Abstract
Abstract
Collagen, as a thermal-sensitive protein, is the most abundant structural protein in animals. Native collagen has been widely applied in various fields due to its specific physicochemical and biological properties. The beneficial properties would disappear with the collapse of the unique triple helical structure during heating. Understanding thermal stability of collagen is of great significance for practical applications. Previous studies have shown the thermal stability would be affected by the different sources, extraction methods, solvent systems in vitro and modified methods. Accordingly, the factors affecting thermal stability of collagen are discussed in detail in this review.
Graphical abstract
Publisher
Springer Science and Business Media LLC
Reference235 articles.
1. Li ZQ, Liao LL. The chemistry and histology of animal skins. China: China Leather Industry Press; 2010.
2. Avery NC, Bailey AJ. The effects of the Maillard reaction on the physical properties and cell interactions of collagen. Pathol Biol. 2006;54:387–95.
3. Gelse K. Collagens-structure, function, and biosynthesis. Adv Drug Deliv Rev. 2003;55:1531–46.
4. Jiang TD. Collagen and collagen protein. China: Chemical Industry Press; 2006.
5. Ricard-Blum S. The collagen family. Cold Spring Harb Perspect Biol. 2010;3:1.
Cited by
67 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献