Search Results (255)

Freshwater surimi typically exhibits poor gel-forming capability and is prone to gel deterioration, limiting its applications in food products. This study successfully prepared silver carp surimi gels with improved gel strength and water-holding capacity (WHC) using carboxymethyl konjac glucomannan (CKGM) as a functional modifier. Furthermore, the regulatory mechanism of CKGM with different degrees of substitution (DS) on the gel properties of silver carp surimi was systematically investigated. Results demonstrated that DS significantly influenced gel strength, WHC, and microstructure. CKGM (DS = 0.21%) substantially enhanced the gel strength and WHC through strengthened hydrophobic interactions and hydrogen-bond networks. However, CKGM with a higher DS (0.41%) induced a steric hindrance effect, decreasing elastic modulus and WHC and resulting in a more porous gel network. Raman spectroscopy analysis revealed that CKGM facilitated the conformational transition of myofibrillar proteins from α-helix to β-sheet, thereby improving the density of the gel network. The study provides theoretical foundations and technical guidance for the quality improvement of surimi products. Full article

Surimi products are popular due to their high protein and low fat content. However, traditional processing methods rely on high concentrations of salt (2–3%) to maintain texture and stability, contributing to excessive sodium intake. As global health trends advance, developing green and low-salt technologies while maintaining product quality has become a research focus. Alkaline amino acids regulate protein conformation and intermolecular interactions through charge shielding, hydrogen bond topology, metal chelation, and hydration to compensate for the defects of solubility, gelation, and emulsification stability in the low-salt system. This article systematically reviews the mechanisms and applications of alkaline amino acids in reducing salt and maintaining quality in surimi. Research indicates that alkaline amino acids regulate the conformational changes of myofibrillar proteins through electrostatic shielding, hydrogen bond topology construction, and metal chelation, significantly improving gel strength, water retention, and emulsion stability in low-salt systems, with the results comparable to those in high-salt systems. Future research should optimize addition strategies using computational simulations technologies and establish a quality and safety evaluation system to promote industrial application. This review provides a theoretical basis for the green processing and functional enhancement of surimi products, which could have significant academic and industrial value. Full article

This study investigated quality changes in seaweed–yak patties before and after freeze–thaw by varying seaweed addition levels (10–70%). Macroscopically, the effects on water-holding capacity, textural properties, and oxidative indices of restructured yak patties were evaluated. Microscopically, the impact of seaweed-derived bioactive ingredients on patty microstructure and myofibrillar protein characteristics was examined. LF-NMR and MRI showed that 40% seaweed addition most effectively restricted water migration, reduced thawing loss, and preserved immobilized water content. Texture profile analysis (TPA) revealed that moderate seaweed levels (30–40%) enhanced springiness and minimized post-thaw hardness increases. SEM confirmed that algal polysaccharides formed a denser protective network around the muscle fibers. Lipid oxidation (MDA), free-radical measurements, and non-targeted metabolomics revealed a significant reduction in oxidative damage at 40% seaweed addition, correlating with increased total phenolic content. Protein analyses (particle size, zeta potential, hydrophobicity, and SDS-PAGE) demonstrated a cryoprotective effect of seaweed on myofibrillar proteins, reducing aggregation and denaturation. These findings suggest that approximately 40% seaweed addition can improve the physicochemical stability and antioxidant capacity of frozen seaweed–yak meat products. This work thus identifies the optimal seaweed addition level for enhancing freeze–thaw stability and functional quality, offering practical guidance for the development of healthier, high-value restructured meat products. Full article

The effects of octenyl succinic anhydride-modified hydrophobic starch (OSA starch) on the properties of myofibrillar protein (MP) emulsions were investigated. The results show that the stability of protein emulsions was significantly enhanced with the addition of OSA starch (0.25–1.0%), with the most pronounced effect observed at a 1% concentration. Concomitantly, increasing OSA starch concentrations led to a reduction in the fat globule size. Electrostatic interactions between anionic groups in the modified starch and myofibrillar proteins were observed, which effectively decreased the zeta potential of the emulsion to a minimum of −52.3 mV. However, in the composite emulsion system, a competitive relationship between OSA starch and myofibrillar proteins was evident, as reflected by the decrease in interfacial protein content from 1.16 mg/mL in the control (CK) group to 0.78 mg/mL in the OSA starch-treated group. Despite this competition, the overall emulsion stability was improved due to the synergistic effects of the modified starch and proteins. These findings suggest that OSA-modified starch holds promise as a stabilizer for enhancing the stability of myofibrillar protein emulsions. Full article

