Evolution of conformation and thermal properties of bovine hides collagen in the sodium sulphide solution

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Conformations of secondary and super secondary structure from bovine hides collagen are very important for constructing collagen molecular space structure, and directly related to its properties. In this work, the evolutional mechanism of the collagen conformation in the environment of sodium sulphide (Na2S) solution is periodically studied by FT-IR spectroscopy, the Gaussian peak fitting of secondary derivative, and auxiliary methods such as SDS-PAGE, SEM and TG. As a result, the three polypeptide chains structure of bovine hide collagen was hardly affected by the ions of OH−, HS− and S2−. The conformation of collagen molecules such as β-turn, triple helix and β-strand were gradually evolved into unordered structure and α-helix with the sequential addition of OH−, HS− and S2−, which is because the hydrogen bond inside collagen molecular is extended or opened with the increase of the synergistic effect of pH and reducibility of HS− and S2− in the solution. The bound water content and thermal properties of the treated collagen molecules are decreased. Finally, the order of the hydrolysis ability to collagen is NaOH < NaHS < Na2S at the same condition, which was confirmed by measuring the content of hydroxyproline from their solutions after treating the collagen. This work provides very important information for understanding the evolutional mechanism of bovine hide collagen conformation in the Na2S solution, developing the alternatives of sulfide, extraction of collagen, tanning, and application of collagen in biological and material science.