An Investigation on the Rate of Reaction of the Enzyme Catalase on the Substrate Hydrogen Peroxide.

The hypothesis is that catalase activity will increase exponentially with higher concentrations of hydrogen peroxide until all catalase active sites are filled, in which case the

We used apple, potato, and chicken liver to prove that not only beef liver contains catalase. The group conducted three experiments: one contained potato and H2O2, another had apple and H2O2, and the last had chicken liver and H2O2. We added 2mL of hydrogen peroxide (H2O2) to all three test tubes. The bubbling effect proved that all three had catalase in them. We realized that the more the substance bubbled the more catalase it contained, and that the less it bubbled, the less catalase there was. We also rated the reactions by the speed of the reaction in seconds, like we learned in part

Hypothesis: If the concentration of the substrate is increased, then the rate of enzyme activity will decrease. This is because as the concentration of the substrate increases, there is an increasing amount of occupied active sites at any given moment. This will cause a decrease in the rate of enzyme activity as substrate-active site collisions are increasingly slowed down thus bringing down the rate of enzyme activity.

An enzyme is a protein macromolecule which acts as a catalyst, an agent which speeds up reactions without being consumed by it. They are vital to life; cellular chemical reactions would not occur fast enough to support life, without the aid of enzymes. They do this by lowering the activation energy (EA), which is the energy that must be added to the reactants at the start of reactions, it has to be reached in order for the reaction to occur (Reece, Wasserman and Urry). There are hundreds of enzymes known, but not all cells contain the same ones, an example of this is catalase which will be the experimental enzyme in the lab.

Substrate concentration also affects the rate of reaction as the greater the substrate concentration the faster the rate of reaction and all the active sites are filled. At this point the rate of reaction can only be increased if you add more enzymes in to make more active sites available.

The purpose of this investigation is to discover the effect of pH on the activity of catalase, an enzyme which plays the integral role of converting hydrogen peroxide into water and oxygen, and discover which pH level it will work at the most efficient rate (the optimum). The original hypothesis states that that the optimum would be at a pH is 7, due to the liver, where catalase usually resides, being neutral. The experiment consists of introducing the catalase to hydrogen peroxide, after exposure to certain solutions; hydrogen peroxide, water and hydrochloric acids, all containing the adjusted pH, and measuring the height of froth formed, an observable representation of the activity of the enzyme. The final data indicated that

How does changing the substrate concentration affect the rate of a catalase reaction in an enzyme? Hydrogen peroxide was used as the substrate and the rate was measured by oxygen production.

The purpose of this experiment was to analyze the effects of substrate concentration and temperature on activity of catalase. The activity was measured by observing the amount of time it took for 10 mL of oxygen to evolve as an outcome of the catalyzed breakdown of hydrogen peroxide. Increased temperature and substrate concentration will both effect the activity of a catalase enzyme. We used 4 different temperatures of an enzyme, as well as a variety of scientific materials. The results of this experiment confirmed the hypothesis that was tested.

As we study biomolecules, the subject of how do enzymes work comes up. The reasoning behind the catalase enzyme lab was to see how enzymes break down compounds. My objective being to see how the catalase enzyme will react to liver, potato and apple. We will also use a base or acid to see how these factors will affect the independent variable. My hypothesis is the liver and potato will react to the peroxide but the apple will not.

The purpose of this experiment was to record catalase enzyme activity with different temperatures and substrate concentrations. It was hypothesized that, until all active sites were bound, as the substrate concentration increased, the reaction rate would increase. The first experiment consisted of five different substrate concentrations, 0.8%, 0.4%, 0.2%, 0.1%, and 0% H2O2. The second experiment was completed using 0.8% substrate concentration and four different temperatures of enzymes ranging from cold to boiled. It was hypothesized that as the temperature increased, the reaction rate would increase. This would occur until the enzyme was denatured. The results from the two experiments show that the more substrate concentration,

Concentration: when the concentration of the substrates is increased, they are more likely to collide to an enzyme. This increases the rate of reaction as collisions are happening at a faster rate. However, due to the increased substrate concentration there are less free enzymes available to bind with which would stop effecting the rate

Enzymes are natural catalysts that work from the ability to increase the rate of reaction by decreasing the activation energy of a reaction. (Blanco, Blanco 2017) An enzyme can do this 10^8- to 10^10 fold, sometimes even 10^15 fold. (Malacinsk, Freifelder 1998) The substrate will momentarily bind with the enzyme making the enzyme-substrate complex, of which the shape of the substrate is complimentary to the shape of the active site on the enzyme it is binding with. There are two main theories as to how an enzymes and substrates interact, the lock-and-key model and induced fit theory. The lock-and-key model suggests that the enzyme has a specific shape that fits the substrate and only that substrate. The induced fit theory says the active site and substrate are able to change shape or distort for the reaction to take place with (Cooper,

In the catalase activity there were three different procedures that led to the results that will be discussed. In the first procedure as you can see in table 1, a catalase was used to test what would occur to it when hydrogen peroxide is added. In this particular lab, potatoes were used as the catalase since they’re already buffered at pH 7.4, which will show better results than using any other catalase buffered at pH 7.0. The potato would speed up the breakdown of the hydrogen peroxide, this would result in the water and oxygen molecules being released (Mader, 2013). The cause of the oxygen molecules being released is that bubbling will begin to occur from the result of the hydrogen peroxide breaking apart (Mader, 2013). This explains why bubbles appear after a slice of potato was placed inside the test tube

Catalase breakdown hydrogen peroxide into water and oxygen. This experiment was to test the reaction on catalytic activity

BACKGROUND: Catalase (the enzyme) is found in yeast, it breaks down hydrogen peroxide (the substrate) into water and oxygen according to this equation. 2H2O2(aq) -------------------> 2H2O(l) + O2(g) + catalase(aq) One molecule of catalase can break 40 million molecules of hydrogen peroxide each second. Factors that affect the rate of reaction § Increasing the temperature increases the kinetic energy at which the enzyme and substrate collide.