Catechol Oxidase: Competitive And Noncompetitive En

Enzymes are biological catalysts. Catalysts can increase the rate of reaction and remain unchanged by the reaction. In addition, enzymes are considered proteins. Because of the protein structure, enzymes are only allowed a limited number of reactions(Schultz, 2006). Enzymes reduce the activation energy required under ideal conditions. Extremes of the pH or high temperature can cause a stable enzyme to unfold and loosen up its shape or cause denaturing, destruction of enzyme properties and structure(Schultz, 2006). The substrate won’t bind with the enzyme if the shape is altered which is known as an inhibition. Inhibitors can slow down the reaction rate in two ways: competitive and noncompetitive inhibition. In this experiment, what is investigated …show more content…
The enzyme catechol oxidase is found in plants known as polyphenoloxidase and in animals it is called tyrosinase(Schultz, 2006). The catechol oxidase is extracted from the potato. This enzyme is capable of catalyzing the oxidation of catechol substrate into the products of ortho-quinone and water. Ortho can also be found in substances as a brownish color; for example, the browning in cut apples represents the oxidation of the catechol to ortho-quinone (Schultz, 2006) The brown coloring is what helps to determine the concentration of the enzymes in the prepared dilutions. The purpose of the enzyme being added to the solutions made in each part was to observe how the enzyme changed the effect of the reaction rate by its absorbance speeding up the reaction. Since it is known that the enzyme will increase the rate of reaction it is supposed that in every part of this experiment, the reaction rate will rapidly increase but will end up leveling off. In Part 1 there’s expected to see an obvious decrease in the enzyme activity due to pure dilution. Part 2 and 3 were the continuous dilution which should show the leveling off of the reaction rate due to the amount of enzyme and substrate