The purpose of this study is to explain the mechanism of porcine myofibrillar protein gel properties modulated by κ-carrageenan. The textural properties results showed that the stress at fracture of the composite gel with 0.4% κ-carrageenan had the highest value (91.33 g), which suggested that the 0.4% κ-carrageenan addition was the limitation. The strain at fracture was significantly reduced with κ-carrageenan addition. The composite gel with 0.4% κ-carrageenan had the lowest proportion of T22 (7.85%) and the shortest T21 relaxation time (252.81 ms). The paraffin section showed that the phase separation behavior of the composite gel transformed from single-phase behavior to dispersed phase behavior to bi-continuous phase behavior, and the ratio of CG/MP phase area significantly increased from 0.06 to 1.73. The SEM showed that the three-dimensional network of myofibrillar protein transformed from a loose structure to a compact structure to an unaggregated structure with κ-carrageenan addition. The myofibrillar protein network of the treatment with 0.4% κ-carrageenan had the highest DF value (1.7858) and lowest lacunary value (0.452). The principal component analysis was performed on the data of microstructure and textural properties, and the results showed that the dispersed phase behavior and moisture stabilization promoted the aggregation of myofibrillar protein and the composite gel had better water holding capacity and textural properties, while bi-continuous phase behavior hindered the aggregation of myofibrillar protein and the composite gel had worse water holding capacity and textural properties.

This paper focuses on the effect of malondialdehyde-induced oxidative modification (MiOM) on the gel properties of duck myofibrillar proteins (DMPs). DMPs were first prepared and treated with oxidative modification at different concentrations of malondialdehyde (0, 0.5, 2.5, 5.0, and 10.0 mmol/L). The physicochemical changes (carbonyl content and free thiol content) and gel properties (gel whiteness, gel strength, water holding capacity, rheological properties, and microstructural properties) were then investigated. The results showed that the content of protein carbonyl content increased with increasing MDA oxidation (p < 0.05), while the free thiol content decreased significantly (p < 0.05). Meanwhile, there was a significant decrease in gel whiteness; the gel strength and water-holding capacity of protein gels increased significantly under a low oxidation concentration of MDA (0–5 mmol/L); however, the gel strength decreased under a high oxidation concentration (10 mmol/L) compared with other groups (0.5–5 mmol/L). The storage modulus and loss modulus of oxidized DMPs also increased with increasing concentrations at a low concentration of MDA (0–5 mmol/L); moreover, microstructural analysis confirmed that the gels oxidized at low concentrations (0.5–5 mmol/L) were more compact and homogeneous in terms of pore size compared to the high concentration or blank group. In conclusion, moderate oxidation of malondialdehyde was beneficial to improve the gel properties of duck; however, excessive oxidation was detrimental to the formation of dense structured gels.