ArticleFoods (Basel, Switzerland)2024
Preparation, Characterization and Stability of Calcium-Binding Peptides Derived from Chicken Blood.
Article in Foods (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed.
- Preparation optimization, structural characterization, stability and promoting calcium absorption mechanism of sturgeon cartilage peptide-calcium chelates.Food chemistry: X · 2026Article
- Article
- Valorization of Goat Blood: Hydrolysate Production, Identification, Stability, and Bioavailability upon Gastrointestinal Digestion of Peptides with Dual ACE and DPP-IV Inhibitory Properties.Foods (Basel, Switzerland) · 2026Article
- Fabrication of Fructooligosaccharide-Food science & nutrition · 2026Article
- The binding mechanism of a novel ferrous ion chelating peptide from chicken blood hemoglobin and the bioavailability of the chelate.Food chemistry: X · 2025Article
- Optimization of the Preparation Process and Ameliorative Efficacy in Osteoporotic Rats of Peptide-Calcium Chelates from Skipjack Tuna (Foods (Basel, Switzerland) · 2024Article
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7 authors.
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Abstract
Calcium-binding peptides have gained significant attention due to their potential applications in various fields. In this study, we aimed to prepare, characterize, and evaluate the stability of calcium-binding peptides derived from chicken blood. Chicken hemoglobin peptides (CPs) were obtained by protease hydrolysis and were applied to prepare chicken hemoglobin peptide-calcium chelate (CP-Ca). The preparation conditions were optimized, and the characteristics and stability of CP-Ca were analyzed. The optimal chelating conditions were determined by single-factor and response surface tests, and the maximum calcium ion chelating rate was 77.54%. Amino acid analysis indicated that glutamic acid and aspartic acid motifs played an important role in the chelation of the calcium ions and CP. According to the characterization analysis, CP-Ca was a different substance compared with CP; calcium ions chelated CPs via the sites of carbonyl oxygen, carboxyl oxygen, and amino nitrogen groups; and after the chelation, the structure changed from a smooth homogeneous plate to compact granular. The stability analysis showed that CP-Ca was stable at different temperatures, pH, and gastrointestinal conditions. The study indicates that chicken blood is a promising source of peptide-calcium chelates, providing a theoretical basis for application in functional foods and improving the utilization value of chicken blood.
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