(U1) Enzymes Flashcards

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1
Q

What are the stages in enzyme action? (4)

A
  • substrate attaches to active site
  • enzyme-substrate complex formed
  • enzyme-product complex formed
  • products leave active site separately
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2
Q

What are the 2 forms of metabolic reaction?

A
  • catabolism (cut)
  • anabolism (add)
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3
Q

What is activation energy? (2)

A
  • the minimum amount of energy
  • required for a reaction to occur
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4
Q

Why does high and low pH affect enzyme active sites? (2)

A
  • active sites have their shape due to bonds in tertiary protein structure
  • changes to pH affect ionic bonds, thus changing the shape of the active site
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5
Q

How does an enzyme actually breakdown a substrate? (3)

A
  • enzyme puts pressure on bonds in the substrate
  • weakens bonds
  • bonds break
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6
Q

Explain the lock and key model (2)

A
  • enzyme has an exactly complementary active site to the substrate
  • collisions between the two result in an enzyme-substrate complex
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7
Q

Explain the induced fit model (4)

A
  • enzyme active site not totally complementary to substrate
  • active site undergoes a conformational change in shape
  • active site now precisely fits the substrate
  • enzyme-substrate complexes now form on collisions with the substrate
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8
Q

What is the effect of increasing substrate concentration on enzyme activity? (4)

A
  • enzyme activity increases, then levels off
  • greater concentration increases chance of collisions between active sites and substrates
  • therefore more enzyme-substrate complexes are formed
  • at high conc, enzyme concentration becomes limiting - all active sites occupied
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9
Q

What is the point at which the substrate concentration / enzyme activity graph levels off at called?

A

Point of saturation

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10
Q

What is the effect of increasing enzyme concentration on enzyme activity? (5)

A
  • enzyme activity increases, but can level off
  • greater concentration increases chance of collisions between active sites and substrates
  • therefore more enzyme-substrate complexes are formed
  • at high conc, substrate concentration can become limiting - all active sites occupied
  • if in excess, the trend just continues - increasing activity
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11
Q

What is the effect of changing pH on enzyme activity? (4)

A
  • deviation from optimum causes decrease in enzyme activity
  • ionic bonds in tertiary structure of enzyme disrupted
  • active site undergoes a conformational change in shape - becomes denatured
  • less enzyme-substrate complexes formed on collisions with substrates
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12
Q

What is the effect of increasing temperature on enzyme activity? (5)

A
  • increasing temperature increases enzyme activity until a point where activity dramatically declines
  • increases due to increased kinetic energy
  • increases chance of collisions between substrates and active sites - forming enzyme-substrate complexes
  • high temps, hydrogen bonds broken in tertiary structure of the enzyme, causing a conformational change in shape of active site (denaturation)
  • active site no longer complementary - no more enzyme-substrate complexes formed
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13
Q

What are the advantages of using enzyme immobilisation in industry? (4)

A
  • production can occur continuously
  • product is enzyme free, reducing purification costs
  • enzymes easily reused
  • stability of enzyme improved: active over greater range of pH and temps (thermostable)
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14
Q

What are the 5 methods of immobilisation?

A
  • absorption onto an inert support (e.g. collagen matrix)
  • covalent bonding onto a solid support (e.g. cellulose fibres)
  • cross-linking via a binding chemical (e.g. glutaraldehyde)
  • encapsulation in a semi-permeable membrane (e.g. nylon)
  • entrapment inside a gel (e.g. silica gel)
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15
Q

Where are enzymes used in industry?

in terms of machinery

A

Flow-column reactors

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16
Q

What are the advantages and disadvantages of absorption immobilisation? (4)

(enzymes)

A

Advantages:

  • easy to immobilise, therefore cheap
  • no gel barrier diffusion neccessary

Disadvantages:

  • enzymes easily washed away - unreliable
  • active sites may be made inaccessible (blocked by material)
17
Q

What are the advantages and disadvantages of covalent bonding immobilisation? (7)

(enzymes)

A

Advantages:

  • enzymes not washed away - reliable
  • resistant to pH and temp changes
  • active sites must be exposed

Disadvantages:

  • relatively expensive
  • active sites may be made inaccessible (blocked by material)
  • long term regeneration of enzyme is impossible
  • high activity can’t be obtained

Most widely used method

18
Q

What are the advantages and disadvantages of cross-linking immobilisation? (7)

(enzymes)

A

Advantages:

  • enzymes not washed away - reliable
  • resistant to pH and temp changes
  • active sites must be exposed

Disadvantages:

  • relatively expensive
  • active sites may be made inaccessible (blocked by material)
  • long term regeneration of enzyme is impossible
  • high activity can’t be obtained
19
Q

What are the advantages and disadvantages of encapsulation immobilisation? (3)

(enzymes)

A

Advantages:

  • active sites must be exposed - activity not adversely affected

Disadvantages:

  • diffusion of substrate across matrix reduces rate of activity
  • some enzymes “leak out
20
Q

What are the advantages and disadvantages of entrapment immobilisation? (4)

(enzymes)

A

Advantages:

  • active sites exposed - reliable - activity not adversely affected
  • enzymes can’t “leak out”

Disadvantages:

  • slow diffusion across matrix reduces rate of activity
  • slow diffusion of products out of matrix