The isoelectric point (pI) of a protein is the pH at which the protein carries no net electrical charge. For proteins like pepsin, which contain various amino acids with different acidic and basic side chains, determining the pI involves identifying the pH at which the positive and negative charges on the amino acids balance.
Given that the pH of the chyme (mixture of food, HCl, and digestive enzymes) is around 1.5, this indicates an acidic environment in the stomach.
For pepsin to have a pI lower than the chyme pH of 1.5, it must have a net positive charge at this pH. This means that the functional groups contributing to the pI of pepsin would be mostly protonated amino groups (NH₃⁺) from amino acids' side chains.
The amino acids that contribute ionizable amino groups and can influence the pI of proteins are:
1. Lysine (Lys): Lysine has an amino group that can be protonated and carry a positive charge at low pH. It has a pKa value around 10.5, which means that at low pH, the amino group is likely to be protonated.
2. Arginine (Arg): Arginine also has an amino group that can be protonated at low pH. It has a pKa value around 12.5, making it more likely to be protonated at low pH.