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Home / Equine Research Bank / Sci Rep / Preparation and tissue structure analysis of horse bone coll...
Scientific reports2024; 14(1); 25687; doi: 10.1038/s41598-024-75960-7

Preparation and tissue structure analysis of horse bone collagen peptide.

Abstract: Horse bone is rich in collagen, with a composition similar to that of human collagen. Collagen peptides supply nutrients needed for human growth that act as antioxidants, lower blood pressure. This study explored the extraction of collagen and the preparation of collagen short peptides from Mongolian horse bones. Bones were collected from horses of varying ages, and the collagen content along with calcium salt distribution were observed through staining and imaging analyses. Next, the bones were processed into a powder and then subjected to ultra-high-pressure processing for degreasing. The degreasing conditions were optimised by single-factor and orthogonal tests. Following this, collagen was extracted using an acid-enzymatic method, and its structural characteristics and thermal stability were assessed. The collagen short peptides were extracted from the collagen samples, and the effects of the enzymatic hydrolysis time, temperature, pH, and enzyme amount on the extraction rate were evaluated. Finally, the resulting collagen peptides were analysed for antioxidant activity. In summary, this experiment optimised the extraction conditions for horse bone collagen, demonstrating that the ultra-high-pressure method minimally affects collagen structure, and the extraction rate was high. Hence our method has significant development potential.
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Publication Date: 2024-10-28 PubMed ID: 39463408PubMed Central: PMC11514178DOI: 10.1038/s41598-024-75960-7Google Scholar: Lookup
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  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research explores the extraction of collagen and collagen peptides from horse bones, confirming that the ultra-high-pressure method has minimal effect on collagen structure and guarantees a high extraction rate, suggesting its significant potential for development.

Overview of the Research

  • The research focuses on the extraction and analysis of collagen and collagen peptides from horse bones. Collagen peptides are crucial for human growth and have various health benefits such as antioxidative properties and lowering blood pressure.
  • The paper emphasizes the importance of collagen from horse bones due to its compositional similarity with human collagen.

Methodology of the Research

  • The bones were collected from Mongolian horses of varying ages for this experiment. Imaging analysis was done to observe the collagen content and calcium salt distribution in the bones.
  • These bones were further powdered and subjected to ultra-high-pressure processing for degreasing. The optimal conditions for this degreasing process were established with single-factor and orthogonal tests.
  • The collagen was then separated using an acid-enzymatic method, which involves the use of an acid and an enzyme to extract the collagen. The structural character and thermal stability of the extracted collagen were subsequently evaluated.
  • Collagen peptides were then derived from these collagen samples. The effects of various factors like the enzymatic hydrolysis time, temperature, pH, and enzyme amount on the extraction rate of these peptides were assessed.

Findings of the Research

  • The study found that the prepared collagen and collagen peptides were antioxidant, indicating their health benefits.
  • The use of the ultra-high-pressure method in the extraction process reportedly had minimal effects on the collagen structure, indicating the efficiency of this method.
  • The extraction rate for the collagen was found to be high, suggesting a promising efficiency method for collagen extraction.

Conclusion

  • The study affirmed that the extraction conditions for horse bone collagen were optimized, implying the viability of the extraction procedure for large-scale collagen extraction.
  • Conclusively, the study highlights significant potential for the development of collagen extraction methods, given the minimal effects on collagen structure and high extraction rates.

Cite This Article

APA
Wu J, Na H, Bai F, Li S, Gao H, Sha R. (2024). Preparation and tissue structure analysis of horse bone collagen peptide. Sci Rep, 14(1), 25687. https://doi.org/10.1038/s41598-024-75960-7

Publication

Scientific reports
ISSN: 2045-2322
NlmUniqueID: 101563288
Country: England
Language: English
Volume: 14
Issue: 1
Pages: 25687

Researcher Affiliations

Wu, Jindi
  • College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot, 010018, China.
Na, Heya
  • College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot, 010018, China.
Bai, Fan
  • Veterinary Research Institute, Inner Mongolia Academy of Agricultural and Animal Husbandry Sciences, Hohhot, 010031, China.
Li, Siyu
  • College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot, 010018, China.
Gao, Hao
  • College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot, 010018, China.
Sha, Rina
  • College of Food Science and Engineering, Inner Mongolia Agricultural University, Hohhot, 010018, China. spsharina@imau.edu.cn.

