In this video, we're going to talk about optimal enzyme conditions. It turns out that proper enzyme catalysis requires a very specific set of conditions, including a very specific pH and a very specific temperature. Moving forward, we're first going to focus on optimal pH, and then later in our next video, we'll focus on the optimal temperature. We know that most enzymes have an optimal pH that allows them to display their greatest amount of activity. Most enzymes are proteins, and both enzymes and proteins are sensitive to pH; different enzymes have their own optimal pH. Why are enzymes sensitive to the pH? Recall from our previous lesson videos that the charges of ionizable amino acids actually vary with pH. pH changes could cause active site amino acids to change their charges. The charges of amino acids in the active site could potentially be super important for enzyme catalysis. If we change those charges, then we could potentially hinder enzyme catalysis. Later in our course, we'll talk more about enzyme catalysis when we discuss different types of enzyme catalysis. For now, all you need to know is that the charges of amino acids are not only potentially important for enzyme catalysis but also for maintaining protein structure, specifically the tertiary and quaternary structure. By changing the pH significantly enough, that could cause the enzyme to denature. If we denature the entire enzyme, enzyme catalysis will definitely be hindered.
In our example below, it's asking us, what is the approximate optimal pH for pepsin and for chymotrypsin? Pepsin's curve is in black, and chymotrypsin's curve is in pink. Starting with pepsin, its optimal pH is where it displays the greatest amount of activity. We have enzyme activity on the y-axis and the pH on the x-axis. What do you think? The optimal pH for pepsin is right where it displays its optimal activity, corresponding with the x-axis where it has the highest peak. That looks to be about 1.5. Now, if we do the same for chymotrypsin, it's going to be right where it displays its highest amount of activity, corresponding with the x-axis just above 8, so it's about 8. That is the optimal pH of pepsin and the optimal pH of chymotrypsin. Pepsin is typically found in the stomach where the pH is super acidic, about 2. Pepsin is going to be very active in the stomach. Chymotrypsin is found more so in the small intestine where the pH is a little higher, allowing it to operate better in those conditions.
This concludes our lesson on optimal pH, and in our next lesson video, we'll talk about optimal temperatures. I'll see you there.