# Collagen from Bovine Omentum: Extraction and Characterization

**Authors:** Ajay Mittal, Catherine Collins, Lena Madden, Nigel Brunton

PMC · DOI: 10.3390/foods15010044 · Foods · 2025-12-23

## TL;DR

This study shows that collagen can be extracted from bovine omentum, a by-product of beef processing, and could be used in the food industry.

## Contribution

The study demonstrates a new method for extracting collagen from bovine omentum with potential industrial applications.

## Key findings

- Acid-soluble collagen was extracted with a yield of 3.98%.
- Enzymatic extraction using Protana® Prime produced collagen yields between 4.98% and 11.15%.
- All collagen samples maintained the triple helical structure and contained type I collagen.

## Abstract

Bovine omentum, a by-product of beef processing, offers potential for collagen recovery within the circular bioeconomy. It consists mainly of lipids (42.14%) and proteins (18.79%), such as collagen. In this study, collagen was isolated using acid-based and enzymatic methods. Acid-soluble collagen (ASC) was successfully extracted, yielding 3.98%. Additionally, enzymatic extraction of collagen from the residue obtained after ASC extraction using Protana® Prime (1–10%, w/w) resulted in variable yields (4.98% to 11.15%) (p < 0.05). The maximum solubility of all collagen samples was observed at pH 3, while NaCl concentrations above 4% (w/v) significantly reduced solubility (p < 0.05). ASC demonstrated the highest emulsifying activity index and emulsion stability index (213.73 m2/g and 172.09 min, respectively) (p < 0.05), whereas enzyme-extracted collagens exhibited comparatively lower emulsifying capacities, particularly at higher enzyme concentrations (7.5% and 10%). FTIR spectra revealed characteristic bands for collagen, indicating that the triple helical structure was maintained, irrespective of treatment. All collagen samples contained glycine as the major amino acid (approximately 1/3rd of the total amino acid) with proline and hydroxyproline. SDS-PAGE identified type I collagen, which consisted of αI and αII chains. Therefore, bovine omentum would be an alternative source of collagen for various applications in the food industry.

## Linked entities

- **Proteins:** COL3A1 (collagen type III alpha 1 chain), AI (beta-fructosidase), NLRP3 (NLR family pyrin domain containing 3)
- **Chemicals:** NaCl (PubChem CID 5234)

## Full-text entities

- **Chemicals:** glycine (MESH:D005998), proline (MESH:D011392), hydroxyproline (MESH:D006909), SDS (MESH:D012967), NaCl (MESH:D012965), lipids (MESH:D008055)
- **Species:** Bos taurus (bovine, species) [taxon 9913]

## Full text

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## Figures

3 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12785756/full.md

## References

53 references — full list in the complete paper: https://tomesphere.com/paper/PMC12785756/full.md

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Source: https://tomesphere.com/paper/PMC12785756