Academic Journal
Enhancement of gel properties of low‐salt Scomberomorus niphonius surimi by egg white protein: Structural refinement and intermolecular interaction analysis.
| Τίτλος: | Enhancement of gel properties of low‐salt Scomberomorus niphonius surimi by egg white protein: Structural refinement and intermolecular interaction analysis. |
|---|---|
| Συγγραφείς: | Tang, Yi‐Xiao1,2,3,4,5 (AUTHOR), Zhang, Lin‐Da1,2,3,4,5 (AUTHOR), Man, Xinyan1,2,3,4,5 (AUTHOR), Lv, Yin‐Yin1,2,3,4,5 (AUTHOR), Jiang, Heng6 (AUTHOR), Yao, Yuan6 (AUTHOR), Yan, Jia‐Nan1,2,3,4,5 (AUTHOR), Wang, Ce1,2,3,4,5 (AUTHOR), Lai, Bin1,2,3,4,5 (AUTHOR) laibin@dlpu.edu.cn, Wu, Hai‐Tao1,2,3,4,5 (AUTHOR) |
| Πηγή: | Journal of the Science of Food & Agriculture. Oct2026, Vol. 106 Issue 13, p7711-7723. 13p. |
| Θεματικοί όροι: | *Surimi, *Gelation, *Food texture, *Proteins, *Disulfides, *Fishery processing |
| Περίληψη: | BACKGROUND: High‐quality gelation of Scomberomorus niphonius (SN) surimi under low‐salt conditions remains challenging for the seafood industry. This study evaluated egg white protein (EWP) substitution (1–9%) to enhance the gel properties and water retention of low‐salt (1% sodium chloride) SN surimi under reduced ionic strength. RESULTS: The results demonstrated that the optimal performance was achieved at 5% EWP substitution, where the breaking force significantly increased by 58.9% compared to the low‐salt control (LC) group, and the water‐holding capacity (WHC) concurrently improved to 73.03%. Quantitative cryo‐scanning electron microscopy (cryo‐SEM) analysis revealed substantial network densification, characterized by a decrease in porosity from 55.67% (LC group) to 34.85% and a minimum mean pore size of 0.25 ± 0.16 μm. Pearson correlation and heat map visualization confirmed that this microstructural refinement (r = −0.921 with WHC) and the enhanced formation of disulfide bonds (r = 0.993 with breaking force) were the primary drivers for the improved water retention and gel strength, respectively. Mechanistically, at moderate substitution levels (≤ 5%), EWP was partially compatible with SN myofibrillar proteins, functioning as a co‐gellant and crosslinker via disulfide‐related interactions that transformed the loose, porous matrix into a compact honeycomb structure; however, excessive substitution (> 5%) promoted preferential EWP self‐aggregation and microphase separation, thereby undermining network continuity and integrity. CONCLUSION: Optimal EWP substitution (5%) effectively overcomes the gelation defects of low‐salt SN surimi by forming a co‐gel network driven by disulfide crosslinking and structural densification. These findings elucidate the quantitative structure–function relationship of EWP in low‐ionic‐strength systems, providing a solid theoretical foundation for the development of healthy, salt‐reduced surimi products. © 2026 Society of Chemical Industry. [ABSTRACT FROM AUTHOR] |
| Βάση Δεδομένων: | Academic Search Index |
καταχωρήστε σχόλιο πρώτοι!