Changing the Gel‐Forming Properties of Myofibrillar Protein by Using a Gentle Breaking Method

Abstract

Chopping and stirring methods were used to prepare surimi gels in a way that preserved their inherent characteristics while maintaining or improving their textural properties and microstructures. In samples with the samesalt levels, the stirring process led to a higher gel strength than the chopping process (P < 0.05), improved the gels' water holding capacity (WHC) and viscosity, and slightly decreased the amount of salt-soluble protein. Low-field nuclear magnetic resonance showed that the stirring method improved the WHC of the product more than the chopping method. Scanning electron microscopy revealed that the surimi gels produced by stirring with 3% salt had a denser and more uniform microstructure than those produced by chopping with 2% or 3% salt. Overall, the results indicated that the stirring method is comparatively more gentle than the chopping method and can produce high-quality surimi gels that retain their original properties.Practical Application: The study examines a gentle breaking method for improving the textural properties of surimi gels while remaining their original characteristics of fish. Stirring processing, as a low-intensity breaking method, can significantly increase the gel strength and slightly increase the WHC of surimi gels compared to chopping methods. The method produces high-quality products with nutritional value, which benefits both producers and customers.

Study on the water state, migration, and microstructure modification during the process of salt‐reduced stewed duck

“…The changes in the relaxation time T 2 in the duck thigh meat after stew were shown in Table 3. As mentioned previously, T 2 value could successfully reflects the tightness of the combination between water state and duck thigh meat, where T 20 and T 21 represented the bound water, T 22 and T 23 represented the immobilized water and the free water respectively (Wang et al., 2019). According to the results displayed in Table 3, whichever group, no significant difference ( p < 0.05) was noted for the relaxation time of T 20 and T 21 with the increase of stewed time, and the value of two treated groups also presented similar levels throughout the stew process.…”

“…The changes in the relaxation time T 2 in the duck thigh meat after stew were shown in Table 3. As mentioned previously, T 2 value could successfully reflects the tightness of the combination between water state and duck thigh meat, where T 20 and T 21 represented the bound water, T 22 and T 23 represented the immobilized water and the free water respectively (Wang et al, 2019). According to the Different lowercase letters column (comparison of moisture in the same state) represents significant differences (p < 0.05).…”

Effects of salt‐induced changes in protein network structure on the properties of surimi gels: computer simulation and digestion study

“…The solubility of the salt solution proteins of surimi was determined using a modified method previously reported (Wang et al., 2018a; Wang et al., 2018b). Three grams of surimi samples were homogenised at 10 000 rpm with 27.0 mL buffer (0.6 m KCl, 20.0 m m Tris‐HCl, pH 7.0) for 1 min.…”

“…Salt ions effectively dissolve the salt‐soluble proteins in fish, thereby resulting in formation of a cross‐linked network structure that improves textural properties and taste (Zhang et al., 2017a; Zhang et al., 2017b). Salt typically ionises into anions and cations in aqueous solutions, thereby changing the hydration layer outside of proteins (Wang et al., 2018a; Wang et al., 2018b) MgCl 2 and CaCl 2 affect enzyme activity and the conformation of protein gels, thus altering gel properties (Barat et al., 2013; Hamzah et al., 2015). Ca 2+ and Mg 2+ play major roles in the gelation process because they affect transglutaminase (TGase) activity, thus influencing acyl transfer reactions against glutamine and lysin.…”