MeSH Terms

  • Horses
  • Animals
  • Collagen / chemistry
  • Bone and Bones / chemistry
  • Bone and Bones / metabolism
  • Peptides / chemistry
  • Antioxidants / chemistry
  • Temperature
  • Hydrolysis
  • Hydrogen-Ion Concentration

Grant Funding

  • 2022QN03026 / Natural Science Foundation of Inner Mongolia Autonomous Region
  • RC1900004555 / Postgraduate Training fund

Conflict of Interest Statement

The authors declare no competing interests.

References

This article includes 46 references
  1. Linjie Y. Current status and development trend of ultra-high pressure food processing equipment.. China Food Saf. Mag. 31, 162–164 (2021).
    doi: 10.16043/j.cnki.cfs.2021.31.049google scholar: lookup
  2. Shengjie X, Dong Z, Xiang G, Cheng D, Weitao H. Application research of ultra-pressure food processing equipment in food industry.. Food Ind. 40(12), 222–225 (2019).
    doi: 10.16043/j.cnki.cfs.2019.40.049google scholar: lookup
  3. Kazutaka Y. Food processing by high hydrostatic pressure.. Biosci. Biotechnol. Biochem. 81(4), 672–679 (2017).
    pubmed: 28300504doi: 10.1080/09168451.2017.1281723google scholar: lookup
  4. Nan J. Effect of ultra-high pressure on molecular structure and properties of bullfrog skin collagen.. Int. J. Biol. Macromol. 111, 200–207 (2018).
    pubmed: 29307800doi: 10.1016/j.ijbiomac.2017.12.163google scholar: lookup
  5. Patrignani F. Ultra) high pressure homogenization potential on the shelf-life and functionality of kiwifruit juice.. Front. Microbiol. 10, 246 (2019).
    pmc: PMC6389688pubmed: 30837971doi: 10.3389/fmicb.2019.00246google scholar: lookup
  6. Xi J, Li Y. The effects of ultra-high-pressure treatments combined with heat treatments on the antigenicity and structure of soy glycinin.. Int. J. Food Sci. Technol. 56(10), 5211–5219 (2021).
    doi: 10.1111/ijfs.15297google scholar: lookup
  7. Aganovic K. Aspects of high hydrostatic pressure food processing: Perspectives on technology and food safety.. Compreh. Rev. Food Sci. Food Saf. 20(4), 3225–3266 (2021).
    pubmed: 34056857doi: 10.1111/1541-4337.12763google scholar: lookup
  8. Dong X B. Development of a novel method for hot-pressure extraction of protein from chicken bone and the effect of enzymatic hydrolysis on the extracts.. Food Chem. 157, 339–346 (2014).
    pubmed: 24679789doi: 10.1016/j.foodchem.2014.02.043google scholar: lookup
  9. Kim D. Anti-oxidation and anti-wrinkling effects of Jeju horse leg bone hydrolysates.. Food Sci. Anim. Resour. 34(6), 844–851 (2014).
    pmc: PMC4662201pubmed: 26761683doi: 10.5851/kosfa.2014.34.6.844google scholar: lookup
  10. León-López A, Fuentes-Jiménez L, Hernández-Fuentes A D, Campos-Montiel R G, Aguirre-Álvarez G. Hydrolysed collagen from sheepskins as a source of functional peptides with antioxidant activity.. Int. J. Mol. Sci. 20(16), 3931 (2019).
    pmc: PMC6719941pubmed: 31412541doi: 10.3390/ijms20163931google scholar: lookup
  11. Miroslava G M. Bioactive peptides from collagen hydrolysates from squid (Dosidicus gigas) by-products fractionated by ultrafiltration.. Int. J. Food Sci. Technol. 54(4), 1054–1061 (2019).
    doi: 10.1111/ijfs.13984google scholar: lookup
  12. Hou N T, Chen B H. Extraction, purification and characterization of collagen peptide prepared from skin hydrolysate of Sturgeon fish.. Food Qual. Saf. 7, fyad033 (2023).
    doi: 10.1093/fqsafe/fyad033google scholar: lookup
  13. Rozi P. Research progress on chemical composition and biological activity of 4 animal bones.. Mod. food Sci. Technol. 36(05), 337–346 (2020).
  14. Rozi P. Isolation and evaluation of bioactive protein and peptide from domestic animals’ bone marrow.. Molecules 23(7), 1673 (2018).
    pmc: PMC6100344pubmed: 29987262doi: 10.3390/molecules23071673google scholar: lookup
  15. Xu S, Yang H, Shen L, Li G. Purity and yield of collagen extracted from southern catfish (Silurus meridionalis Chen) skin through improved pretreatment methods.. Int. J. Food Prop. 20(sup1), S141–S153 (2017).
