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Updated: Sep 15, 2025

An Improved Method for the Preparation of Type I Collagen From Skin
Published on: January 21, 2014
Insights into microstructure, physicochemical characteristics and functional properties of collagen extracted from
Ming Zhu1,2, Shaobo Li1, Li Chen1
1Key Laboratory of Agro-Products Quality and Safety Control in Storage and Transport Process, Ministry of Agriculture and Rural Affairs, Beijing, China.
Background:
Aiming to systematically assess the functional properties of collagen from livestock by-products, the present study examined the rheological properties, thermal stability and microstructure of collagen extracted from sheep, pig, cow and donkey skins.
Results:
Sheep skin collagen exhibited a gel strength of 446.71 g, which was 2.47 times higher than that of donkey skin collagen. Differential scanning calorimetry revealed sheep skin collagen's denaturation temperature (109.61 °C) exceeded that of pig (87.92 °C), cow (62.14 °C) and donkey (96.46 °C) collagen, indicating superior thermal stability. Amino acid analysis showed sheep skin collagen contained elevated proline (176.32 g kg-1) and hydroxyproline (190.50 g kg-1) levels, reinforcing its triple-helical structure. Scanning electron microscopy confirmed sheep skin collagen's dense, interconnected fibrillar network, correlating with enhanced mechanical integrity.
Conclusion:
Sheep skin collagen exhibits exceptional physicochemical properties, making it a promising material for gel-based foods (e.g. confectionery, meat analogs) and biodegradable packaging. These findings support the sustainable utilization of livestock by-products, aligning with circular economy principles. © 2025 Society of Chemical Industry.
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