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MOLECULAR NUTRITION & FOOD RESEARCH · 2018 ·Vol. 62 ·期 7 ·1700981 · IF 5.151

Comparison of the Oral Absorption, Distribution, Excretion, and Bioavailability of Zinc Sulfate, Zinc Gluconate, and Zinc-Enriched Yeast in Rats

Shuang-Qing Zhang,Xue-Feng Yu,Hai-Bo Zhang,Ning Peng,Zhi-Xian Chen,Qian Cheng,Xiao-Li Zhang,Sui-Han Cheng,Yan Zhang

Scope The oral absorption, distribution, excretion, and bioavailability of zinc sulfate (ZnS), zinc gluconate (ZnG), and zinc-enriched yeast (ZnY) in rats are fully and systemically compared for the first time. Methods and results After zinc compounds were orally administered to rats at a single dose of 4 mg Zn kg –1 , blood, tissues, urine, and feces at different time points were collected for the quantification of zinc concentration. Blood was also harvested for the zinc assay in the multiple-dose administration. Plasma zinc levels among three zinc compounds showed no difference, and zinc was widely distributed in various tissues with the level sequence of bone > liver > pancreas > testes. The net Zn balance was 2.993, 5.125, and 7.482% for ZnS, ZnG, and ZnY, respectively. Conclusion ZnS, ZnG, and ZnY show equivalent bioavailability based on plasma and tissues zinc levels, although ZnY was statistically more absorbed and retained than ZnS and ZnG based on the excretion amount.

研究领域: 营养学 · 药理学
✓ 已验证 DOI PubMed 高影响因子
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Journal of Advanced Research · 2025 · IF 13

A dual absorption pathway of novel oyster-derived peptide-zinc complex enhances zinc bioavailability and restores mitochondrial function

Ximing Yang,Siyi Wang,Hanxiong Liu,Tuo Zhang,Shuzhen Cheng,Ming Du

Zinc deficiency is a global health issue that impairs immune function, growth, and energy metabolism. Although conventional zinc supplements have been developed, their effectiveness is limited by poor bioavailability and susceptibility to dietary inhibitors. In this study, a peptide-zinc complex (IE-Zn) derived from oysters was developed to enhance zinc uptake and address metabolic disruptions caused by deficiency. It was determined that Zn 2+ binds with high affinity to the IE peptide, promoting structural flexibility that facilitates zinc transport through both zinc ion transporters and oligopeptide transporters. In Caco-2 and IEC-6 cell models, IE-Zn was shown to significantly improve zinc absorption and retention compared to ZnSO 4 , driven by the upregulation of ZIP4 and PEPT1 transporters. In vivo studies in a zinc-deficient mouse model confirmed enhanced zinc absorption and distribution across serum, intestine, and liver. Moreover, IE-Zn restored energy homeostasis by activating the AMPK/PGC1-α/NRF-1/TFAM signaling pathway, promoting mitochondrial biogenesis and reducing oxidative stress. These findings suggest that IE-Zn is a superior zinc supplement with higher bioavailability and serves as a potent regulator of cellular energy metabolism, offering therapeutic potential for managing conditions related to zinc deficiency and mitochondrial dysfunction. This study lays the foundation for further exploration of peptide-mineral complexes as advanced nutritional supplements with broad applications. Subsequent studies will further investigate the absorption pathway and targeting of peptide-zinc complex. The hope is to provide potential preventive applications for people in need, including zinc deficiency and a range of diseases caused by zinc deficiency.

CAS / MDL: 9048-46-8 7446-20-0
研究领域: 营养学 · 分子生物学 · 代谢研究
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Food Bioscience · 2023 · IF 5.2

Establishment of oyster protein hydrolysate-chitosan oligosaccharide-zinc delivery system and its characterization, digestion & absorption in-vitro and in-vivo

