Effect of...
- Created by: Jasmin
- Created on: 19-10-13 18:48
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- Effect of...
- TEMPERATURE
- 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
- SUBSTRATE CONCENTRATION
- 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
- R of R is low. Enzyme molecules have a limited number of substrate molecules to collide with
- 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
- TEMPERATURE
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