An oyster protein hydrolysates-zinc complex (OPH-Zn) was prepared and investigated to improve zinc bioaccessibility. Zinc ions chelating with oyster protein hydrolysates (OPH) cause intramolecular and intermolecular folding and aggregation, homogeneously forming the OPH-Zn complex as nanoclusters with a Z-average at 89.28 nm (PDI: 0.16 ± 0.02). The primary sites of zinc-binding in OPH were carboxyl groups, carbonyl groups, and amino groups, and they were related to the high number of charged amino acid residues. Furthermore, formation of the OPH-Zn complex could significantly enhance zinc solubility both under specific pH conditions as well as during simulated gastrointestinal digestion, compared to the commonly used ZnSO₄. Additionally, after digestion, either preserved or enhanced antioxidant activity of OPH was found when chelated with zinc. These results indicated that the OPH-Zn complex could be a potential functional ingredient with improved antioxidant bioactivity and zinc bioaccessibility.

制备牡蛎蛋白水解物-锌复合物（OPH-Zn），并进行研究以改善锌的生物利用度。与牡蛎蛋白水解物（OPH）螯合的锌离子会引起分子内和分子间的折叠和聚集，均匀地形成OPH-Zn复合物，成为Z值在89.28 nm的纳米团簇（PDI：0.16±0.02）。OPH中锌结合的主要位点是羧基，羰基和氨基，它们与大量带电荷的氨基酸残基有关。此外，与常用的ZnSO ₄相比，在特定的pH条件下以及在模拟的胃肠道消化过程中，OPH-Zn络合物的形成都可以显着提高锌的溶解度。。另外，消化后，与锌螯合后，发现OPH的抗氧化活性得以保持或增强。这些结果表明，OPH-Zn复合物可能是具有改善的抗氧化剂生物活性和锌生物可及性的潜在功能成分。