Votorx said:
On the molecular level, why and how does the ph level effect enzymatic activities?
By the bazillions, our body builds big molecules out of little ones, and it breaks big ones into little ones. There are ideal temperatures in which these reactions happen. If you get too cold, then these reactions happen slower. If you get too hot, then the molecules sort of unravel and just do not want to cooperate. In the middle, 37 degrees Celsius, or 98.6 Fahrenheit, the temperature is just right and these reactions can go both ways. Enzymes are molecules that tell the other molecules which way to go.
The ph concentration needs the same sort of balance. If the solution is too acid, meaning that there are too many free protons (H+), then some of the chemical reactions will not take place. If the solution is too alkaline, meaning too many hydroxyl ions (OH-), then again, some of the reactions will not happen.
The enzyme is a biological catalyst. Technically, it lowers the activation energy needed for a reaction. The idea is that before a reaction takes place, you first have to pump some energy into the reactants before they will combine. The act of combining may consume or release energy. It can even release much more energy than the activation energy needed to get it started. However, without first supplying the activation energy, the reaction will not take place. With a catalyst, that enzyme, the reactants do not need as much activation energy, so the reactions happen more often.
The catalyst or enzyme is changed in the reaction, but reverts to its original shape immediately afterwards. The net result is that the enzyme does not change because of the reaction. It just stays the same, ready to speed up another reaction. If the solution containing the enzyme and reactants has the wrong ph, then the enzyme, or the reactants, bind to free protons or hydroxyl ions instead of each other. The result is that the reaction slows or does not happen at all.