ArticleFoods (Basel, Switzerland)2025
Donkey-Hide Gelatin Peptide-Iron Complexes: Structural Characterization, Enhanced Iron Solubility Under Simulated Digestion, and Dual Iron Chelation-Antioxidant Functions.
Article in Foods (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Oyster Peptide-Ferrous Chelate Preparation Optimization Structural Characteristics and Enhanced Bioavailability.Foods (Basel, Switzerland) · 2026Article
- Valorization of Camel Milk Residue (CMR) into Hypoglycemic Peptides: An RSM-ANN Modeling Approach.Foods (Basel, Switzerland) · 2025Article
- The Characterization of Physicochemical, Nutritional, and Flavor Properties of Bovine Hide Gelatin Prepared from Different Raw Materials.Foods (Basel, Switzerland) · 2025Article
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Authors and funding
4 authors.
Funding
Abstract
Iron deficiency is a global health issue, making the development of novel iron supplements to enhance iron absorption critically important. In this study, low molecular weight donkey-hide gelatin peptides (LMW DHGP) were enzymatically hydrolyzed from donkey-hide gelatin. Experimental results demonstrated that the iron chelating capacity of LMW DHGP reached 249.98 μg/mg. Key amino acids (Asn, Gly, Cys, Lys) may participate in chelation. Scanning electron microscopy (SEM) and X-ray diffraction (XRD) analysis showed rough, porous amorphous structures of LMW DHGP-iron complexes. The results of circular dichroism spectroscopy (CD) indicated that the self-assembly of LMW DHGP-iron complexes appears to be primarily mediated by peptide α-helical structural conformations. Fourier transform infrared (FTIR) spectroscopy further indicated that the interaction between LWM DHGP and Fe
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