Enzymes Flashcards
What is an enzyme?
An enzyme is a large protein that acts as a biological catalyst by accelerating chemical reactions.
What are enzymes made up of?
Like all proteins, enzymes are made up of chains of animo acid, that fold into unique shapes, that enzymes require to perform their function correctly.
What is a catalyst?
A catalyst is a substance that increases the speed or rate of reaction, without being changed or used up in the reaction.
Draw the lock and key model.
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What is involved in Step 1 of the lock and key model?
Substrates and the Enzyme (Active Site). These are complimentary shapes.
What is involved in Step 2 of the lock and key model?
Enzyme-Substrate Complex
What is involved in Step 3 of the lock and key model?
Product and reusable enzyme
Explain step 1 of the lock and key model
The enzyme and the substrate are specific to one another. The enzyme had to be the right shape for the substrate to bind to the active site of the enzyme. When it denatures, changing shape irreversibly, the chemical reaction no longer works.
Explain Step 2 of the lock and key model
The substrate has now bound to the active site of the enzyme in the enzyme-substrate complex.
Explain step 3 of the lock and key model
The enzyme catalyses the break down of the substrate into products.
Flaws of lock and key model
The model is simpler than reality. In reality, the active site changes shape a little for the substrate to bind to it to get a tighter fit. This is called the ‘induced fit’ model of enzyme action.
Is the enzyme shape reusable?
Yes
What factors affect the rate of enzyme-controlled reactions?
- Temperature
- pH
- Enzyme concentration
- Substrate concentration
How does temperature affect enzymes?
Enzymes work best at optimum temperature. Below this, an increase in temperature provides more kinetic or heat energy to the molecules involves and the number of enzyme-substrate collisions increases, as does the rate of reaction. However, beyond this temperature, the enzyme denatures, changing shape irreversibly, and the active site is disrupted. Most human enzymes work best at 37 degrees Celsius, as this is the standard body temperature.
Draw graph showing relationship of temperature and enzyme rate of reaction
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How does pH affect enzymes?
Enzymes work best at optimum pH. If the pH changes too much from the optimum, the chemical nature of the animo acids can change. This may result in a change in the bonds and so the tertiary structure may break down. The active site will be disrupted, the enzyme denatured.
Show the effect of pH on enzyme rate of reaction on a graph
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How does enzyme concentration affect enzyme rate of reaction?
At low enzyme concentration, there is more competition for the active sites, and the rate of reaction is low. As enzyme concentration increases, there are more active sites and the reaction can proceed at a faster rate. Eventually, increasing the enzyme concentration beyond a certain point has no effect as the substrate concentration becomes the limiting factor, and it plateaus.
Draw a graph to show the effect of enzyme concentration to the rate of reaction
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How does substrate concentration affect enzyme rate of reaction?
At low substrate concentration, many active sites are not occupied. This means the reaction rate is low. When more substrate molecules are added, more enzyme-substrate complexes can be formed. As there are more active site, the rate of reaction increases. Eventually, the substrate concentration will have no effect. The active sites will be saturated so no more enzyme-substrate complexes can be formed.
Draw a graph to show how substrate concentration affects rate of reaction
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How to investigate the effect of enzyme rate of reaction?
- The amylase, starch and buffer experiment
- The trypsin and milk experiment
Describe the trypsin and milk experiment.
- Label two test tubes A and B
- Using a clean syringe, place 10cm^3 of milk suspension into Tube A
- Using a clean syringe, place 10cm^3 of Trypsin solution into Tube B
- Place the tubes in a water bath at 20 degrees Celsius and leave to equibrilate for 5min
- Pour the contents of Tube B into Tube A and stir. Start the timer
- Hold the tube against the white card and observe the X through the solution at regular intervals
- As soon as the X becomes visible through the solution, stop the timer and record your results
- Repeat the above procedure at temperatures of: 20, 30, 40, 50, 60, 70 and 80 degrees Celsius
Risk of amylase, starch and buffer experiment
Iodine solution is an irritant. If it touches skin it should be washed off.
Goggles should be worn at all times.