroscopy and ultraviolet visible absorption spectroscopy. The findings demonstrated that LYCRPLs enhanced the surface hydrophobicity and particle size of MPs, facilitating expansion and cross-linking of MPs.
CONCLUSIONS: These results provide a theoretical basis for improving the characteristics of surimi gels and thus facilitate the application of LYCRPLs in the aquatic food industry. © 2023 Society of Chemical Industry.

BACKGROUND: Adding appropriate exogenous substances is an effective means to improve the quality of freshwater fish surimi. The present study investigated the effects of chicken breast on the gel properties of mixed minced meat products.
RESULTS: With the increase in the proportion of chicken breast, the breaking force of mixed gels gradually increased. When the addition ratio was 30:70, the gel strength of mixed gels had the highest strength of 759.00 g cm-1 and also the highest water holding capacity of 87.36%. Compared with surimi gels (0:100), the hardness, adhesiveness and chewiness of mixed gels were significantly improved. The increase in the proportion of chicken breast increased the thermal stability of the mixed sol and improved the rheological properties of the mixed sol. When the proportion was 40:60, the area of immobile water (A22 ) in the mixed gel increased significantly, and the highest A22 was 3463.24. The hydrophobic interactions and disulfide bonds in the mixed gel were significantly increased as a result of the addition of chicken breast. The results of microstructure, electrophoresis and Raman spectroscopy indicated that the addition of chicken breast promoted the cross-linking of the proteins in mixed gels, which facilitated the transformation of the protein secondary structure from α-helical to β-folded structure, thus forming a more uniform and orderly network structure.
CONCLUSIONS: These results suggest that improving the gel properties of silver carp surimi by use of chicken breast has practical implications for the development of new blended products for surimi processing. © 2023 Society of Chemical Industry.

This work investigated the effects of liquid nitrogen immersion freezing (LNF), -35 °C air freezing (AF-35℃) and -18 °C air freezing (AF-18℃) on the physical and chemical characteristics and flavor quality of surimi gels with different cross-linking degrees. Compared to AF-35 °C and AF-18 °C, LNF was shown to considerably delay the texture deterioration and water migration of frozen gels, as well as the accumulation of thiobarbituric acid reactive substance values and carbonyl contents. Additionally, an appropriate increase of cross-linking degree (45.83 to 62.99%) was found able to improve gel properties and inhibit quality deterioration during freezing. Moreover, LNF-treated gels were closer to fresh gels in the amount of volatile compounds, in contrast to most significant negative aroma changes in AF-18℃-treated gels. Furthermore, 29, 29 and 31 key differential volatile compounds were screened for gels with a cross-linking degree of 29.66, 45.83 and 62.99%, respectively, mainly including aldehydes, alcohols and esters.

This study investigated the cryoprotective mechanism of ultrafiltration membrane-separated fractions (>10 kDa, UF-1; 3-10 kDa, UF-2; and <3 kDa, UF-3) derived from silver carp hydrolysates on frozen surimi. The surimi gel incorporating UF-3 exhibited a compact, continuous structure with uniform pores, even after undergoing six freeze-thaw (F-T) cycle, with the minimal reduction in entrapped water (from 95.1 % to 91.1 %) and least increase in free water (from 4.5 % to 6.6 %) as revealed by SEM and LF-NMR analysis. Through molecular docking analysis, three major peptides in UF-3 were identified to form robust interactions with the myosin head pocket, facilitated by hydrogen bonds, electrostatic forces, and hydrophobic interactions. Furthermore, molecular dynamics simulations demonstrated that the three peptides effectively prevented myosin from unfolding and aggregating by tightly binding to basic amino acids (Arg, Lys) and hydrophobic amino acids (Phe, Leu, Ile, Met, and Val) residues in the myosin head pocket, primarily governed by electrostatic energies (-156.95, -321.38, and -267.53 kcal/mol, respectively) and van der Waals energies (-395.05, -347.46, and -319.16 kcal/mol, respectively). Notably, the key action site was identified as Lys599 on myosin. The hydrophilic and hydrophobic hotspot residues of the peptides worked synergistically to stabilize the myosin structure in frozen surimi.