{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T05:18:13Z","timestamp":1787980693109,"version":"build-2784847793"},"reference-count":56,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2026,8,22]],"date-time":"2026-08-22T00:00:00Z","timestamp":1787356800000},"content-version":"vor","delay-in-days":21,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:00:00Z","timestamp":1785542400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["ift.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Food Science"],"published-print":{"date-parts":[[2026,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:sec>\n                    <jats:label\/>\n                    <jats:p>\n                      Proteins are effective carriers for polyphenols, yet whether structural differences between plant\u2010 and animal\u2010derived proteins influence the delivery and functionality of polyphenols in their nanocomplexes remains unclear. In this study, soy protein isolate\u2010curcumin (SPI\u2010CUR) and myofibrillar protein\u2010curcumin (MP\u2010CUR) nanocomplexes were fabricated via a pH\u2010driven method, and their physicochemical properties, interaction mechanisms, and cryoprotective effects on surimi were investigated. Both nanocomplexes achieved high encapsulation efficiencies (90.63% for SPI\u2010CUR and 83.29% for MP\u2010CUR) and thus exhibited enhanced antioxidant activity. CUR loading induced conformational changes in the protein carriers, as evidenced by increased \u03b1\u2010helix content and decreased \u03b2\u2010sheet content, suggesting the formation of a more compact structure. Meanwhile, this conformational change was accompanied by a marked reduction in particle size, with SPI\u2010CUR reaching 66.13\u00a0nm. Molecular docking further revealed that hydrophobic interactions and hydrogen bonding were the primary forces stabilizing both nanocomplexes. During freeze\u2013thaw cycles of surimi, both SC and MC nanocomplexes were superior to commercial cryoprotectants in preserving product quality, evidenced by improved water\u2010holding capacity, enhanced gel properties, and inhibited protein oxidation. Notably, the two nanocomplexes exhibited distinct protective profiles depending on the protein source. MP\u2010CUR demonstrated superior preservation of gel texture by minimizing thawing loss to 0.53% and maintaining high hardness (425.50 \u00b1 34.85\u00a0g) and springiness (0.81 \u00b1 0.03), which facilitated the formation of a denser gel network. In contrast, SPI\u2010CUR demonstrated superior viscoelasticity and yielded the highest storage modulus (\n                      <jats:italic>G<\/jats:italic>\n                      \u2032). This study establishes a foundation for the rational design of natural and efficient surimi cryoprotectants derived from protein\u2010polyphenol complexes.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1111\/1750-3841.71400","type":"journal-article","created":{"date-parts":[[2026,8,22]],"date-time":"2026-08-22T10:25:06Z","timestamp":1787394306000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Comparative Effects of Soybean Protein Isolate\u2010 and Myofibrillar Protein\u2010Based Curcumin Nanocomplexes on the Freeze\u2013Thaw Stability of Surimi"],"prefix":"10.1111","volume":"91","author":[{"given":"Xiaoyu","family":"Liu","sequence":"first","affiliation":[{"name":"Key Laboratory of Chinese Cuisine Intangible Cultural Heritage Technology Inheritance, Ministry of Culture and Tourism, College of Tourism and Culinary Science Yangzhou University  Yangzhou 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