Kinetic energy of particles increased as they move faster and collide more often - Rate of reaction increased
Temperature coefficient - Q10:
Measure of how much that rate of reaction INCREASES with a 10 degrees Celsius rise in temperature
Temperature coefficient:
Rate of reaction doubles with a 10 degrees Celsius temperature increase
Denaturation from temperature:
Higher temperatures - Bonds vibrate more
Vibrations increase until bonds are strained then break
Specific 3d tertiary structure changes
Enzyme denatured
Denatured enzymes:
Active site begins to change shape
No longer complementary to substrate
Substrate can no longer fit into activesite and does not function as a catalyst
Optimumtemperature - Temperature enzymes have the highest rate of activity
Most enzymes optimum is around 40 degrees Celsius
Change in pH = Change in hydrogen ion concentration
Specific 3d tertiary structure held in place by hydrogen and ionic bonds between R-groups
Ionic and hydrogen bonds are from interactions between polar and charged r-groups on amino acids - Primary structure formed
More hydrogen ions = Low pH (Acidic)
Fewer hydrogen ions = High pH (Alkaline)
Optimum pH - Active site at the right shape at a certain hydrogen ion concentration
Renaturation - pH changing back after optimum is surpassed and its active site is altered then returning back to normal shape
Denatured = When pH has a more significant change - Structure of the enzymes is irreversibly altered and activesite is no longer complementary to substrate
Enzyme denatured - Rate of reaction is reduced
Changing concentration of hydrogen ions - Changes interactions hydrogen ions have with polar and charged R-groups
Interactions of R-groups together - Affected by interaction of R-groups with hydrogen ions
More hydrogen ions present (Low pH) or Less hydrogen ions present (High pH):
Less the R-groups are able to interact with each other
Bonds break
Enzyme shape changes
Shape of enzymes changes as pH changes - Only functions within a narrow range
Increasing substrate concentration:
Higher collision rate - More enzyme-substrate complexes formed
Rate of reaction increases
Increasing concentration of enzymes:
Number of available active sites increased
More enzyme-substrate complexes are formed at a faster rate
Rate of reaction increases until Vmax
At Vmax:
All active sites are occupied by substrate particles
No more enzyme-substrate complexes can be formed until products are released from active sites
Increase rate of reaction past Vmax - Add more enzymes or increase temperature
Adding more enzymes past Vmax:
More active sites are available
Rate of reaction rises towards a higher Vmax
Concentration of substrate becomes the limiting factor again - If increased rate of reaction rises until the higher Vmax is reached