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Isolation, structure identification, and antioxidant activity of collagen peptides from horse bone marrow

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Abstract

Insufficient research on the material basis and functional product development of horse bones has led to the waste of resources. This paper, as the by-product of horse meat bone marrow was the object, aimed to discover the flavor and antioxidant activity of novel collagen peptides. Two peptides, HBMP-1-1 and HBMP-2-1, were isolated and purified from horse bone marrow collagen protein (HBMP) hydrolysates. The combination of spectroscopic and chromatographic methods including SDS-PAGE, UV, FT-IR, CD, and SEM identified the structures of the peptides. The amino acid composition, flavor characteristics, and antioxidant activity were also evaluated. SDS-PAGE analysis showed that the molecular weight of the two peptides was concentrated under 4.1 kDa. The total amino acid contents of the HBMP-1-1 was up to 570.779 mg/g. Leucine, alanine, and glutamicacid were the predominant amino acids in HBMP-1-1 with high nutritional value, and it contained 10.07% β-folding, 46.39% β-turn, and 43.54% random coil structure. The peptide sequences IDDPTDSKPE, LNGKLTGM, ELDEGYVPK, AFQEDPDKF, and FVGKVVDPTQK with molecular weights of 1116.51, 833.45, 1049.51, 1096.49, and 1217.69 Da were detected using LC-MS/MS. The results of the antioxidant activity test showed that separation and purification significantly improved the bioactivity of the protein. The half-inhibition rate of HBMP-1-1 against DPPH, ABTS, and hydroxyl radicals were 0.054, 0.050, and 0.137 mg/mL, respectively. This article provides a scientific basis for clarifying the material basis of horse bone marrow collagen peptides. Also, it provides new approaches and ideas for exploring efficient and safe bone-derived lead compounds and products.

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Acknowledgements

This research was supported by the Young Natural Science Project of the University Scientific Research Program of Xinjiang Uygur Autonomous Region (XJEDU2019Y022).

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Rozi, P., Mattohti, W., Ababakri, G. et al. Isolation, structure identification, and antioxidant activity of collagen peptides from horse bone marrow. Food Measure (2024). https://doi.org/10.1007/s11694-024-02477-y

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