This study investigated the synergistic effects of ultra-high pressure (UHP) and egg white protein (EWP) on the gel properties of sodium-reduced shrimp surimi. A Box–Behnken design targeting UHP pressure (200–400 MPa), duration (10–20 min), and EWP/myofibrillar protein (MP) ratio (1:9–5:5) was implemented to optimize gel strength, water holding capacity (WHC), and whiteness. Optimal conditions (290 MPa/15 min/EWP:MP = 3:5) yielded the following validated improvements, versus conventional processing: 282.27 g·mm gel strength, 14.90% WHC enhancement, and 16.63% reduced cooking loss. Texture profile analysis demonstrated superior elasticity in composite gels. Magnetic resonance imaging and scanning electron microscopy revealed a denser microstructure with enhanced water-binding capacity, corroborated by the rheological evidence of strengthened viscoelasticity. UHP promotes the partial expansion of MP, exposing hydrophobic groups and sulfhydryl groups, thereby enhancing intermolecular interactions. It also promotes the expansion of EWP, enabling the formation of disulfide bonds between molecules and facilitating the formation of network structures. These findings propose a scalable strategy for developing clean-label salt-reduced aquatic surimi products. Full article

This study explores the potential of lysine (Lys) and tilapia myofibrillar protein (MP) composite particles in the formulation of highly inwardly directed emulsions (HIPEs). Infrared spectroscopy, potentiometric analysis, and molecular docking studies revealed that the interaction between Lys and MP is primarily governed by hydrogen bonding and electrostatic forces. The incorporation of Lys significantly influenced the particle size, secondary and tertiary structures, solubility, and turbidity of MP. Lys-MP-stabilized HIPEs can form highly stable denser self-supporting gel network structures. Rheological analysis of HIPEs stabilized by MP showed a low energy storage modulus (G’ 110.66 Pa) and water–oil separation, therefore preventing 3D printing. However, HIPEs stabilized by Lys (especially 1.5 wt%) significantly improved the energy storage modulus (G’ 1002.10 Pa), increased viscoelasticity and thixotropic recovery, and reduced droplet size (10.84 μm), facilitating the use of HIPE inks for 3D printing. Furthermore, HIPEs stabilized with 1.5 wt% Lys-MP demonstrated superior print accuracy (91.36%), resolution, and clarity in 3D printing applications. Overall, these findings offer a promising strategy for developing Lys-MP composite particle-stabilized HIPEs tailored for advanced 3D printing technologies. Full article

To investigate the interaction effects of resting times (0, 6, and 12 h) and NaHCO₃ concentrations (0, 2, 4, and 6 g/kg) on chicken myofibrillar protein (CMP), this study analyzed the changes in solubility, active sulfhydryl groups, rheological behavior, fluorescence, and gel properties of CMP solutions (60 mg/mL). The results indicated that pH significantly increased with higher NaHCO₃ concentrations and longer resting times. Consequently, solubility, active sulfhydryl groups, apparent viscosity, shear stress, G’ value at 80 °C, hardness, springiness, and cohesiveness all significantly increased, while particle size, turbidity, and whiteness significantly decreased. However, these trends were not observed in samples treated with an amount of 6 g/kg NaHCO₃ and/or a resting time of 12 h. The findings suggest that treatment with 4 g/kg NaHCO₃ and a resting time of 6 h effectively reduced protein aggregation and enhanced solubility. Conversely, excessive NaHCO₃ or prolonged resting times resulted in decreased protein solubility and deteriorated textural properties. Full article

Freezing has been widely used to preserve the freshness and quality of crayfish (Procambarus clarkii). However, temperature fluctuations during transportation and storage inevitably affect the quality attributes of crayfish. In this study, the effect of liquid nitrogen freezing (LNF) on crayfish myofibrillar protein (MP) was investigated under freeze–thaw (FT) cycles. The small ice crystals formed by LNF could reduce the conversion of sulfhydryl groups to disulfide bonds, preventing the exposure of hydrophobic groups, thereby maintaining the functional properties of MP. LNF could prevent the degradation and oxidation of MP and maintain its compact and smooth microstructure. Compared to refrigerator freezing (RF), LNF showed a stronger protective effect on the secondary and tertiary structures of MP, alleviating their conformational changes. Therefore, LNF could be an alternative freezing method to preserve crayfish quality against FT cycles during transportation and storage. Full article

