Polysaccharides Regulate the Structural Stability and Gelation Behavior of Oxidized Myofibrillar Protein in Cantonese Sausage Storage

Abstract

This study investigated how laminarin (Lam), Tremella polysaccharide (TrP), and Astragalus polysaccharide (AsP) regulate the structural integrity and gel-forming ability of oxidized myofibrillar protein (MP) and explored their potential application in the storage process of Cantonese sausage. Under oxidative conditions, all three polysaccharides reduced the formation of carbonyl groups, inhibited MP aggregation, and helped maintain the α-helical structure, indicating their protective effect on protein oxidation. Scanning electron microscopy observations showed that low concentrations of polysaccharides promoted the formation of a tight and uniform gel matrix by reducing water channels, thereby enhancing water retention. Molecular docking further revealed that the representative structural units of these three polysaccharides mainly bind to porcine myosin through hydrogen bonding, accompanied by electrostatic and hydrophobic interactions, providing molecular evidence for the stabilizing effect of polysaccharides on the MP structure. In the Cantonese sausage system, the addition of polysaccharides effectively inhibited protein oxidation, maintained product color, delayed oxidative deterioration, stabilized pH during storage, and significantly enhanced water retention and texture characteristics. Overall, these findings suggest that polysaccharides reduce oxidative damage to MP through radical scavenging and protein–polysaccharide interactions. This study evaluated the abilities of laminarin (Lam), Tremella polysaccharide (TrP), and Astragalus polysaccharide (AsP) in maintaining the structural stability and gel characteristics of oxidized myofibrillar proetin (MP), as well as their potential application value in the storage of Cantonese sausage.