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independent variables to change when doing enzyme investigations
pH
temperature
concentration of substrate
concentration of enzyme
dependent variables in enzyme investigations
time
volume
mass
absorbance
from a graph what are three different rates that can be calculated
rate between two line
initial rate- instant that the substrate and enzymes are mixed
rate at a particular time
how to work out the rate
change in y axis value divided by change in x axis value
how to explain low pH in a graph
in low pH there is a high concentration of H+ ions
more amino groups will have a positive charge so will affect hydrogen and ionic bonding in the protein
this will change the 3D shape of the active site
as the pH becomes more acidic fewer bonds can form between the active site and the substrate molecules
fewer enzyme-substrate complexes form and the rate decreases.
how ton explain high pH in a graph
not enough H+ ions are present
increasing number of carboxylic acid groups have negative charge
hydrogen anionic bonding are effected and the 3D shape of the active site changes making it less able to from bonds within the substrate.

what happens at A (3)
at low substrate concentration, the number of substrate molecules is low and not all the active sites of the enzyme molecules are occupied
as the concentration of the substrate increases, there is a greater frequency of enzyme- substrate complex formation and an increase in rate of reaction.
at low substrate concentrations the number of molecules of substrate acts as the limiting factor.

what happens at B (3)
at higher substrate concentrations more of the active sites are occupied at the same time
frequency of enzyme-substrate complex formation increases at a slower rate.
smaller increase in rate of reaction

what happens at C (4)
because there are a fixed number of active sites eventually you reach a maximum rate of reaction
all the active sites are occupied- SATURATED
adding more substrate cannot cause an increase in the rate of reaction as no more active sites are available
at high substrate concentrations the number of molecules of enzyme acts as a limiting factor

what happens at A (4)
at low enzyme concentrations the number of enzyme molecules is low and all active sites the enzyme molecules are occupied
as the concentration of enzymes increases more active sites are available
there is a greater frequency of enzyme-substrate complex formation and an increase in the rate of reaction
at low enzyme concentrations the number of molecules of enzyme acts as a limiting factor

what happens at B (4)
at higher enzyme concentrations, more active sites become available
substrate concentration is limited
the frequency of enzyme-substrate complex formation increases at a slower rate
smaller increase in rate of reaction

what happens at C (4)
because there are a fixed number of substrate molecules eventually you reach a maximum rate of reaction
adding more enzyme substrate cannot cause an increase in rate of reaction as no more substrate molecules are available
at high enzyme concentrations, the number of molecules of substrate acts as a limiting factor
only adding more substrate can the maximum be increased