Rhodotorula mucilaginosa plays a key role in developing the taste of dry-cured ham, while the mechanism of Rhodotorula mucilaginosa proteases on myofibrillar protein (MP) hydrolysis and the evolution of taste substances has not been studied. The enzymatic characteristics, hydrolysis capacities for MPs, free amino acid contents, metabolite compositions, and taste attributes were investigated during the interactions of MPs and proteases. The proteases of R. mucilaginosa EIODSF019 (RE) and R. mucilaginosa XZY63-3 (RX) showed high hydrolytic activities at the conditions of pH 5.0~7.0 and 30~40 °C. Compared with RX, RE showed a lower Michaelis constant (Km) value and a better affinity for protein substrates. RE showed a higher capability to degrade myosin and actin compared with RX and P. kudriavzevii XS-5 proteases (PK). The microtopography of enzyme-treated MPs in RE presented a smoother surface and lower root mean square roughness than that in RX and PK. The total content of free amino acids significantly increased from 0.34 mg/100 mL of CK to 17.10 mg/100 mL of RE after 4 h of hydrolysis of MPs. Sixty-two metabolites were identified by LC-MS/MS, and γ-glutamyl peptides were the main components of MP hydrolysates. Sensory scores of umami, richness, and aftertaste showed the largest values in RE among these groups. Partial least squares discriminant analysis and correlation network demonstrated that γ-Glu-Lys, γ-Glu-Tyr, γ-Glu-Glu, γ-Glu-His, γ-Glu-Leu, γ-Glu-Cys, γ-Glu-Ala, and γ-Glu-Gln were positively correlated with the improvements of umami, richness, and aftertaste in RE. Full article

Health benefits associated with hyaluronic acid, along with its properties such as water-binding capacity and antimicrobial activity, suggest that incorporating it into meat systems could provide a basis for formulating functional meat products. This study aimed to evaluate the properties of myofibrillar protein gels and emulsions with varying concentrations of hyaluronic acid. The results indicate that increasing the hyaluronic acid concentration (0.008% to 0.04%) does not significantly affect the cooking loss, while a concentration of 0.08% enhances cooking loss. This, in turn, increased gel hardness, while the water-holding capacity remains unaffected. Cryo-scanning electron microscopy (Cryo-SEM) images revealed a partial disruption of the gel structure, with rising hyaluronic concentrations. In pork myofibrillar protein emulsions, smaller droplets and higher stability were observed after HA incorporation. Samples containing hyaluronic acid were more viscous and exhibited shear-thinning properties. Overall, the hyaluronic acid used in this study improved emulsion properties, whereas the gel structure was compromised. Full article

Surimi gel, a type of hydrocolloidal food, is formed through the gelation of fish meat proteins. Myosin heavy chain (MHC), a key myofibrillar protein, plays a crucial role in the formation of the gel network via both transglutaminase (TGase)-catalyzed and non-enzymatic polymerization. Gel disintegration in surimi is primarily attributed to the proteolytic degradation of MHC. This study focused on golden threadfin bream Nemipterus virgatus, a species characterized by low TGase activity and high protease activity at elevated temperatures. We investigated the competition between non-enzymatic polymerization and proteolytic degradation of MHC and their effects on gel mechanical properties using a mathematical model. A mathematical model based on kinetic reactions accurately reflected the changes in MHC observed through SDS-PAGE analysis during N. virgatus gel disintegration. Our results indicate that not only unpolymerized but also polymerized MHC was significantly degraded, which substantially contributed to the reduction in the mechanical properties of the N. virgatus surimi. Mathematically understanding the dynamics of MHC in surimi during heating helps promote the utilization of noncommercial fish species for surimi processing by enabling better control over surimi gel properties. Full article

