ArticleJournal of the science of food and agriculture2026
Enhancement of gel properties of low-salt Scomberomorus niphonius surimi by egg white protein: Structural refinement and intermolecular interaction analysis.
Article in Journal of the science of food and agriculture, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
backgroundHigh-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.
resultsThe 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.
conclusionOptimal 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.
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