Study the graphs of enzyme activity below and answer the questions that follow - Leaving Cert Biology - Question 13 - 2014
Question 13
Study the graphs of enzyme activity below and answer the questions that follow.
Graph A
Graph B
(i) In the case of each graph state the relationship between the r... show full transcript
Worked Solution & Example Answer:Study the graphs of enzyme activity below and answer the questions that follow - Leaving Cert Biology - Question 13 - 2014
Step 1
i) In the case of each graph state the relationship between the rate of reaction (y-axis) and another factor (x-axis).
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Answer
For Graph A, the relationship shows that as the factor on the x-axis increases, the rate of reaction decreases. This is typically indicative of a substrate inhibition or unfavorable conditions affecting enzyme activity.
For Graph B, the rate of reaction initially increases with the factor on the x-axis before decreasing. This suggests that there is an optimal range for enzyme activity, after which denaturation or inhibition occurs.
Step 2
ii) In the case of graph B, what factor could be responsible for the changes in activity of the enzyme?
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Answer
The factor that could be responsible for the changes in activity in Graph B is likely to be temperature or pH. As temperature increases, enzyme activity initially rises but can lead to denaturation at higher temperatures.
Step 3
i) Give a detailed account of how enzymes work, referring in your answer to their specificity.
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Enzymes are biological catalysts that speed up chemical reactions in biological systems. They function by binding to specific substrates at their active site, creating an enzyme-substrate complex. The specificity of enzymes arises from the precise arrangement of amino acids at the active site, which allows for a complementary fit with the substrate. Once bound, the enzyme lowers the activation energy required for the reaction, facilitating product formation while remaining unchanged themselves.
Step 4
ii) Name two processes that occur in plant or animal cells that require the use of enzymes.
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Cellular respiration, where glucose is broken down to release energy.
Digestion, where enzymes like amylase and protease help in the breakdown of food.
Step 5
1. Suggest why such enzymes are included in washing powder.
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Enzymes are included in washing powders to break down biological stains, such as proteins, fats, and carbohydrates. They enhance the cleaning efficiency at lower temperatures, making the washing process more effective.
Step 6
2. Why is 40 °C the recommended temperature for these washing powders?
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40 °C is recommended because it is warm enough to enhance enzyme activity while preventing denaturation. At this temperature, enzymes can effectively break down stains without losing their catalytic abilities.
Step 7
3. Suggest what would happen to these enzymes in an 80 °C wash.
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In an 80 °C wash, most enzymes would denature, losing their structure and function. This means they would no longer be effective at catalyzing reactions, reducing the cleaning efficiency of the washing powder.
Step 8
i) Draw a labelled diagram of the apparatus you used to prepare alcohol.
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The apparatus typically consists of a fermentation flask fitted with an airlock to allow gases to escape while preventing contaminants. Labels should indicate:
Flask containing the yeast and glucose solution
Air lock or oil layer for anaerobic conditions.
Step 9
ii) Give two advantages of using immobilised yeast cells in the production of alcohol.
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Immobilised yeast can be reused multiple times, reducing costs in industrial processes.
They provide a more controlled fermentation environment, enhancing the efficiency of alcohol production.
Step 10
iii) How did you test for the presence of alcohol?
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To test for the presence of alcohol, I used the iodofom test, where the sample was mixed with potassium iodide solution. The presence of alcohol would cause a color change indicating its formation, or alternatively, I could have used dichromate test, where a color change from orange to green indicates alcohol presence.
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