Factors affecting thermal stability of collagen from the aspects of extraction, processing and modification

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.

Study of the Efficiency of Squeezing Moisture-Saturated Products

“…The analysis and study of the structure and properties of collagens in semi-finished leather after liquid processing with chemical additives are given in [5,6].…”

Experimental dehydration of wet fibrous materials

“…The study in [1] describes the current trend in applying vegetable tanning technology and wet processing methods based on new solvents, ionic and other liquids when solving the problem of using chromium in the leather industry. In [2][3][4][5][6][7][8][9][10][11], the influence of the technology of liquid, chemical, and mechanical treatment on the properties of leather collagens and its deformation and filtration parameters was studied. In [12], a review of 39 peer-reviewed articles in English devoted to the study of leather processing is given, of which 30 articles were published in the last 6 years.…”

Thermally stable collagen from Piranha and Rohu with improved physical, biochemical, and morphological properties

“…Hydrogen bonds in Gly‐X‐Y (Glycine‐Proline‐Hydroxyproline) collagen backbone, peptide backbone, hydrogen bond in the water moiety, inter‐molecular weak van der Waals interactions, electrostatic forces and stronger hydrophobic interactions between the aminoacids in cumulus contribute to stabilize the α‐helix in the triple helical conformation and maintain structural integrity 26 . A slight increase in heat above the threshold limit could disrupt these bonds and cause conformational change in the protein decreasing the thermal stability 25 . To increase the thermal stability, cross‐linking agents are employed to achieve the required applications 27…”

“…23,24 Triple helical conformation of the collagen accords to the self-assembly, fibril forming ability, biocompatibility, tissue engineering and regeneration applications, food, pharma and cosmetic applications. 25 Hydrogen bonds in Gly-X-Y (Glycine-Proline-Hydroxyproline) collagen backbone, peptide backbone, hydrogen bond in the water moiety, inter-molecular weak van der Waals interactions, electrostatic forces and stronger hydrophobic interactions between the aminoacids in cumulus contribute to stabilize the α-helix in the triple helical conformation and maintain structural integrity. 26 A slight increase in heat above the threshold limit could disrupt these bonds and cause conformational change in the protein decreasing the thermal stability.…”

“…26 A slight increase in heat above the threshold limit could disrupt these bonds and cause conformational change in the protein decreasing the thermal stability. 25 To increase the thermal stability, cross-linking agents are employed to achieve the required applications. 27 Thermal stability of collagen from freshwater sources is better than the marine sources due to high intermolecular cross-links and relative abundance of imino acids.…”