Enzyme Catalase Essay

The scientific purpose of this experiment was to examine the rate of enzyme activity of a potato catalase when mixing 2.5 ml of potato catalyst with either 2.5 ml of H2O, 2.5 ml of 5% salt concentration, 2.5 ml of 15% salt concentration, or 2.5 ml of 30% salt concentration. It was hypothesized that the higher the concentration of salt each catalysts solution contained, the rate of enzyme activity would decrease when applied to hydrogen peroxide. This was tested by measuring (up to 240 seconds) in

Andra Larade Bio 30 B7 11/20/15 Liver Enzyme Lab The Effect of pH and Temperature on the Efficiency of Catalase Abstract: In order to determine how pH and temperature affect the liver enzyme catalase, an experiment was conducted. Catalase breaks apart hydrogen peroxide producing water and oxygen. Using an O2 sensor to measure how much additional oxygen is added into a sealed Nalgene bottle, we could determine the enzymes effectiveness. Three variations of temperature were tested: cold, hot and

Catalase lab background The question being answered by these experiments is: How do different conditions affect the productivity of enzymes? Enzymes are produced by cells and they act as catalysts, which means they are organic molecules that speed up chemical reactions. How effectively they work depends on the conditions they are in, such as level of temperature, pH level, substrate concentration, and salt concentration. In these experiments, Catalase will be placed in different conditions with hydrogen

that organism (Zamocky, 2008). To remove the destructive chemical compound, the body produces an enzyme referred to as catalase. This particular enzyme speeds up the reaction that specifically breaks down H2O2 into H2O and O2. Catalases, as well as other enzymes, are able to speed up the chemical reaction by lowering the activation energy (Urry, 2016). There are multiple ways to affect how fast a catalase can lower the activation energy during the breakdown of hydrogen peroxide: Tissues of different

introduction of this lab has been supported by the procedures. As the temperature varied from catalases optimal of 37° C, the reaction rate of catalase decreased. 37°C had the highest reaction rate of the three, at 3, while 4°C had the middle rate of reaction at 2.5, and 100° C had the lowest reaction rate of 0.5. Since enzymes are proteins, they are subject to denaturation at high temperatures. Catalase is an enzyme present in the human liver and functions at an optimum of 37°C. The data from the 36.7°

that the data did in fact support the hypothesis, because the salt and potato peroxidase solution for each type of potato showed that the more salt concentration there was, the longer it took for the enzymes to break it down. This may be because after time, the high level of salt will denature the enzyme, causing it to react and work slower. For the red potato peroxidase, the control group without any salt took only 26 seconds whereas when the highest amount of salt concentrate - 10.88% - was present

oxygen produced, also changed accordingly. This enzyme controlled reaction will be fastest at a particular pH – the optimum for the enzyme and slower at pH values above and below the optimum. The values from my experiment clearly show that when the pH of the reaction mixture was increased towards or decreased from the optimum pH of the enzyme the rate of the reaction subsequently increased or decreased. My results visibly show that the optimum for this enzyme is pH 7, the pH at which the highest rate of

a. The enzyme of this experiment is the catalase from the potatoes. Catalase is an enzyme present in humans that breakdown peroxide (H2O2), a toxic substance to organisms but is a byproduct of biochemical reaction. Catalase is found in peroxisomes within cells, and typically breakdown the hydrogen peroxide (if any) produced within the cell before it is able to leave. This makes catalase an extremely vital enzyme as it basically prevents the toxin from doing any true harm.   b. The substrate of this

of this lab is to observe the catalase found in liver cells by measuring how temperature, pH and enzyme concentrations affect the reaction rates of enzymes. Background Enzymes are considered to be “biological catalysts” meaning they can speed up a chemical reaction in a cell without being used up in the process. Enzymes do this by lowering the amount of energy needed to activate the process. The lower the activation energy, the faster the reaction. Without enzymes, vital life processes would occur

Introduction This research experiment will fundamentally focus on the activity of catalase, an enzyme that can be found in nearly every living organism. The essential function of catalase is to decompose hydrogen peroxide to produce water and oxygen. This enzyme also plays a major role within the protection of the cell from the oxidative damage that the reactive oxygen species are capable of causing. In addition, catalase is known to have the ability of chemically converting substrates such as hydrogen