Active site Site on surface of the enzyme to which the substrate binds Substrate A molecule which after combining with an enzyme is converted to a product
How do enzymes lower activation energy
- Enzyme binds to substrate - Lowers activation energy - By wearing bonds - Making substrate more likely to react
Outline how lock and key model catalyse reactions
- It explains the ability of specific enzymes to bind to specific substrates - Substrates fits exactly into the complementary shape to the active site of enzyme to form an enzyme substrate complex by lowering the activation energy - The active site can be changed by different chemicals/temperature/oH, so substrate can’t bind
Outline how induced fit model catalyse reactions
- It explains the ability of some enzymes to bind to several substrates - Active site of enzyme binds to substrate, but they do not match up exactly - Enzyme changes shape once bound, and this change in shape facilitates bond breaking by reducing activation energy - Once complete, products leave and enzyme works again
How active sites promotes enzyme-substrate specificity
- Shape of active site matches that of the substrate - Active site can change to induce fit of substrate
Explain enzyme-substrate specificity
- Enzyme shape is specific to substrate - Lock and key model - Lipid and Lipase - Has specific 3D shape essential to functioning - Active site on enzyme binds to substrate - Substrate and active site complementary due to structure - Enzyme substrate complex forms - Denaturation changes enzyme’s binding ability
Explain the effects of pH on enzyme catalysed reactions
- Enzymes has a optimum pH - Active sites work best at this pH - Activity decreases above and below the optimum - By interfering with H-bonds - Denaturing by extremes of pH so enzyme activity stops - The formation of the enzyme-substrate complex and binding to active site Effect to enzyme when exposed to increasing temperatures - Rate of reaction increases when temperature increases as there is a greater proportion of molecules with energy greater than the activation energy - Maximum rate is achieved at optimum temperature - Rate decreases above optimum temperature as enzymes are denatured at high temperature - Heat causes vibration inside the enzyme which breaks bonds for maintaining the structure of enzyme - To form enzyme substrate, substrate should fit in active site of enzyme - Since shape of active site has changed, substrate cannot bind to the enzyme
Explain the effect of change of pH, substrate concentration and
temperature on enzyme activity pH: - Enzymes have an optimum pH - Activity increase as pH gets closer to optimum pH - Extreme pH denatures enzymes by breaking bonds and altering structure Substrate: - As substrate concentration increases, activity increases - As substrate concentration increases, the collisions between substrate and enzyme increases - Till a plateau is reached and/or all active sites are occupied Temperature: - Enzymes have an optimum temperature - Activity increases as it gets closer to optimum temperature - High temperatures stop enzyme activity due to irreversible changes in structure by breaking bonds
Explain the production of lactose-free milk
- Lactase added to milk - Lactose hydrolysed into glucose and galactose - For those who are lactose intolerant - Increases sweetness and smooth texture
Discuss the use of lactase in the production of lactose-free milk
- Lactose is a disaccharide present in milk - Lactase digests lactose into galactose and glucose - Lactase produced naturally by yeast - Biotechnology companies isolate lactase for use in food processing - Lactase can be added to milk to reduce the level of lactose in the milk - Immobilised enzymes may be used - Lactose intolerant people cannot drink milk - Galactose and glucose are sweeter than lactose - So less sugar is need in food production - Bacteria ferment glucose and galactose more quickly than lactose - Galactose and glucose are more soluble so improve the texture of foods