Protein solubility, secondary structure and microstructure changes in two types of undenatured type II collagen under different gastrointestinal digestion conditions

Sodium dodecyl sulfonate polyacrylamide gel electrophoresis (SDS-PAGE), circular dichroism spectroscopy (CD), transmission electron microscope (TEM) and atomic force microscope (AFM) were used to analyze the structural properties and gastrointestinal digestive characteristics of natural insoluble undenatured type II collagen (IC II) and pepsin soluble undenatured type II collagen (SC II). Results showed that, after gastric digestion, especially under low pH conditions, some thick and short collagen fibers were dissolved from IC II, which was accompanied by the release of soluble protein with triple helix structure. As to SC II, when gastric digestion was performed under higher pH conditions, collagen fibers were mildly thinned and curved, and the triple helix structure was slightly destroyed. However, those changes hardly occurred during the intestinal digestion. Moreover, the undenatured type II collagen existing in SC II digestive supernatant was 1.2-12.4 times higher than that of IC II depending on the pH conditions. These results suggested that, it is more likely for SC II to exert its activity of relieving arthritis, and it should be taken when the pH of gastric environment is high.

Automated summary

IC II dissolves thick collagen fibers and releases soluble protein with triple helix structure under low pH gastric digestion, while SC II shows mild thinning and slight destruction of triple helix structure under higher pH gastric digestion, with minimal changes during intestinal digestion. The undenatured type II collagen content in SC II is higher than in IC II, suggesting that SC II is more likely to relieve arthritis when taken in high pH gastric environment.