Most enzymes are highly specific. This means that most of the time a single enzyme molecule will catalyst only one chemical reaction. For an enzymatic reaction to occur, an enzyme binds to a substrate causing an enzyme-substrate complex. Cathode is a naturally occurring compound found in many vegetables and fruits. When different substrates (Cathode, Resorcinol, and Hydrogenous) are added to a solution, the rate of the enzymatic reaction will gradually change. Cathode oxides reacts with the substrates Cathode, Resorcinol, and Hydrogenous to form a Bounciness, which is the product.
A simplified version of the reaction can be written: The substrates in the experiment are the reacting molecules. The only difference between the Cathode, Resorcinol and Hydrogenous is that they differ in the relative positions of the hydroxyl group. When the reaction takes place, the color of bounciness will be yellowish-brown. The more a product is colored, the more light it will absorb at specific wavelengths: Beer’s Law. It was hypothesized that when different substrates are added to a solution, the rate of the enzymatic reaction will change.
If this is true, then as time increases, the rate of the reaction of enzymatic activity will gradually change due to the direct relationship between absorbency and concentration. The purpose of this experiment was to determine the change of enzymatic reaction by adding different substrates to the solution. The null hypothesis is that when substrates Cathode, Resorcinol, and Hydrogenous are added to the solution, the rate of the enzymatic reaction will not change. The alternative hypothesis is that when substrates Cathode, Resorcinol, and Hydrogenous are added to the solution, the rate of the enzymatic reaction will change.
Results: The change of reaction rate was determined by addition of different substrates (Cathode, Hydrogenous, and Resorcinol). The concentration of Cathode increased as the time increased. The concentration for Resorcinol decreased as time increased. In addition, the concentration of Hydrogenous remained fairly constant as time began to increase. The change in concentration does support the hypothesis because the rate of the reaction changes for the substrates as time increases. One factor why Resorcinol and Hydrogenous enzymatic activity creased was the dilution of the enzyme or substrate.
As the gap for the starting time to ending time gets longer, the concentration for Cathode, on the other hand, gradually increases; therefore, increasing the rate of the enzymatic reaction. Conclusion: After analyzing the results, the null hypothesis was rejected because the rate of enzymatic reaction changed when the different substrates were added to the solution. Even though the rate of enzymatic reaction for Resorcinol and Hydrogenous did not greatly increase as Cathode, it did not remain the same.