期刊
FOOD CHEMISTRY
卷 258, 期 -, 页码 269-277出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2018.03.030
关键词
Oyster peptides-zinc complex; Nanocomposite; Characterization; Solubility; Simulated digestion
资金
- Guangxi Natural Science Foundation [AA17204075]
- Bagui Scholars Distinguished Professor Special Project, Natural Science Foundation of China [31701539]
- Natural Science Foundation of Guangdong Province [2017A030313127]
- Qinzhou University Science Research Foundation [2013XJKY-11B]
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.
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