    doi: 10.1080/10942912.2017.1291677google scholar: lookup
  16. Yanxing Z. Comparative analysis of methods for determination of protein content in dairy drinks.. China Food Saf. Mag. 09, 101–103 (2021).
    doi: 10.16043/j.cnki.cfs.2021.09.060google scholar: lookup
  17. Xinsen F, Xiuhua L, Kai W, Nairui H. Preparation and antioxidative activity of sheep bone hydrolysate with high yield of short peptides.. J. Shanxi Agric. Sci. 45(07), 1157–1161 (2017).
    doi: 10.3969/j.issn.1002-2481.2017.07.29google scholar: lookup
  18. Xie Z. Antioxidant and functional properties of cowhide collagen peptides.. J. Food Sci. 86(5), 1802–1818 (2021).
    pubmed: 33822356doi: 10.1111/1750-3841.15666google scholar: lookup
  19. Zedda M, Sathe V, Chakraborty P, Palombo M R, Farina V. A first comparison of bone histomorphometry in extant domestic horses (Equus caballus) and a pleistocene Indian wild horse (Equus Namadicus).. Integr. Zool. 15(6), 448–460 (2020).
    pubmed: 32297705doi: 10.1111/1749-4877.12444google scholar: lookup
  20. Isaksson H. Collagen and mineral deposition in rabbit cortical bone during maturation and growth: Effects on tissue properties.. J. Orthop. Res. 28(12), 1626–1633 (2010).
    pubmed: 20540098doi: 10.1002/jor.21186google scholar: lookup
  21. Ali A M M, Kishimura H, Benjakul S. Extraction efficiency and characteristics of acid and pepsin soluble collagens from the skin of golden carp (Probarbus jullieni) as affected by ultrasonication.. Process Biochem. 66, 237–244 (2018).
    doi: 10.1016/j.procbio.2018.01.003google scholar: lookup
  22. Lee J E, Noh S K, Kim. Effects of enzymatic- and ultrasound-assisted extraction on physicochemical and antioxidant properties of collagen hydrolysate fractions from Alaska pollack (Theragra chalcogramma) skin.. Antioxidants 11(11), 2112 (2022).
    pmc: PMC9686691pubmed: 36358484doi: 10.3390/antiox11112112google scholar: lookup
  23. Matinong A M E, Chisti Y, Pickering K L, Haverkamp R G. Collagen extraction from animal skin.. Biology 11(6), 905 (2022).
    pmc: PMC9219788pubmed: 35741426doi: 10.3390/biology11060905google scholar: lookup
  24. Vidal A R. Extraction and characterization of collagen from sheep slaughter by-products.. Waste Manag. 102, 838–846 (2020).
    pubmed: 31835061doi: 10.1016/j.wasman.2019.12.004google scholar: lookup
  25. Jie L A. Extraction and characterization of type I collagen from skin of tilapia (Oreochromis niloticus) and its potential application in biomedical scaffold material for tissue engineering.. Process Biochem. 74, 156–163 (2018).
    doi: 10.1016/j.procbio.2018.07.009google scholar: lookup
  26. Singh P, Benjakul S, Maqsood S, Kishimura H. Isolation and characterisation of collagen extracted from the skin of striped catfish (Pangasianodon Hypophthalmus).. Food Chem. 124(1), 97–105 (2011).
    doi: 10.1016/j.foodchem.2010.05.111google scholar: lookup
  27. Hazeena S H. Structural characteristics of collagen from cuttlefish skin waste extracted at optimized conditions.. Int. J. Food Prop. 25(1), 2211–2222 (2022).
    doi: 10.1080/10942912.2022.2127762google scholar: lookup
  28. Gao L L, Wang Z Y, Li Z, Zhang C, Zhang D. The characterization of acid and pepsin soluble collagen from ovine bones (Ujumuqin sheep).. J. Integr. Agric. 17(3), 704–711 (2018).
    doi: 10.1016/s2095-3119(17)61751-9google scholar: lookup
  29. Yu F. Optimization of extraction conditions and characterization of pepsin-solubilised collagen from skin of giant croaker (Nibea Japonica).. Mar. Drugs 16(1), 29 (2018).
    pmc: PMC5793077pubmed: 29342895doi: 10.3390/md16010029google scholar: lookup
  30. Ye M. Valorization of yak (Bos grunniens) bones as sources of functional ingredients.. Waste Biomass Valoriz. 12(3), 1553–1564 (2021).
    doi: 10.1007/s12649-020-01078-2google scholar: lookup
