Effect of...

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  • Created by: Jasmin
  • Created on: 19-10-13 18:48
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  • Effect of...
      • R of R doubles for every 10C rise in temp until an optimum is reached
      • Low temp
        • R of R is low. Enzymes do not have enough energy to collide. Inactivated
      • Increase in temp - molecules get greater kinetic energy. Molecules move around more quickly increasing the chance of molecules colliding, making reaction more successful
      • Optimum
        • R of R highest/fastest. Enzyme at its best shape, increasing likelihood that a reaction will be successfuk
      • High temp
        • Increase vibrations of the molecules causes H bonds to break and causes change in 3. Alters AS of enzyme. Denatured. Permanent change in structure
    • pH
      • Narrow optimum range
      • Small changes in pH outside the optimum can cause small reversible changes in enzyme structure --> inactivation
      • Charges on the AA side chains of enzymes AS are affected by H ions or hydroxyl ions
      • Low pH
        • Acidic. R of R is low. pH outside optimum range causing inactivation
      • Optimum
        • R of R is maximum. Substrate is attached to AS and so enzyme-substrate complex if formed
      • High pH
        • Alkaline. R of R is low. Charges on AAs are altered and can cause the bonds in 3 to break. Denatured
      • If amount of enzyme is constant the R of R will increase if the substrate increases
      • Doesn't keep going up because not enough AS for the substrates to bind to
      • Low substrate concentration
        • R of R is low. Enzyme molecules have a limited number of substrate molecules to collide with
          • Therefore the AS of the enzymes are not working to full capacity
      • Optimum
        • R of R at maximum. All AS are filled and working to full capacity
      • High substrate concentration
        • R of R levelled off, no increase. No effect on all AS are already occupied at one time
    • Enzyme Concentration
      • Increase E.C will increase R of R as long as there are enough substrate molecules to occupy the AS


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