Short half-life corresponds to high reactivity. The one nanosecond half-life of the hydroxyl radical indicates that it is so reactive that it reacts with the first molecule it bumps into. Ascorbate forms H2O2 on autoxidation direct combination with oxygen.
The effect of catalase on hydrogen peroxide The effect of catalase on hydrogen peroxide 8 August Chemistry The aim of the experiments is to see if increasing the surface area of the enzyme Catalase, affects the relative activity of the substrate Hydrogen peroxide.
Then to observe and measure the effect the Catalase has on the chemical breakdown of the hydrogen peroxide.
My theory is if you keep increasing the surface area of Catalase, the more active sites are available to join with the substrate causing an increase in the breakdown of the hydrogen peroxide producing more oxygen and water.
We will write a custom essay sample on The effect of catalase on hydrogen peroxide or any similar topic specifically for you Do Not Waste HIRE WRITER There will be an optimal point when all the active sites are filled, at this point the reaction will stop, as all the hydrogen peroxide will have been broken down leaving only Catalase, water and oxygen.
I predict the more you increase the surface area of Catalase, the more oxygen produced, because the hydrogen peroxide has more surface area to collide with, causing a faster rate of reaction.
Put on safety glasses 2. Set up equipment as shown above 3. Use the hole borer and bore out pieces of potato then cut into 2cm lengths. Put 1x2cm piece of potato in the conical flask with 50ml of hydrogen peroxide. Replace bung immediately and start stopwatch for 5 minutes.
After 5 minutes pull out bung, read the measurement on the upside down measuring cylinder. Record your results 6. Empty and rinse conical flask. Refill upside down measuring cylinder with water 8. Repeat steps another 4 times but in step 4 add another 2cm piece of potato each time.
Perform the experiment three times Take the room temperature at the start middle and end of the experiment Repeat the steps this time omit the potato, this gives the control result. You only need do this once. Enzymes are effective in the body, because they lower the amount of energy required for a reaction to happen All enzymes have an active site.
Johnson This is where another molecule can bind with the enzyme. This molecule is known as the substrate. When the substrate binds with the enzyme, it converts the substrate into one or more products. Enzymes are specific to their substrate, because the shape of their active site will only fit the shape of their substrate.
It is said that the enzymes active site is complimentary to their substrate. This is known as the lock and key theory. Another theory is the Induced fit theory it is when the substrate and enzyme fit together but the enzyme-substrate complex changes shape a little to complete the fit. This locks the substrate even more tightly to the enzyme.
They are 2 types of inhibitors that can affect the rate of enzyme action. Competitive inhibitors which have a similar shape to the normal substrate. The competitive inhibitor can form a complex with the enzymes active site preventing the normal substrate binding, so normal reaction cant take place.
The second is the non competitive inhibitor which distorts the shape of the active site. Enzymes have an optimum temperature and ph level at which they work best. If the temperature is too high or the ph level is too high or too low, the enzyme becomes denatured.
Enzymes are globular proteins, with a complex tertiary structure, in which polypeptides are curled up into a ball shape; they are compact and soluble so they are easily transported around the blood. The 3d shape of the enzyme molecule is important, as if the shape is changed, the enzyme cannot bond with the substrate.
The enzyme shape is maintained by hydrogen bonds and ionic forces. Catalase is a globular protein molecule that is found in all living cells.
Bowness Catalase breaks down hydrogen peroxide into harmless water and oxygen gas. Hydrogen peroxide is a highly reactive chemical often used for bleaching and cleaning minor wounds.
Hydrogen peroxide is continually formed as a by product of a chemical reaction in living cells, however is highly poisonous and must be removed or broken down immediately by the cells.The effect of enzyme concentration, substrate concentration, pH, and temperature on the enzyme catalase.
Introduction: Enzymes are biological catalysts; proteins and RNA. They are required for most biological reactions and they are highly specific. Each enzyme has an active site. Staphylococcus aureus is a human pathogen that can cause a wide spectrum of diseases, including sepsis, pneumonia, arthritis, and endocarditis.
Ineffective treatment of a number of staphylococcal infections with antibiotics is due to the development and spread of antibiotic-resistant strains following decades of antibiotic usage. The aim of this study was to test the rate of reactivity of the enzyme catalase on hydrogen peroxide while subject to different concentrations of an inhibitor.
The hypothesis was that hydrogen peroxide will be broken down by catalase into hydrogen and oxygen, where a higher concentration of inhibitor will yield less oxygen, resultant of [ ].
The Effect of pH on Enzyme Activity Essay - The Effect of pH on Enzyme Activity pH is a measure of the concentration of hydrogen ions in a solution. Effect of Temperature on the Enzyme Catalase Stephen Francis Biology Abstract This experiment was performed to determine the resultant effect of temperature change on the reaction between the enzyme catalase and hydrogen peroxide.
General methods of preparation and properties of Alkenes and alkynes – electrophilic and radical addition mechanisms- addition reactions with H2, X2, HX, HOX, H2SO4, H2O, hydroboration Ozonolysis and peroxide effect.