An enzyme is a catalytic protein, meaning it has unique 3D conformation with a unique sequence of amino acids.

This structure gives every type of enzyme an active sites, which are an area or groove for a substrate (molecule to be broken down by the enzyme) to attach to. If the substrate cannot fit into the active site, the reaction does not occur. The substrate is held in the enzymes active site by weak hydrogen and ionic bonds. The enzyme speeds up the chemical reaction by lowering the amount of activation energy needed. Reactions require a small number of enzymes to catalyze a reaction because enzymes can be reused numerous times. The substrate and enzyme dynamic works either like a lock and key or an induced fit. In the lock and key formation, the substrate fits in the active site perfectly. However, not all substrates naturally fit into an active site. The induced fit model describes a situation whereas the enzyme- substrate-complex does not fit perfectly but the substrate can still fit well enough to cause a strain on its chemical bonds. Specificity refers to the ability of a substrate to fit into a specific active site. When there is no specificity, the enzyme wont catalyze the reaction. .To investigate the influence of temperature on the activity of an enzyme, I would use catalase and my enzyme and hydrogen peroxide (H2O2) as my substrate. The independent variable would be the temperature increments and the dependent variable would be the intensity of the reaction, or basically how much foam is formed once the catalase and H2O2 come into contact. Materials for this experiment would include: raw potatoes because it contains catalase, ten test tubes, a graduated cylinder for measuring the H2O2, a thermometer, a knife to cut the potatoes, a hot plate, ice, liquid water, test tube rack, and ten beakers. First, label the ten test tubes and place them in the test tube rack. Then use the knife to cut ten small and congruent chunks of the potato; then place each piece in a test tube. After, fill up each beaker with liquid water. Each beaker should differ in temperature by increments of ten going from zero degrees Celsius to one-hundred. The water can be made colder by adding ice and warmer by adding boiling water which can be made using the hot plate. Once each beaker is set to the right incremented temperature, place one test tube in each beaker. Then after two minutes, fill up the graduated cylinder with 2ml of hydrogen peroxide and add it to the first test tube. The intensity of this reaction including how much it bubbles should be recorded. Then, refill the graduated cylinder with another 2ml of hydrogen peroxide and repeat this process ten times until all ten test tubes have had a reaction in them and the reactions have been recorded. The data from this experiment could be graphed afterwards to show the influence of temperature on the activity levels of an enzyme. The x-axis could be titled temperature and the y-axis could be titled intensity of the reaction in which it would measure how high the bubbles came up in the test tube during the reaction. Every enzyme has an optimal temperature, which is where the most kinetic energy can be given by heat to the solution the enzyme and substrate are in without denaturing the enzyme. As the temperature increases, the substrate collides with the enzyme more frequently; thus, the reaction time will lessen. However, too high of a temperature will disturb the bonds that

stabilize and maintain the enzymes conformation. The enzyme, catalase, / used in the experiment mentioned above has an optimum temperature of about forty degrees Celsius. If the experiment was carried out, high temperatures such as the beaker with boiling water (100C) would have no reaction occur because the enzyme would be denatured from the heat and the active site would not fit with the substrate anymore.