Preparation and tissue structure analysis of horse bone collagen peptide

Abstract

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.

Keywords

• Mongolian horse bones
• Hard tissue section
• Ultra-high pressure
• Collagen peptide
• Antioxidant activity