Generally, all enzymes are inactivated at temperatures below 10°C and get denatured (lose its three-dimensional protein nature) above its optimum temperature (Seager & Slabaugh 2010).
Experiments conclude that enzyme activity increases by almost ten percent coupled to each degree rise in temperature until it reaches its optimum state and declines beyond it as they start denaturing (Seager & Slabaugh 2010).
2. Do plants and animals have an enzyme that breaks down hydrogen peroxide? How could you test this?
The process of converting toxic hydrogen peroxide into harmless substances occurs at a very slow rate; therefore, both plants and animals have enzymes to catalyze it. Catalase is an enzyme that is present in animal cells; however, plants possess enzyme peroxidase to carry out this decomposition (Seager & Slabaugh 2010).
It can be tested by mixing hydrogen peroxide and a piece of animal liver (containing catalase) or a piece of potato (source of peroxidase) in a test tube. Bubbles of gas will be observed showing the decomposition of hydrogen peroxide (Seager & Slabaugh 2010).
3. How does the boiling water affect the overall reaction?
Boiling water has a temperature that is much higher than the optimum temperature of catalase and peroxidase, therefore; it will denature the enzymes thus causing a decrease in the rate of reaction (Seager & Slabaugh 2010).
4. How can enzyme activity be increased?
Enzyme activity can primarily be increased by adjusting the surrounding temperature and pH to achieve optimal state for an enzyme-catalyzed reaction (Seager & Slabaugh 2010).
5. Design an experiment to determine the optimal temperature...
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