Although the inferior protein bioavailability of purely plant-based meat alternatives relative to animal-derived meats is well-established, the digestion and absorption characteristics of hybrid animal-plant protein products formulated through partial substitution remain poorly characterized. To address this, the hybrid surimi/plant protein (HSP) gels crosslinked by transglutaminase (TGase) with uniform gel strength were prepared by modulating TG dosage (wheat: 18 U/100 g surimi; soybean and rice: 9 U/100 g; pea: 6 U/100 g). In vitro gastrointestinal digestion revealed no significant differences (P > 0.05) in protein or dry matter digestibility (61.50%-69.15%) across groups. However, the legume-based composites (soybean and pea) exhibited significantly higher digestion rate constants (k = 0.029 min⁻¹) than cereal-based composites (k = 0.024 min⁻¹), alongside reduced half-digestion times (t_0.5 = 163.3 min vs. 170.9 min), indicating enhanced digestibility. Particle size distribution analysis showed a significant reduction (P < 0.05) in pea protein gel particle size after pepsin digestion, whereas wheat protein gels retained larger residual particles (D₅₀ = 27.48 μm) post-pancreatin digestion, suggesting greater hydrolytic resistance. Electrophoresis confirmed digestion products were predominantly <20 kDa fragments. Notably, pea protein digests exhibited potent antioxidant activity, strongly correlated with six high-abundance antioxidant peptides identified by mass spectrometry: TLEDQLSEIK, VLNAGVIPEGQF, DAGDGVTHNVPVYEG, VGLLHSQNTSL, LASLYPAVVEDTTK, and LLVVPQNF. Collectively, partial plant protein substitution conferred favorable protein digestibility and nutrient acquisition potential to hybrid surimi gels, with pea protein emerging as particularly valuable for enhancing nutritional functionality in meat-reduced formulations.

In order to rapidly and accurately predict the shelf life of river crab sauce, prepared from river crab processing waste, during storage at 25 ℃, river crab sauce was stored at 37, 45 or 55 ℃ to accelerate its quality deterioration. A first-order kinetic model was established with total volatile basic nitrogen (TVB-N) as the dependent variable. The predicted value of shelf life was determined by the kinetic model and the Arrhenius equation. The results showed that the activation energy (E_a) and pre-exponential factor (k₀) obtained from the Arrhenius equation were 29.28 kJ/mol and 1.443 × 10³, respectively, and the shelf life of river crab sauce at 25 ℃ was calculated to be 183 days.

The effects of adding different amounts (0.1%, 0.2%, 0.3%, 0.4% and 0.5%) of psyllium husk powder (PHP), gellan gum (GG) or konjac glucomannan (KGM) on the properties of phosphorylated surimi-crab meat mixed gels (MG) were investigated. The gel properties were improved by adding a small amount (0.1%) of PHP or GG. With increasing addition level of hydrophilic colloids, phase separation occurred, so that the gel properties did not significantly change and even began to decrease. However, the addition of KGM had no significant effect on the breaking force or gel strength, and no phase separation was observed under laser scanning confocal microscopy (LSCM). The addition of PHP and GG increased the temperature at which G’ began to decrease, which was beneficial to the improvement of gel properties. The denaturation of myosin required higher temperature and less energy in the phosphorylated MG system with hydrophilic colloids, and temperature may become a major influential factor in the denaturation process. The overall structural stability of proteins in MG was enhanced by adding a small amount of PHP or KGM. However, PHP and GG had a destructive effect on actin. On the contrary, the addition of a small amount of KGM could increase the structural stability of actin, which may be unfavorable for the formation of gels. The interaction between myosin and actin in the MG system was conducive to enhancing the overall structural stability of proteins. The three hydrophilic colloids, especially GG, at an addition level of 0.1% was beneficial to the improvement of gel properties. The incorporation of hydrophilic colloids may be a novel strategy to improve the quality of phosphorylated MG.

This study investigated the effects of adding different levels of tetrasodium pyrophosphate (TSPP), sodium tripolyphosphate (STPP) or sodium hexametaphosphate (SHMP) on the structural and functional properties of myofibrillar proteins from silver carp in a low-salt (1 g/100 mL NaCl) environment. The results indicated that under low-salt conditions, the solubility, surface hydrophobicity, and emulsification properties of increased with increasing addition of phosphate. All three phosphates introduced phosphate groups into myofibrillar proteins. The pyrolysis rate of myofibrillar proteins was reduced by the addition of 0.2–0.5 g/100 mL STPP, indicating improved thermal stability. The protein was most significantly phosphorylated by the addition of 0.4 g/100 mL STPP, resulting in binding of a large number of phosphate groups to the protein. TSPP and STPP led to protein aggregation, while proteins phosphorylated by SHMP were more stable. In conclusion, the addition of 0.4 g/100 mL STPP improved the functional properties of myofibrillar proteins to a greater extent under low-salt conditions.

In order to study the effect of freezing methods on the quality of crayfish, changes in the properties and structure of crayfish myofibrillar proteins (MPs) after air freezing (AF), immersion freezing (IF), static magnetic field-assisted immersion freezing (SMF), and liquid nitrogen freezing (LNF) were examined. Compared with AF, IF and LNF could enhance the absolute value of the zeta potential of crayfish MPs to different degrees, inhibit the decrease of total sulfhydryl content, and maintain the structural characteristics of the proteins enhancing their stability. SMF improved the stability of MPs more significantly than any other freezing treatment (P < 0.05), as evidenced by lower turbidity and particle size, higher absolute zeta potential and total sulfhydryl content, better maintained structural features, lower surface hydrophobicity, and greater retention of the myosin heavy chains. In conclusion, the quality of frozen crayfish is affected by different freezing media, and SMF can better stabilize the functional properties of crayfish MPs.

The tropomyosin (TM) fractions of crab proteins may cause allergic reactions in individuals susceptible to allergies; however, efficient and safe methods by which to reduce such allergenicity are not currently available. Therefore, in this study, the effects of three different processing methods, i.e., microwave, ultrasound, and high temperature-pressure (HTP) treatments, on the digestion stability of TM from Chinese mitten crab muscle and the allergenicity of TM digestion products were explored. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed that microwaving had little effect on the digestion stability of TM. In contrast, ultrasound and HTP treatments facilitated the degradation of TM. Similarly, Western blotting and inhibition ELISA indicated that the IgE-binding activity of TM was significantly reduced after treatment with ultrasound or HTP. Among the three different processing methods, HTP was the most effective method for improving digestibility of TM and reducing immunoreactivity. This finding provides new insights into treatments for crab allergies.