enzymes : the effect of substrate concentration on the rate of enzyme-catalysed reactions Flashcards
(15 cards)
define concentration
number of molecules per unit volume
what happens if there isn’t any substrate present ?
- an enzyme-catalysed reaction can’t proceed
why can’t the enzyme-catalysed reaction proceed ?
- as there aren’t any substrate molecules to fit into the enzyme molecules’ active sites
–> so enzyme-substrate-complexes can’t be formed
what happens when a substrate is added ?
- its concentration increases
–> the rate of reaction also increases
why does this occur and what does it lead to ?
- this is because more (ESC) can form
- more product molecules are formed
what is the limiting factor and why ?
- substrate concentration is limiting the reaction –> as it increases –> the rate of reaction also increases
what happens when the concentration of the substrate is increased further ?
- the reaction will reach its maximum rate
what happens if one adds more substrate molecules after maximum rate and why ?
- it won’t increase the rate of reaction
- as all the enzymes active sites are occupied with substrate molecules
- if more substrate molecules are added they can’t successfully collide with and fit into an enzyme’s active site
draw a graph representing the effect of increasing substrate concentration on the rate of an enzyme-controlled reaction and LABEL
find in textbook :)
what is the balanced equation for the reaction controlled by catalase ?
H2O2 –> H2O + O2
is catalase an intracellular enzyme or an extra cellular enzyme ?
intracellular
draw an label the set up of the experiment
- conical flask with catalase source and hydrogen peroxide
- delivery tube
- measuring cylinder
- water trough
explain the shape of the graph using biological ideas and relevant enzyme theory
- graph should show an increase in rate of gas production with an increase in substrate concentration
–> this is because there is more substrate for the enzyme to work on so more product is formed more quickly
–> if there is a levelling off , this is because the enzyme cannot work more quickly and the substrate molecules effectively have to queue up for an enzyme to become free
–> so the rate levels off
state a limitation of the experiment and how one could overcome it
- gas may escape while trying to put the bung in
–> use a gas syringe or do replicates at each concentration
how to calculate the rate of reaction on a graph ?
- construct a tangent line using a ruler
- calculate the gradient of the line by dividing change in y / change in x
- value is the initial rate of reaction