2.5 Enzymes Flashcards

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1
Q

Enzyme

A
  • A globular protein that increases the rate of a biochemical reaction by lowering the activation energy threshold (i.e. a biological catalyst)
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2
Q

Active Site

A
  • Region on the surface of an enzyme to which the substrates bind and which catalyzes the reaction.
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3
Q

Substrates

A
  • Substances that enzymes convert into products in these reactions (the reactants).
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4
Q

Products

A
  • The end result.
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5
Q

Lock and Key model

A
  • The first theory of the action of an enzyme binding to a substrate.
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6
Q

Induced Fit Model

A

-The current theory of the action of an enzyme binding to a substrate.

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7
Q

Enzyme-substrate specificity

A
  • A feature of an enzyme activity with regard to the kind of substrate reacting with an enzyme to yield a product.
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8
Q

State what is meant by the term collision in enzyme catalysis.

A
  • The coming together of a substrate molecule and an active site is known as a collision.
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9
Q

Explain why not all collisions between enzymes and substrates result in catalysis.

A
  • As not all collisions result in binding.
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10
Q

Explain why the presence of water is critical for most enzyme reactions.

A
  • Most enzyme reactions occur when the substrates are dissolved in water.
  • All molecules dissolved in water are in random motion, with each molecule moving separately.
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11
Q

Enzymes can be immobilized (e.g. embedded in cell membranes). Enzymes can also be free to move, but they tend to move more slowly than substrates, explain why.

A
  • If not immobilized the enzyme can move too, however enzymes tend be larger than the substrate(s) and therefore move more slowly.
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12
Q
  • Effects of Temperature on Rate of Reaction
A
  • Low temperatures result in insufficient thermal energy for the activation of a given enzyme-catalysed reaction to be achieved.
  • Increasing the temperature will increase the speed and motion of both enzyme and substrate, resulting in higher enzyme activity.
  • This is because a higher kinetic energy will result in more frequent collisions between enzyme and substrate.
  • At an optimal temperature (may differ for different enzymes), the rate of enzyme activity will be at its peak.
  • Higher temperatures will cause enzyme stability to decrease, as the thermal energy disrupts the hydrogen bonds holding the enzyme together.
  • This causes the enzyme (particularly the active site) to lose its shape, resulting in a loss of enzyme activity (denaturation).
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13
Q

Effects of pH on Rate of Reaction

A
  • Changing the pH will alter the charge of the enzyme, which in turn will protein solubility and may change the shape of the molecule.
  • Changing the shape or charge of the active site will diminish its ability to bind to the substrate, halting enzyme function.
  • Enzymes have an optimum pH and moving outside of this range will always result in a diminished rate of reaction.
  • Different enzymes may have a different optimum pH ranges.
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14
Q

Effects of Substrate Concentration on Rate of Reaction

A
  • Increasing Substrate Concentration increases Rate of Reaction.
  • At optimum concentration of substrate molecules, all active sites are full and working at maximum efficiency.
  • Any increase in concentration beyond the optimum, will have no added effect as there are no extra active sites to be used.
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15
Q

List eight common uses of enzymes in industry.

A
  • Detergents.
  • Food Industry.
  • Paper production.
  • Textiles.
  • Brewing.
  • Medicine & Biotechnology.
  • Biofuels.
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16
Q

Enzymes used in industry are commonly immobilised.

Describe the advantages of immobilising enzymes.

A
  • Concentration of substrate can be increased as the enzyme is not dissolved - this increases the rate of reaction.
  • Recycled enzymes can be used many times, immobilized enzymes are easy to separate from the reaction mixture, resulting in a cost saving.
  • Separation of the products is straight forward (this also means that the the reaction can stopped at the correct time).
  • Stability of the enzyme to changes in temperature and pH is increased reducing the rate of degradation, again resulting in a cost saving.
17
Q

List three ways in which enzymes can be immobilised.

A
  • Enzymes used in industry are usually immobilized. They are attached to a material so that their movement is restricted. Common ways of doing this are:
  • Aggregations of enzymes bonded together.
  • Attached to surfaces, e.g. glass.
  • Entrapped in gels, e.g. alginate gel bead.
18
Q

Outline the process by which lactose-free milk is produced by immobilized enzymes.

A

Production of Lactose-free milk:

  • Lactase obtained from commonly from yeast (bacteria is an alternative).
  • Lactase is bound to the surface of alginate beads.

Milk is passed (repeatedly) over the beads.

  • The lactose is broken down into glucose and galactose.
  • The immobilized enzyme remains to be used again and does not affect the quality of the lactose free milk.
19
Q

State the three other commercial reasons that lactose free milk is produced.

A
  • As a means to increase the sweetness of milk (glucose and galactose are sweeter in flavour), thus negating the need for artificial sweeteners.
  • As a way of reducing the crystallisation of ice-creams (glucose and galactose are more soluble than lactose).
  • As a means of shortening the production time for yogurts or cheese (bacteria ferment glucose and galactose more readily than lactose).