The Importance Of Enzyme Kinetics

Enzymes are known as catalysts that cause reactions to occur more rapidly by lowering the reaction’s activation energy. A reaction’s activation energy is known as the minimum amount of energy required to get a chemical reaction started1. In order for cells to efficiently manage thousands of different chemical reactions, they make use of biological catalysts. Without these catalysts, biological reactions would not be able to proceed at a proper rate necessary to maintain life. Most, but not all, catalysts are made up of proteins that increase the rate of reactions within a system. Like most proteins, structure determines function. Therefore, the functionality of a catalyst depends heavily on how the proteins are folded2.
Enzyme kinetics is known as the study of how biological catalysts are able to increase the rate at which reactions are performed. Reaction rates are typically measured as the amount of products produced per unit of time for a single given concentration3. Enzyme kinetics can be affected by the concentration of the substrate, the presence of inhibitors, as well as changes in temperature, and in pH. A substrate is known as the substance that is catalyzed by an enzyme2. An increase in substrate concentration leads to an increase in product formation due to a greater amount of collisions between both the substrate and the enzyme molecules. This remains true until the enzyme becomes saturated with substrate molecules. At this point, the reaction rate is occurring at its max velocity and an increase in substrate concentration from this point on will have no effect on the saturated enzyme. Changes in temperature determine whether or not the collisions between enzyme and substrate molecules will increase or decrease. A decrease in temperature will lead to fewer collisions, therefore causing the reaction to occur at a slower rate. An increase in temperature will create more rapid and frequent collisions, thus increasing the rate of the reaction. A dramatic change in temperature can change the shape of the enzyme, thus denaturing the enzyme and rendering it useless. PH levels also have an effect on enzymatic activity since high and low pH values can lead to a loss of enzymatic activity while an optimum pH value is one where the enzyme is most active4. The presence of inhibitors effect enzymatic activity by either blocking off the active site of an enzyme or by changing the shape of the active site. Competitive inhibitors compete with the substrates for the active site of an enzyme and once bound to the active site, it prevents the substrates from binding and inhibits any reaction from occurring. Non-competitive inhibitors bind to the allosteric site of an enzyme and changes the shape of the active site, therefore not allowing the catalysis of a reaction since the substrates can no longer bind to that altered active site2. In this experiment, different amounts of the enzyme glucose oxidase (GOx) were used in order to test whether or not enzymatic activity …show more content…
An increase in the amount of GOx used leads to an increase in the GOx concentration in each different mixture. GOx is known to be a stable enzyme that oxidizes glucose into glucolactone while also converting oxygen into hydrogen peroxide5. The function of the GOx enzyme is mainly centered around the hydrogen peroxide production since hydrogen peroxide can be used to kill bacteria. For example, GOx is found on the surfaces of many fungi in order to protect against bacterial infections and is also found in honey, acting as a