The aim of my investigation is to see how pH affects the activity of potato tissue catalase, during the decomposition of hydrogen peroxide to produce water and oxygen.
Enzymes are types of proteins that work as a substance to help speed up a chemical reaction (Madar & Windelspecht, 104). There are three factors that help enzyme activity increase in speed. The three factors that speed up the activity of enzymes are concentration, an increase in temperature, and a preferred pH environment. Whether or not the reaction continues to move forward is not up to the enzyme, instead the reaction is dependent on a reaction’s free energy. These enzymatic reactions have reactants referred to as substrates. Enzymes do much more than create substrates; enzymes actually work with the substrate in a reaction (Madar &Windelspecht, 106). For reactions in a cell it is
Enzymes are a key aspect in our everyday life and are a key to sustaining life. They are biological catalysts that help speed up the rate of reactions. They do this by lowering the activation energy of chemical reactions (Biology Department, 2011).
Oxygen production will occur in tube 5, 6, and 7 because each of those tubes 1 mL of distilled water, 3 mL of hydrogen peroxide, 1 mL of catalase solution, and 1 mL of a pH of 5, 7, or 9. These three different tubes do not contain HCl or NaOH that would change the pH of the solution in the tubes. HCl is a strong acid, whereas NaOH is a strong
This experiment was performed to determine the resultant effect of temperature change on the reaction between the enzyme catalase and hydrogen peroxide. This experiment was performed by measuring and comparing the amount of oxygen bubbles produced and the absorbance of the catalase and hydrogen peroxide solution over time at room temperature, 2°C, 50°C, and 60°C. The overall result of this experiment proved that this reaction works best at room temperature, slows down when the temperature is lowered, and does not take place when the temperature gets too high due to the enzyme denaturing at these higher temperatures. The hypothesis that was
A catalase is an enzyme that protects cells from oxidative damage. It does so by breaking down hydrogen peroxide, which the catalase generates during cell metabolism. Catalase deactivates millions of hydrogen peroxide molecules per second. First, the catalase breaks down hydrogen peroxide by removing and binding one oxygen atom and next releasing the rest of the hydrogen peroxide molecule as water. Then, the catalase breaks down a second hydrogen peroxide molecule by releasing oxygen gas and water. The optimum temperature- the temperature at which the enzyme is the most active at- is 40°C. Also, the optimum pH level for the catalase is pH 7.
Enzymes are biological catalysts that carry thousands of chemical reactions that occur in living cells. They could be found in every living thing. Enzymes increase the rate at which chemical reactions occur. A catalyst speeds up a chemical reaction by lowering the activation energy required. They are proteins made up of several amino acids. Each enzyme is different due to its structure, it all has different amino acid sequence. An enzymes ability to function depends on it’s environment. These factors include temperature, denaturation, pH, the size , the shape, and the amount of enzymes present. Enzymes performs best at ph7. That is the same pH as blood , the more enzymes stray away from pH7 the weaker it becomes , the active site gets damaged. This makes the enzyme not active, no longer functional. When it comes to temperature enzymes at a certain temperature have maximum activity. As temperature increases the enzyme activity also increases. When enzymes reach their maximum activity level and the temperature is still increasing it will start to decline (denaturation). The rate of reaction also depends on how much enzymes are present. We tested 5 hypothesis which were the amount of enzyme does not alter the rate of a reaction. pH does not influence the rate of an enzyme reaction. Temperature does not influence the rate of an enzyme activity. Boiling an enzyme before a reaction does not influence enzyme activity. The
Enzymes are complex proteins that function as biological catalysts, which act by increasing the rate of biochemical reactions to alter a substance (known as a substrate) in metabolic processes, such as respiration and digestion. In order for enzymes to function at their best, they need their environment to be at certain conditions for the chemical reactions to take place. The environment where the enzymes will function at their best is called ‘optimum conditions’ and will vary from enzyme to enzyme, depending on the chemical reaction.
Enzymes primary job is to catalyse reactions in almost all biological functions in the body, speeding them up by lowering activation energy, taking the reaction rate from almost stagnant to a workable efficiency. Although, enzymes are only most efficient while in their optimum temperature and pH level, becoming inactive at high pH / low temperature and permanently denatured at low pH / high temperature rendering them useless due to the deformed active site. Pepsin for example, an enzyme used to break down protein in the stomach, has an optimum temperature or 37-42 degrees celsius and an optimum pH of 1.5-2.5.
All living things need catalase to live. Weather it regulating the amount of a substance in the body or decomposition it is always constant. In this experiment it looks at how cells react to their environment. The cells in this experiment would be the enzymes.
Effect of Temperature on Rate of Reaction of Catalase Introduction This investigation was in an attempt to try to find out how varying the temperature can affect an enzyme. The enzyme used was catalase which breaks down Hydrogen Peroxide, this gives off water and oxygen as effervescence. This effervescence is what is used to measure the reaction rate of the catalase. The optimal heat for enzyme activity is proven to be 37oC as anything above this denatures the enzyme.
Figure A shows the data collected when an enzyme’s reaction rate, in other words, absorbance, is measured at varying temperatures. Beginning with an absorbance of 0.549, the enzyme, catecholase, shows an inversely proportional relationship between its absorbance and increasing temperature. Our data shows that as the enzymes are subjected to higher temperatures, the enzymes are rendered inactive and therefore denatured. On the other hand, the enzyme’s optimal potential is shown somewhere between 10˚C and 24˚C.
The activity of an enzyme is affected by its environmental conditions. Increasing temperatures increases the kinetic energy that molecules possess. If enzymes are overheated, they start denaturing. Denaturing is a process in which the enzyme loses its primary structure due to overheating or by application of some external stress or compound such as a strong acid or base, a concentrated inorganic salt, an organic solvent, radiation or heat. If proteins in a living cell are denatured, this results in possible death of the cell. Denatured proteins can exhibit many different characteristics from loss of physical form to communal aggregation. (www.worthington-biochem.com/introbiochem/factors.html )
For a detailed list of required materials, refer to the enzyme lab handout section C. The independent variable in this study was temperature. The dependent variable was rate of reaction, measured qualitatively on a scale of one to five based on the number of bubbles observed as the reaction took place. The amount of liver and H2O2, the ambient temperature, and the observation time allotted for each reaction were control variables that were kept constant throughout.