This study investigated the effect of the water content of large yellow croaker fillets on their quality characteristics after roasting. The large yellow croaker fillets were randomly divided into groups, namely, the fresh group (BMC-77), the 3% salt-cured group (BMC-70), and groups cured with 3% salt followed by hot air drying to obtain different moisture contents (BMC-65, BMC-60, and BMC-55). Then, the fillets were roasted at 220 °C for 20 min. There were four replicates for each group. Various indicators, including color, texture, thiobarbituric acid-reactive substance (TBARS) content, total volatile basic nitrogen (TVB-N) content, water distribution, volatile components, and myofibrillar proteins were determined, and a sensory evaluation was carried out. The results showed that as the water content decreased, the lightness (L*) of the roasted fillets significantly decreased (p < 0.05), while the redness (a*) and yellowness (b*) increased. The hardness, shear force, TBARS, and TVB-N values all increased significantly (p < 0.05). The proportion of immobile water decreased, while the proportions of tightly bound water, free water, and loosely bound water increased. The electronic nose, electronic tongue, and GC-MS analyses revealed that there were significant differences in odor, taste, and volatile components among fillets with different water contents. A comprehensive analysis of all the indicators demonstrated that the fillets with an initial water content of 65% (BMC-65) achieved the best sensory qualities after roasting in terms of taste and flavor. An appropriate reduction in the initial water content helped to improve the texture and appearance of the fillets while delaying the degradation of proteins and lipids. This study provides a theoretical foundation for optimizing the roasting process of large yellow croaker fillets. Future research could explore the synergistic effects of the roasting conditions and water content to achieve more accurate quality control. Full article

The enhancement of gel properties in chicken myofibrillar proteins (MPs) is a crucial objective in meat processing. In this experiment, we systematically investigated the effects of lentinan (LNT) on MP gel formation ability and three-dimensional network structure features through multi-scale structural characterization and molecular interactions analysis and elucidated the molecular pathways of their molecular actions in regulating gel properties. The addition of LNT (0–2%, w/v) significantly enhanced the water-holding capacity (WHC), textural, and rheological properties of LNT-MPs. As the concentration of LNT increased, the hydrophobic and electrostatic interactions became more pronounced. Conversely, the contribution from disulfide bonds exhibited an inverse relationship, with hydrogen bonds demonstrating the least impact. Subsequently, the α-helix content decreased from 23.75% to 22.64%, and the β-fold content increased from 28.03% to 29.22%, suggesting that the protein aggregates reorganized to form larger aggregates, which contributed to forming a more stable network structure of gels. This investigation establishes LNT’s capacity to modify the gelation mechanisms of MPs. These outcomes offer crucial insights for implementing fungal polysaccharides in processed meat product development. Full article

Foodborne pathogens remain a significant global challenge, contributing to widespread illness and considerable food losses. This study investigates the effects of electron-beam irradiation on beef quality and safety using a pulsed high-frequency linear accelerator (ILU-10). Meat samples were subjected to irradiation at doses of 3, 6, and 9 kGy, with non-irradiated samples serving as controls. The research focused on evaluating microbial reduction, alterations in textural properties, and changes in nutritional components including amino acids, vitamins, and mineral content. Microbiological analysis demonstrated a dose-dependent reduction in total viable counts, with a decrease from 300 CFU/g in controls to 100 CFU/g at 3 and 6 kGy and complete microbial inactivation at 9 kGy. Scanning electron microscopy revealed disruption in myofibrillar structure, with increased interstitial spacing. Chemical analyses indicated a dose-dependent decline in total amino acid content and variable responses among individual amino acids, suggesting irradiation-induced protein fragmentation and oxidation. The findings suggest that, when optimized, irradiation can substantially improve meat safety while maintaining acceptable nutritional and sensory quality. Full article

The effect of oil incorporation (soybean oil [SO] and coconut oil [CO] at 0, 1, 3, and 5 g/100 g) on the rheological, structural, and 3D printing properties of fish myofibrillar protein (MP, also known as surimi) paste and gel was investigated. Small-amplitude oscillatory shear (SAOS) tests showed that increasing oil concentration reduced the storage modulus (G′), weakening the gel network. Large-amplitude oscillatory shear (LAOS) analysis revealed strain-stiffening shifts and nonlinearity at γ = 5%. CO-containing gels exhibited higher hardness and gumminess, particularly at lower concentrations, due to enhanced protein–lipid interactions. In contrast, SO-containing gels showed reduced strength at higher concentrations, indicating phase separation. SEM confirmed that CO promoted a denser network, while SO led to a more porous structure, especially at 5% oil. Three-dimensional printing analysis demonstrated that both oils improved extrusion flowability by reducing nozzle friction. However, CO-containing samples maintained post-extrusion stability at 85% moisture, whereas SO-containing samples collapsed after multiple layers due to excessive softening. These findings highlight oil’s dual role in MP gels, enhancing lubrication and flowability while compromising rigidity. The results offer valuable insights for developing soft, texture-controlled foods using 3D printing, especially for personalized nutrition applications such as elderly care or dysphagia-friendly diets. Full article