Improvement of Gel Quality of Squid (Dosidicus gigas) Meat by Using Sodium Gluconate, Sodium Citrate, and Sodium Tartrate

Abstract

In order to improve the quality of squid surimi products, squid surimi gels were prepared using several types of organic salts under two heating conditions to study the effects of organic salts on squid gel properties. Compared with the NaCl group, organic salts reduced the solubilization capacity of myofibrillar protein, and significant (p < 0.05) decreases in the breaking force, breaking distance, texture, and water-holding capacity of the gel were observed in the sodium gluconate group, while significant (p < 0.05) increases in the breaking force, breaking distance, texture, and water-holding capacity of the gel were observed in the sodium citrate and sodium tartrate groups. Although the mixed addition of NaCl and organic salt improved surimi gel quality, the effective improvement was still lower than that of only organic salt. Rheological properties indicated that sodium citrate and sodium tartrate had high viscoelasticity. The squid surimi gel prepared by direct heating exhibited better properties than gels prepared by two-step heating. The chemical force of squid gel prepared with sodium citrate and sodium tartrate formed a stronger matrix than the gels prepared with other salts. For color, the addition of sodium citrate resulted in an undesirable color of squid surimi gels, while the addition of sodium tartrate improved the whiteness of the surimi gel. The results showed that the quality of surimi gel was dependent upon the choice of heating method and the types of salt used. Sodium citrate and sodium tartrate could significantly improve the gel properties of squid surimi. This study provides reliable guidance for improving the overall quality of squid surimi gels.

The effect of sodium tartrate and sodium citrate on quality changes of squid (Dosidicus gigas) surimi gel

“…The G "of surimi pastes in different treatment groups under heat induction showed a similar trend to G'. G' and G 00 in the ST group were lower than that in the SC group, and this might be related to the solubility of proteins and the inhibitory effect on metalloprotease, which we demonstrated in our previous study (Chu et al, 2022).…”

“…The gel strength of surimi gel was significantly affected by different types and concentrations of organic salt ( p < .05), as shown in Figure 1. The gel strength of the SC group was significantly higher than that of ST groups in the 2.5 and 3.5% addition levels due to the ability of SC to dissolve more myofibrillar proteins (as shown in Figure 2) and form a stronger gel network (Chu et al, 2022). As the salt concentration increased, the changes in gel strength of the SC and ST treatment groups were similar, and the similar chemical structures of ST and SC may have a similar effect on surimi gel (Liu et al, 2017).…”

“…Figure 2) and form a stronger gel network (Chu et al, 2022). As the salt concentration increased, the changes in gel strength of the SC and ST treatment groups were similar, and the similar chemical structures of ST and SC may have a similar effect on surimi gel (Liu et al, 2017).…”

The effect of heating method on the gel structures and properties of surimi prepared from Bombay duck (Harpadon nehereus)

“…Indeed, hardness increased with increasing setting time at 30°C, but it decreased with increasing setting time at 40°C due to gel softening. At 30°C, the disintegration and rearrangement of actin, troponin, tropomyosin, and light chain meromyosin and the protein cross-linking by hydrophobic forces and disulfide bonds formed a dense gel network ( 15 , 22 ). Not only that, endogenous transglutaminase in BD could promote the cross-linking of glutamine and lysine reactions in myofibrillar proteins [epsilon − (γ-glutamyl) -Lysine cross-linkage] creating a more stable gel network ( 23 ).…”

“…The solubility of proteins in the gel was assessed based on the method proposed by Niu et al and Chu et al ( 14 , 15 ), with some modifications. Four chemical reagents [0.6 mol/L NaCl (SA); 0.6 mol/L NaCl, 1.5 mol/L urea (SB); 0.6 mol/L NaCl, 8 mol/L urea (SC); and 0.6 mol/L NaCl, 8 mol/L urea, 0.5 mol/L β-mercaptoethanol (SD)] were used to cleave interactions, dissolve the surimi protein, and examine ionic bonds (SA), hydrogen bonds (SB minus SA), hydrophobic interactions (SC minus SB), and disulfide bonds (SD minus SC) in the gel.…”