PH of Catalase Vs. Pepsin
- Pepsin breaks up proteins from the food you eat into shorter chains of amino acids as part of digestion. Catalase breaks hydrogen dioxide down into water and oxygen molecules. Hydrogen peroxide is a byproduct of certain cellular processes but it is highly reactive and can damage important molecules like DNA; by rapidly eliminating hydrogen peroxide, catalase helps to ensure that it doesn't accumulate.
- A pH of 2 is optimal for pepsin. If the pH level exceeds 7, pepsin will become denatured or lose its structure; above pH 5, it will cease to function. The pH in the stomach is typically close to 2, so conditions here are ideal for the enzyme. Catalase, on the other hand, functions best in the 6.8 to 7.5 pH range, and its optimal pH is 7.
- The body uses pH to ensure that pepsin doesn't become active until it's been exported from the cell--otherwise it would start to digest the cells that manufacture it. Pepsin is originally produced in an inactive form called pepsinogen. Once it's released from the cell into the stomach, the low pH causes pepsinogen to unfold, cleave itself and adopt its active configuration. Unlike pepsin, catalase is produced in an environment where the pH is already within its optimal range, so it doesn't need to change its configuration to become active.
