Why doesn't boiled pepsin break down gelatin?

Answer 1

Gelatin is almost entirely protein. As pepsin is a protease, its job is to facilitate the break down of protein into amino acids. When the enzyme is boiled, it becomes denatured, which prevents it binding to the substrate. As a result of this, the digestion of gelatin cannot take place, so the digestion of gelatin ceases.

Answer 2

the enzymes break down the protein chains usually formed by gelatin as it chills into a solid shape. therefore, the gelatin cannot solidify

Answer 3

Pepsin is an enzyme- so bioling it will denature the active site, meaning it will not fit the substrate's active site, so it will not break anything down.