Interactions between acid and proteins under in vitro gastric condition - a theoretical and experimental quantification.

The gastric digestion of proteins is influenced by the pH and the gastric pH fluctuates after food consumption. However, the dynamics of gastric pH still need to be quantitatively understood. Proteins in food strongly influences the gastric pH. Therefore, we studied the interaction between acid and proteins, including the buffer reaction and the acid diffusion in protein gels. The buffer capacity of proteins stems from its content of ionizable amino acid side groups. Based on this, we set up a model and method to parameterize the buffer capacity of proteins. Moreover, the liberated carboxyl and amino groups during enzymatic hydrolysis of protein can also contribute to the buffer capacity. While we expected protons to diffuse faster than pepsin, we found that the penetration distance of acid is comparable to that of pepsin. The buffer reaction caused the acid to concentrate tenfold in the gel compared to the bulk acid concentration. Therefore, we postulated that the buffer reaction reduces acid diffusivity in gels.