La pepsina es una enzima digestiva que se secreta en el estómago y que hidroliza las proteína en el estómago; las otras enzimas digestivas importantes son la tripsina y la quimotripsina. Fue la primera enzima animal en ser descubierta, por Theodor Schwann en 1836. La pepsina es producida por las células principales de las glándulas gástricas como una proenzima, el pepsinógeno, quien por efecto del pH ácido se hidroliza y adquiere su capacidad enzimática. Actúa principalmente sobre enlaces peptídicos de naturaleza hidrófoba, preferentemente aromáticos. La pepsina es más activa con un pH de entre 2 y 3. Se desactiva permanentemente con un pH superior a 5. Interactúa con las uniones Phe-Phe y Phe-Tyr.

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Pepsin is an enzyme that breaks down proteins into smaller peptides (that is, a protease). It is produced in the stomach and is one of the main digestive enzymes in the digestive systems of humans and many other animals, where it helps digest the proteins in food. It is one of three principal proteases in the human digestive system, the other two being chymotrypsin and trypsin. During the process of digestion, these enzymes, each of which is specialized in severing links between particular types of amino acids, collaborate to break down dietary proteins into their components, i.e., peptides and amino acids, which can be readily absorbed by the small intestine. Pepsin is most efficient in cleaving peptide bonds between hydrophobic and preferably aromatic amino acids such as phenylalanine, tryptophan, and tyrosine. Pepsin's proenzyme, pepsinogen, is released by the chief cells in the stomach wall, and upon mixing with the hydrochloric acid of the gastric juice, pepsinogen activates to become pepsin. Pepsin is an aspartic protease, using a catalytic aspartate in its active site.

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