Catecholase Experiment

Enzymes catalyze chemical reactions by lowering the activation energy. To be more specific, the enzymes have a pocket called an active site where substrates, which are the reactants of the reaction, can bind to. Once they are bound, the complex is called an enzyme-substrate complex. The catalytic action of the enzyme converts the substrate to products by stretching, stressing, and bending bonds to break them and make it easier to get to the transition state where the molecules can form new bonds. The amount of free energy needed to go forth with the reaction decreases, as a result.

Students will be observing normal catalase reaction, the effect of temperature on enzyme activity, and the effect of pH on enzyme activity in this experiment. The enzymes will all around perform better when exposed in room temperature than when it is exposed to hot and cold temperatures. This is based on the fact that the higher the temperature, the better the enzymes will perform, but as the temperature reaches a certain high degree, the enzymes will start to denature, or lose their function.

Note that the enzyme remains unchanged so that more of the some substrates can react.

This would be a suitable independent variable as it would be easy to change ourselves. If the concentration of the substrate increases the faster the rate of reaction, as more hydrogen peroxide molecules can collide with catalase molecules, so more reactions will take place. As you increase the concentration of substrate this will continue to occur up to a point where all the active sites on the enzyme are being used.

Members of two groups had designed their experiment on the effect of temperature on catechol oxidase reactions. The graph that was interpreted for this discussion is as above (Figure 6). The independent variable for this experiment was temperature, and the dependent variable was the absorbance of benzoquinone. The first data set in Figure 6 showed that an increase in temperature resulted in a gradually higher absorbance of benzoquinone until the temperature reached 55° C in which the absorbance dramatically dropped. As the temperature went from cold ice to room temperature 55° C, the absorbance of benzoquinone also increased from 0.07 Au to 0.22 Au. This was due to the fact that higher temperature can increase the kinetic energy of particles (Reece et al., 2011). In this case, the temperature was initially cold, and the catechol substrate molecules and enzyme molecules were moving in a slow motion. These particles would collide less frequently; as a result, less absorbance of benzoquinone displayed. When the temperature increased to a room

The null hypothesis for the first experiment was that substrate concentration would have no effect on the reaction rate. It was hypothesized that the reaction rate would increase with rising substrate concentrations, until all active sites were bound. The null hypothesis for the second experiment was that temperature would not have an effect on reaction rates. It was hypothesized that until the enzyme is denatured, as temperature increased, so would the reaction rate.

To start off the experiment 25mL of water was placed into a labeled beaker and tested for the pH using pH test strips. Next the antacid tablet was placed in the solution and timed for how long it took to dissolve the tablet. Finally the temperature was measured. This same process was repeated for the acidic solution, and finally for the basic solution. After each experiment the pH, the reaction time, and the temperature of the beaker were recorded into a table. For this experiment the independent variable was the substance used (acid, neutral or base), and the dependent variable was the reaction time of each substance. The constant conditions of this experiment included the amount of substance being used, and the placing of one antacid tablet into each beaker. The experimental group was the acidic and basic solution, and the control group was the neutral

Enzymes are proteins that act as catalysts during a biochemical process. Catalysts are non-changing enzymes that can increase or decrease activation energy to accelerate or slow down a biochemical reaction without using additional energy.

As the enzyme concentration increased so too did the activity rate. The relatively level areas show where there was substrate depletion.

However, the rate of reaction only increases for a certain period of time until there is lesser substrate molecules than the enzyme molecules. The increase of enzyme concentration does not have effect if there are lesser substrate molecules than enzyme molecules initially.

Catalysis They serve as enzymatic catalysts that speed up biochemical reactions while remaining unchanged in the process. Without these biological catalysts, chemical reactions would occur so slowly that life as we know it could not exist. With them, chemical reactions can occur at rates as much as 10 billion times faster than would be possible without enzymes. Enzymes are critical to digestion and metabolism, they are required to release nutrients from foods so they can be absorbed and utilized by the body.

An enzyme is a catalyst. Catalysts are known for speeding up the rate of reactions by lowering the activation energy of the biochemical reaction. (Reece et al., 2011)

generally act as a catalase that initially bring about a chemical reaction.” Enzymes play an

Almost all enzymes need specific conditions for them to function. The conditions include temperature, pH level, and concentration of salt. Enzymes have optimal conditions. If they are changed, the enzyme may denature and deactivate. If that happens, the enzyme would not be able to catalyze the reaction, and the reaction rate would decrease (Worthington 2010).

The hypothesis is as the substrate concentration has an increase so will the reaction of velocity if the amount of enzyme is kept constant.