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PORT FOR EXPERIMENT 40 (continued) REPORT FO NAME 3. Does the addition of acid increase or decrease the activity of catalase?
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(3) (a) Does the addition of acid increase or decrease the activity of catalase?

Hydrogen peroxide is a by-product of many biological functions of organisms. All aerobic organisms use oxygen for respiration. The reduction of oxygen into water is sometimes incomplete, and an extra electron from a metal ion can be transferred, causing the formation of peroxide. However, most of the hydrogen peroxide is created during the production of ATP in the mitochondria.
Although peroxide is toxic to living cells, the reaction to break it back down to water and oxygen happens quickly and efficiently. Catalase is known as one of the most efficient enzymes, having a turnover number close to 200,000 events/second/subunit. Without catalase to increase the rate of the reactions, hydrogen peroxide would remain, damaging cells.

(3) (b) Does the addition of base increase or decrease the activity of catalase?

Catalase and its rate of activity are affected by many factors, including temperature, pH, salt concentration, amount of substrate and the presence of inhibitors or activators.

Temperature is an important factor in all biochemical reactions, as high temperatures cause denaturation of enzymes. As the enzyme denatures, it changes the conformation, causing the substrate to bind less efficiently, therefore decreasing the reaction. However, until that maximum temperature (which is different for each type of catalase) is reached, the reaction will increase as the temperature increases.


The pH, the measure of acidity or hydrogen ion concentration with a solution, is measured on a scale of 0-14. As a solution becomes more acidic (below 7), the enzyme can gain a hydrogen ion from the solution and as the solution becomes more basic (above 7), it can lose a hydrogen ion. Either of these extremes can reduce the rate of the reaction as it changes the chemical bonds of the catalase.
There are two types of inhibitors: non-competitive inhibitors, which bind somewhere other than the active site, and competitive inhibitors, which bind to the active site of the catalase. Copper sulfate is a known non-competitive inhibitor of catalase, and cyanide is a known inhibitor.

(4) what does copper ii sulfate do to the enzyme activity using potato liquid. how do you explain this change?

Copper(||) sulphate is a noncompetitive inhibitor.it can bind to the enzymes which are present in potato liquid with or without a substrate at different places at the same time.it changes the conformation of an enzyme as well as its active site which make the substrate unable to bind to the enzyme effectively.so the copper (||) sulphate distorts the overall shape of the enzyme .so the efficiency decrease.the catecholase enzyme is present in potato liquid which efficiency decrease by copper(||) sulphate .because copper (||) sulphate as a noncompetitive inhibitor distorts the overall shape of the enzyme.non competitive inhibitors are usually reversible, but are not influenced by the concentration of the substrate.

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