Xuening Yu,Shijie Dou,Xiaoyang Liu,Fawen Yin,Deyang Li,Pengfei Jiang,Dayong Zhou

Zinc deficiency highly influences human health while the effects of some zinc supplements (peptide-zinc complex) would be negatively attenuated by human gastrointestinal environments. Therefore, it is necessary to develop the embedding methods to improve the stability and absorption effects of zinc supplements. In this study, the chitosan oligosaccharide (COS) was used to react with oyster protein hydrolysates (OPH) for the formation of new zinc carrier. The selected conditions for preparing the OPH-COS-Zn complex were 4 mg/mL, 30°C and 80 min by testing the zinc-chelating capacity. The main binding sites of OPH-COS complex with zinc were presumed to be involved in amino, carboxyl and carbonyl groups. The OPH-COS-Zn delivery system showed high zinc ion release rate (57.04%) by offering high soluble zinc amounts (61.07%) and remained stable in gastrin phase but partially degraded in intestinal phase in gastrointestinal digestion in-vitro . Furthermore, the delivery system was successfully absorbed and carried zinc ions to the serosal side (0.3027 mg/L) in everted rat gut sacs model. The OPH-COS-Zn delivery system showed better in-vivo temporary dynamic absorption of zinc (7.63 μmol/dL) than OPH-Zn (7.07 μmol/dL) and ZnSO 4 (6.09 μmol/dL), showing slow-release effects of zinc ions. This experiment provided the theoretical foundation for further study of embedding effects of peptide-based zinc supplements.

CAS / MDL: 3326-32-7
研究领域: 营养学 · 食品科学 · 生物技术 · 药学
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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY · 2023 · IF 6.1

Structural Characterization of Zinc–Sucrose Complex and Its Ability to Promote Zinc Absorption in Caco-2 Monolayer Cells and Mice

Nan Li,Ruiyan Wang,Zeyuan Deng,Jianqun Zhou,Wenwen Li,Qian Du,Liufeng Zheng

Sucrose emerges as a metal-ion chelating agent with excellent stability that may increase metal-ion absorption. This study aimed to characterize the structure of zinc–sucrose complex and investigate its ability to promote zinc absorption in Caco-2 monolayer cells and mice. Based on the results of the inductively coupled plasma emission spectrometer (ICP-ES), scanning electron microscopy–energy-dispersive X-ray spectroscopy (SEM-EDX), and Fourier transform infrared spectroscopy (FT-IR), it can be inferred that zinc and sucrose were chelated at a 1:1 ratio, with the hydroxyl groups playing a significant role. The Caco-2 monolayer cell model revealed that zinc–sucrose complex increased the amount of zinc uptake, retention, and transport in a dose- and time-dependent manner. Through the upregulation of genes and proteins for ZIP4, MT1, and DMT1, treatment with zinc–sucrose complex improved the proportion of absorbed zinc utilized for transport compared to ZnCl2 (26.21 ± 4.96 versus 8.50 ± 1.51%). Pharmacokinetic analysis of mice confirmed the zinc absorption-promoting effect of zinc–sucrose complex, as indicated by the considerably higher serum zinc level (4.16 ± 0.53 versus 2.56 ± 0.45 mg/L) and intestinal ZIP4, MT1, and DMT1 gene expression than ZnCl2. Further treatment of different zinc channel inhibitors and CETSA demonstrated the direct interaction of zinc–sucrose complex with ZIP4 protein and ZIP4-mediated cellular transport of zinc–sucrose complex. These findings provide a novel insight into the zinc absorption-promoting mechanism of zinc–sucrose complex, which could be used as an ingredient in functional foods to treat zinc deficiency.

CAS / MDL: 7646-85-7
研究领域: 营养学 · 药理学 · 分子生物学 · 细胞生物学 · 生物化学
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Food Bioscience · 2024 · IF 4.8

The structural characteristics of Crassostrea gigas peptide-zinc complexes and the bioactive mechanism of their enhanced zinc absorption

Siyi Wang,Ximing Yang,Shuzhen Cheng,Ming Du

Zinc is an essential mineral for human health, and its deficiency can lead to various health issues. Oysters ( Crassostrea gigas ) are known to be a rich source of protein-bound zinc. Oyster peptides were complexed with zinc sulfate (ZnSO 4 ) to be oyster peptide-zinc chelates (OPZs) that offer potential as a valuable zinc supplement. The complexation of zinc with oyster peptides induces conformational changes in the peptides, altering their overall spatial arrangement. This could potentially impact their functions and properties. OPZs have demonstrated enhanced physical and gastrointestinal stability, as they are resistant to digestion by pepsin and trypsin. The research has shown that OPZs can modulate the expression of key proteins involved in zinc binding (MT1), peptide transport (PePT1), and zinc transport (ZIP4 and ZnT1) in enterocytes. By regulating the proteins expression, OPZs have the potential to affect zinc absorption and homeostasis. Furthermore, OPZs have been found to enhance zinc absorption through dual pathways compared to the single pathway of inorganic zinc. Additionally, they have the potential to improve zinc bioaccessibility and bioavailability, meaning they can make zinc more easily absorbed by the body and readily available for use.

CAS / MDL: 7446-20-0
研究领域: 营养学 · 生物化学 · 分子生物学 · 食品科学
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