Topic 2: Enzyme data and graph questions Flashcards
What are the 4 factors affecting the rate of enzyme catalysed reactions?
- Enzyme concentration
- Substrate concentration
- Temperature
- pH
When carrying out an enzyme practical, one factor will be the independent variable and the other three factors should be controlled (kept the same)
- Enzyme concentration – use the same _____ ________ to make up a set concentration e.g. 1%
- Substrate concentration – use the same _____ ________ to make up a set concentration e.g. 1%
- Temperature – use a ______ _____ set at the optimum temperature of the enzyme
- pH – use a _______
stock solution
stock solution
water bath
buffer
What is the formula for calculating the rate of reaction?
Rate = Y / X
In an exam question, when it says “Analyse the data to explain” What should you do?
(1 point)
- Both describe and explain using theory
In an exam question, when it says “Analyse the data/describe the data” What should you do?
(2 points)
- Only describe (no theory needed)
2. Follow data rules (trend, linear/non-linear, manipulate, divide data, SD bats, greatest increase etc.)
In an exam question, when it says “Explain the data” What should you do?
(1 point)
- Mostly explain, but you will probably need to state the trends that you are explaining,
NOTE: usually no marks for manipulation, greatest increase etc, - as most marks are for explanation
Key Summary: Explain why increasing enzyme concentration increases the initial rate of reaction
As the enzyme concentration increases, the initial rate of reaction increases because … (5 steps)
Eventually reaches a plateau (graph levels off) and {there is no further increase in rate/rate becomes constant} as the substrate concentration becomes the ___________ __________.
- number of enzymes (e.g. trypsin) increases
- so number of enzyme active sites increases
- MORE FREQUENT AND SUCCESSFUL COLLISIONS between enzyme and substrate
- MORE ENZYME-SUBSTRATE COMPLEXES form (lowers activation energy) in a given time
- more product forms in a given time
limiting factor
Key Summary: Why measure the initial rate of reaction?
3 points
- There needs to be enough substrate molecules to saturate the enzyme to ensure that substrate is not a limiting factor.
- Fastest rate is at the start (initial rate) then decreases.
- As reaction proceeds substrate concentration decreases as substrate gets used up by enzyme in the reaction.
Key Summary: Why does increasing substrate concentration increase the rate of reaction?
(4 steps)
- as the substrate concentration increases the rate of reaction increases
- as more substrate molecules are present {they collide with the enzyme more frequently / more successful collisions} , more enzyme-substrate complexes form, so more product forms in a given time
- eventually a maximum rate is reached - all the enzymes are involved in enzyme-substrate complexes (all active sites are {saturated with substrate/occupied})
- if the substrate concentration carries on increasing, there is no further increase in rate of reaction
Increasing substrate concentration increases the number of ________ __________
This means that more enzymes can convert substrate to product at the same ____ (assuming successful collisions) so product is made ______ (reaction rate increases)
___________ _________ limits rate.
substrate molecules
time
faster
Substrate concentration
Eventually a point will be reached where further increases in substrate concentration will not lead to increased rate of reaction as all the enzyme active sites are in use.
__________ ___________ limits rate
Enzyme concentration
At {0 degrees C /low temperature} enzymes are ______ – they lack kinetic energy so rate is slow
As temperature increases (0 - 37 degrees C), the kinetic energy, of the enzyme and substrate increase, so {they collide more often/more successful collisions}, increasing the ____
inactive
rate
At temperatures above the optimum the enzyme _____ _____ become ________ and change ______, so substrate cannot fit, _______ ________ _________ cannot form, so _________ cannot form.
active sites
denatured
shape
enzyme substrate complexes
product
Explain denaturation (in enzymes) (5 steps)
- increased temperature causes BONDS TO BREAK which hold together the enzyme’s tertiary structure
- the SHAPE OF THE ENZYME changes
- the SHAPE OF THE ACTIVE SITE changes (is denatured)
- the SUBSTRATE WILL NOT FIT IN THE ACTIVE SITE, and no enzyme substrate complex is formed
- the reaction rate decreases