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Fibril-associated Collagen

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...

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Updated: Jan 13, 2026

An Improved Method for the Preparation of Type I Collagen From Skin

An Improved Method for the Preparation of Type I Collagen From Skin

Published on: January 21, 2014

Collagen from Bovine Omentum: Extraction and Characterization.

Ajay Mittal¹, Catherine Collins², Lena Madden²

¹UCD Institute of Food and Health, University College Dublin, Belfield Campus, D04 V1W8 Dublin, Ireland.

Foods (Basel, Switzerland)

|January 10, 2026

Summary

This summary is machine-generated.

Bovine omentum is a viable source for extracting acid-soluble collagen (ASC) and enzyme-extracted collagen. These collagens retain their structure and show good emulsifying properties, making them suitable for the food industry.

Keywords:

Protana® Prime acid-soluble collagen bovine omentum collagen characterization techno-functional properties

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Area of Science:

Biochemistry
Food Science
Circular Bioeconomy

Background:

Bovine omentum, a beef processing byproduct, is rich in lipids and proteins, including collagen.
Collagen recovery from this source aligns with circular bioeconomy principles.
The potential of bovine omentum as a collagen source requires investigation.

Purpose of the Study:

To isolate and characterize collagen from bovine omentum using acid-based and enzymatic methods.
To evaluate the yield, solubility, and functional properties of extracted collagens.
To confirm the structural integrity and type of collagen obtained.

Main Methods:

Acid extraction to obtain acid-soluble collagen (ASC).
Enzymatic extraction using Protana® Prime on ASC residue.
Solubility tests at varying pH and NaCl concentrations.
Analysis of emulsifying activity and stability.
Fourier-transform infrared (FTIR) spectroscopy and SDS-PAGE for structural and type identification.

Main Results:

ASC extraction yielded 3.98%; enzymatic extraction yielded 4.98%–11.15%.
Maximum collagen solubility occurred at pH 3; high NaCl reduced solubility.
ASC exhibited superior emulsifying activity and stability compared to enzyme-extracted collagens.
FTIR and SDS-PAGE confirmed the presence of type I collagen with intact triple helix structure.

Conclusions:

Bovine omentum is a valuable alternative source for collagen extraction.
Extracted collagens, particularly ASC, possess favorable functional properties for food applications.
This study supports the utilization of bovine omentum in the circular bioeconomy for collagen production.