ArticleJournal of food science2026
Comparative Effects of Soybean Protein Isolate- and Myofibrillar Protein-Based Curcumin Nanocomplexes on the Freeze-Thaw Stability of Surimi.
Article in Journal of food science, 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
Proteins are effective carriers for polyphenols, yet whether structural differences between plant- and animal-derived proteins influence the delivery and functionality of polyphenols in their nanocomplexes remains unclear. In this study, soy protein isolate-curcumin (SPI-CUR) and myofibrillar protein-curcumin (MP-CUR) nanocomplexes were fabricated via a pH-driven method, and their physicochemical properties, interaction mechanisms, and cryoprotective effects on surimi were investigated. Both nanocomplexes achieved high encapsulation efficiencies (90.63% for SPI-CUR and 83.29% for MP-CUR) and thus exhibited enhanced antioxidant activity. CUR loading induced conformational changes in the protein carriers, as evidenced by increased α-helix content and decreased β-sheet content, suggesting the formation of a more compact structure. Meanwhile, this conformational change was accompanied by a marked reduction in particle size, with SPI-CUR reaching 66.13 nm. Molecular docking further revealed that hydrophobic interactions and hydrogen bonding were the primary forces stabilizing both nanocomplexes. During freeze-thaw cycles of surimi, both SC and MC nanocomplexes were superior to commercial cryoprotectants in preserving product quality, evidenced by improved water-holding capacity, enhanced gel properties, and inhibited protein oxidation. Notably, the two nanocomplexes exhibited distinct protective profiles depending on the protein source. MP-CUR demonstrated superior preservation of gel texture by minimizing thawing loss to 0.53% and maintaining high hardness (425.50 ± 34.85 g) and springiness (0.81 ± 0.03), which facilitated the formation of a denser gel network. In contrast, SPI-CUR demonstrated superior viscoelasticity and yielded the highest storage modulus (G'). This study establishes a foundation for the rational design of natural and efficient surimi cryoprotectants derived from protein-polyphenol complexes.
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