ArticleFoods (Basel, Switzerland)2022
Isolation, Purification and Structure Identification of a Calcium-Binding Peptide from Sheep Bone Protein Hydrolysate.
Article in Foods (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 31 citations in OpenAlex.
- MBPBERT: A Large Language Model for Metal-Binding Peptide Discovery.Interdisciplinary sciences, computational life sciences · 2026Article
- Preparation, Structural Characterization, and Calcium Supplementation Activity ofFoods (Basel, Switzerland) · 2025Article
- Identification and Characterization of Glycine- and Proline-Rich Antioxidant Peptides From Antler Residues Based on Peptidomics, Machine Learning, and Molecular Docking.Food science & nutrition · 2025Article
- Article
- Analyzing the Effect of Dried Shrimp on the Flavor of Sheep Bone Soup Through Sensory Evaluation Combined with Untargeted Approaches.Foods (Basel, Switzerland) · 2025Article
- Highly Self-Adhesive and Biodegradable Silk Bioelectronics for All-In-One Imperceptible Long-Term Electrophysiological Biosignals Monitoring.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Novel peptides with calcium-binding capacity from antler bone hydrolysate, its bioactivity on MC3T3-E1 cells, and the possible chelating mode.Food science & nutrition · 2024Article
- Preparation, Structural Characterization, and Stability of Low-Molecular-Weight Collagen Peptides-Calcium Chelate Derived from Tuna Bones.Foods (Basel, Switzerland) · 2023Article
- Study on the Interaction Mechanism of Methoxy Polyethylene Glycol Maleimide with Sweet Potato β-Amylase.Molecules (Basel, Switzerland) · 2023Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
To isolate a novel peptide with calcium-binding capacity, sheep bone protein was hydrolyzed sequentially using a dual-enzyme system (alcalase treatment following neutrase treatment) and investigated for its characteristics, separation, purification, and structure. The sheep bone protein hydrolysate (SBPH) was enriched in key amino acids such as Gly, Arg, Pro, Leu, Lys, Glu, Val, and Asp. The fluorescence spectra, circular dichroism spectra, and Fourier-transform infrared spectroscopy results showed that adding calcium ions decreased the α-helix and β-sheet content but significantly increased the random and β-turn content (p < 0.05). Carboxyl oxygen and amino nitrogen atoms of SBPH may participate in peptide−calcium binding. Scanning electron microscopy and energy dispersive spectrometry results showed that SBPH had strong calcium-chelating ability and that the peptide−calcium complex (SBPH−Ca) combined with calcium to form a spherical cluster structure. SBPH was separated and purified gradually by ultrafiltration, gel filtration chromatography, and reversed-phase high-performance liquid chromatography. Liquid chromatography-electrospray ionization/mass spectrometry identified the amino acid sequences as GPSGLPGERG (925.46 Da) and GAPGKDGVRG (912.48 Da), with calcium-binding capacities of 89.76 ± 0.19% and 88.26 ± 0.25%, respectively. The results of this study provide a scientific basis for the preparation of a new type of calcium supplement and high-value utilization of sheep bone.
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