  31. Kobrina Y. Infrared spectroscopy reveals both qualitative and quantitative differences in equine subchondral bone during maturation.. J. Biomed. Opt. 15(6), 067003 (2010).
    pubmed: 21198207doi: 10.1117/1.3512177google scholar: lookup
  32. Sarin J K. Dataset on equine cartilage near infrared spectra, composition, and functional properties.. Sci. Data 6(1), 164 (2019).
    pmc: PMC6717194pubmed: 31471536doi: 10.1038/s41597-019-0170-ygoogle scholar: lookup
  33. Ferraro V. Collagen type I from bovine bone. Effect of animal age, bone anatomy and drying methodology on extraction yield, self-assembly, thermal behaviour and electrokinetic potential.. Int. J. Biol. Macromol. 97, 55–66 (2017).
    pubmed: 28038914doi: 10.1016/j.ijbiomac.2016.12.068google scholar: lookup
  34. Jiang Z, Xu Y, Su Y. Preparation process of active enzymolysis polypeptides from seahorse bone meal.. Food Sci. Nutr. 2(5), 490–499 (2014).
    pmc: PMC4237479pubmed: 25473507doi: 10.1002/fsn3.125google scholar: lookup
  35. Vidal A R. Production of collagens and protein hydrolysates with antimicrobial and antioxidant activity from sheep slaughter by-products.. Antioxidants 11(6), 1173 (2022).
    pmc: PMC9219988pubmed: 35740070doi: 10.3390/antiox11061173google scholar: lookup
  36. Beaubier S, Framboisier X, Fournier F, Galet O, Kapel R. A new approach for modelling and optimizing batch enzymatic proteolysis.. Chem. Eng. J. 405, 126871 (2021).
    doi: 10.1016/j.cej.2020.126871google scholar: lookup
  37. Wang J. Preparation and identification of novel antioxidant peptides from camel bone protein.. Food Chem. 424, 136253 (2023).
    pubmed: 37236074doi: 10.1016/j.foodchem.2023.136253google scholar: lookup
  38. Bo S, Zhang X, Wang Q. Study on extraction technology and functional activity of sika deer velvet (residue) collagen.. Adv. Eng. Res. 141, 94–100 (2017).
  39. Chen X. Antioxidant peptides from the collagen of antler ossified tissue and their protective effects against H2O2-induced oxidative damage toward HaCaT cells.. Molecules 28(19), 6887 (2023).
    pmc: PMC10574659pubmed: 37836729doi: 10.3390/molecules28196887google scholar: lookup
  40. Hernández-Ruiz K L. Collagen peptide fractions from tilapia (Oreochromis aureus Steindachner, 1864) scales: Chemical characterization and biological activity.. Food Bioscience 53, 102658 (2023).
    doi: 10.1016/j.fbio.2023.102658google scholar: lookup
  41. Shen D Y. In vitro and in vivo antioxidant activity and umami taste of peptides (< 1 kDa) from porcine bone protein extract.. Food Bioscience 40, 100901 (2021).
    doi: 10.1016/j.fbio.2021.100901google scholar: lookup
  42. Sun X. Purification and characterization of antioxidant peptides from yak (Bos grunniens) bone hydrolysates and evaluation of cellular antioxidant activity.. J. Food Sci. Technol. 58(8), 3106–3119 (2021).
    pmc: PMC8249534pubmed: 34294973doi: 10.1007/s13197-020-04814-7google scholar: lookup
  43. Kobayashi K. Direct assessments of the antioxidant effects of the novel collagen peptide on reactive oxygen species using electron spin resonance spectroscopy.. J. Pharmacol. Sci. 116(1), 97–106 (2011).
    pubmed: 21512306doi: 10.1254/jphs.10321fpgoogle scholar: lookup
  44. Zu X. Peptide extraction from silver carp (Hypophthalmichthys molitrix) scales via enzymatic hydrolysis and membrane filtration.. Ital. J. Food Sci. 35(2), 44–53 (2023).
    doi: 10.15586/ijfs.v35i2.2248google scholar: lookup
  45. Zu X Y. Physicochemical properties and biological activities of silver carp scale peptide and its nanofiltration fractions.. Front. Nutr. 8, 812443 (2021).
    pmc: PMC8765580pubmed: 35059429doi: 10.3389/fnut.2021.812443google scholar: lookup
  46. Irshad I, Kanekanian A, Peters A, Masud T. Antioxidant activity of bioactive peptides derived from bovine casein hydrolysate fractions.. J. Food Sci. Technol. 52(1), 231–239 (2015).
    doi: 10.1007/s13197-012-0920-8google scholar: lookup
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