Gel Property of Soy Protein Emulsion Gel: Impact of Combined Microwave Pretreatment and Covalent Binding of Polyphenols by Alkaline Method

Abstract

This study investigated the effects of microwave modification, alkali polyphenol (ferulic acid) covalently combined modification, and microwave-alkali polyphenol covalently combined modification on the gel properties of soy protein emulsions. The results showed that the properties of soy protein emulsions were improved significantly by the three modification methods. After three kinds of modification, the viscoelasticity of soy protein emulsion gel increased, and a gel system with stronger elasticity was formed. The texture, water-holding, and hydration properties of the emulsion gel increased significantly. The SEM and ClSM results showed that the modified soy protein emulsion gel had a more compact and uniform porous structure, and the oil droplets could be better embedded in the network structure of the gel. Among the three modification methods, the microwave-alkali method polyphenol covalently combining the compound modification effect was best, and the microwave modification effect was least effective compared to the other two methods. Our obtained results suggested that for gel property modification of soy protein emulsion gels, microwave pretreatment combined with the covalent binding of polyphenols by an alkaline method is an effective method.

Study on the effect and mechanism of chicken breast on the gel properties of silver carp (Hypophthalmichtys molitrix) surimi

“…The smaller the relaxation time, the tighter the binding of water and substance 41 . T 21 (< 10 ms) represents bound water tightly bound to the macromolecule; T 22 (10–100 ms) represents partially immobile water, distributed in the network structure of the protein; and T 23 (100–10 000 ms) represents free water, located outside the protein network structure 42,43 . Figure 3 and Table 3 show T 2 of the mixed gels with different ratios, and three hydrogen proton peaks ( T 21 , T 22 and T 23 ) could be clearly observed.…”

“…41 T 21 (< 10 ms) represents bound water tightly bound to the macromolecule; T 22 (10-100ms) represents partially immobile water, distributed in the network structure of the protein; and T 23 (100-10 000 ms) represents free water, located outside the protein network structure. 42,43 Figure 3 and Table 3 show T 2 of the mixed gels with different ratios, and three hydrogen proton peaks (T 21 , T 22 and T 23 ) could be clearly observed. From Table 3, it was found that A 21 ranged from 6.35 to 38.42, and the addition of chicken breast caused a significant decrease in A 21 (P < 0.05).…”

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“…The presence of the aqueous phase may change the interfacial membrane structure of the protein‐coated droplets through the electrostatic shielding effect, thus affecting the stability of the emulsion. The decrease of electrostatic repulsion between adsorbed particles and non‐adsorbed particles may strengthen the interfacial film (Xu et al ., 2022).…”

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“…The parameter settings of the refractive indices were oil phase (1.46) and water phase (1.33). Samples were diluted 100-fold with deionized water to avoid multiple scattering effects and used for analysis [ 47 ].…”