2.5 Enzymes Flashcards

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1
Q

What is an enzyme?

A

An enzyme is a globular protein which acts as a biological catalyst by speeding up the rate of a chemical reaction

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2
Q

Do enzymes get used up?

A

No

Enzymes are not changed or consumed by the reactions they catalyse and thus can be reused

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3
Q

How are enzymes named?

A

Enzymes are typically named after the molecules they react with (called the substrate) and end with the suffix ‘-ase’

For example, lipids are broken down by the enzyme lipase

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4
Q

What is the active site?

A

The active site is the region on the surface of the enzyme which binds to the substrate molecule

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5
Q

What is the active site complementary to?

A

The active site and the substrate complement each other in terms of both shape and chemical properties

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6
Q

What does it mean that the active site is complementary to the substrate?

A

Hence only a specific substrate is capable of binding to a particular enzyme’s active site

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7
Q

Where do enzyme reactions typically occur?

A

Enzyme reactions typically occur in aqueous solutions (e.g. cytoplasm, interstitial fluid, etc.)

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8
Q

How do enzymes usually move around?

A

Consequently, the substrate and enzyme are usually moving randomly within the solution (Brownian motion)

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9
Q

Do enzymes always randomly move?

A

Sometimes an enzyme may be fixed in position (e.g. membrane-bound) – this serves to localise reactions to particular sites

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10
Q

What does enzyme catalysis require?

A

Enzyme catalysis requires that the substrate be brought into close physical proximity with the active site

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11
Q

What is formed when an enzyme and a catalyst collide?

A

When a substrate binds to the enzyme’s active site, an enzyme-substrate complex is formed

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12
Q

What is formed once the reaction is catalysed?

A

The enzyme catalyses the conversion of the substrate into product, creating an enzyme-product complex

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13
Q

What happens after the enzyme has catalysed the reaction?

A

The enzyme and product then dissociate – as the enzyme was not consumed, it can continue to catalyse further reactions

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14
Q

How can the rate of enzyme catalysis be increased?

A

Increasing the molecular motion of the particles (thermal energy can be introduced to increase kinetic energy)

Increasing the concentration of particles (either substrate or enzyme concentrations)

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15
Q

What is the active site’s specificity dependent on?

A

The shape and chemical properties of the active site are highly dependent on the tertiary structure of the enzyme

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16
Q

Can enzymes be denatured like proteins?

A

Yes

Like all proteins, enzyme structure can be modified by external factors such as high temperatures and extreme pH

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17
Q

What happens when an enzyme is denatured?

A

These factors disrupt the chemical bonds which are necessary to maintain the tertiary structure of the enzyme

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18
Q

Why are enzymes not able to catalyse reactions after denaturation?

A

Any change to the structure of the active site (denaturation) will negatively affect the enzyme’s capacity to bind the substrate

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19
Q

What may factors affect in order to affect enzyme activity?

A

Various factors may affect the activity of enzymes, by either affecting the frequency of enzyme-substrate collisions or by affecting the capacity for the enzyme and substrate to interact (e.g. denaturation)

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20
Q

What 3 factors can affect enzyme activity?

A

Temperature, pH and substrate concentration will all influence the rate of activity of an enzyme

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21
Q

How does low temperature affect enzyme activity?

A

Low temperatures result in insufficient thermal energy for the activation of an enzyme-catalysed reaction to proceed

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22
Q

How does increasing the temperature affect enzyme activity?

A

Increasing the temperature will increase the speed and motion of both enzyme and substrate, resulting in higher enzyme activity

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23
Q

Why does increasing temp increase enzyme activity?

A

This is because a higher kinetic energy will result in more frequent collisions between the enzymes and substrates

24
Q

When will enzyme activity be at its peak? (temp)

A

At an optimal temperature (may vary for different enzymes), the rate of enzyme activity will be at its peak

25
Q

How does a temp above the enzyme’s optimum affect its activity?

A

Higher temperatures will cause enzyme stability to decrease, as the thermal energy disrupts the enzyme’s hydrogen bonds

26
Q

Why is it harmful when the enzymes bonds break?

A

This causes the enzyme (particularly the active site) to lose its shape, resulting in the loss of activity (denaturation)

27
Q

How will changing the pH affect enzyme activity?

A

Changing the pH will alter the charge of the enzyme, which in turn will alter protein solubility and overall shape

28
Q

How will changing the pH affect the active site?

A

Changing the shape or charge of the active site will diminish its ability to bind the substrate, abrogating enzyme function

29
Q

At what pH do enzymes function the best?

A

Enzymes have an optimal pH (may differ between enzymes) and moving outside this range diminishes enzyme activity

30
Q

How does increasing substrate concentration affect enzyme activity?

A

Increasing substrate concentration will increase the activity of a corresponding enzyme

31
Q

Why does increasing substrate concentration increase enzyme activity?

A

More substrates mean there is an increased chance of enzyme and substrate colliding and reacting within a given period

32
Q

Does the rate of enzyme increase alongside an increase in substrate concentration?

A

ONLY INITIALLY

After a certain point, the rate of activity will cease to rise regardless of any further increases in substrate levels

33
Q

Why does enzyme activity reach a plateau even though the concentration of substrate is still increasing?

A

This is because the environment is saturated with substrate and all enzymes are bound and reacting (Vmax)

34
Q

What 3 variables must be considered when designing an experiment to test the effect of factors on enzyme activity?

A

Which factor to investigate (i.e. the independent variable)
Which enzyme / substrate reaction to use
How to measure the enzyme activity (i.e. the dependent variable

35
Q

What are the 4 main factors that will affect the activity of an enzyme?

A

Temperature (use water baths to minimise fluctuations)
pH (acidic or alkaline solutions)
Substrate concentration (choose range to avoid saturation)
Presence of inhibitor (type of inhibitor will be enzyme-specific)

36
Q

What are most reactions measured according to?

A

The amount / rate of substrate decomposition (e.g. breakdown of starch)
The amount / rate of product formation (e.g. formation of maltose)

37
Q

What type of enzymes are used commonly in the industry? why?

A

immobilised enzymes have been fixed to a static surface in order to improve the efficiency of the catalysed reaction

38
Q

What are the 2 main reasons for using immobilised enzymes in the industry?

A

Enzyme concentrations are conserved as the enzyme is not dissolved – hence it can be retained for reuse

Separation of the product is more easily achieved as the enzyme remains attached to the static surface

39
Q

In what 6 processes can immobilised enzymes be used?

A
  • biofuels
  • medicine
  • biotechnology
  • food production
  • textiles
  • paper
40
Q

How are enzymes used to create biofuels?

A

Enzymes are used to breakdown carbohydrates to produce ethanol-based fuels

41
Q

How are enzymes used to create medicine?

A

Enzymes are used to identify a range of conditions, including certain diseases and pregnancy

42
Q

How are enzymes used in biotechnology?

A

Enzymes are involved in a number of processes, including gene splicing

43
Q

How are enzymes used in food production?

A

Enzymes are used in the production and refinement of beers and dairy products

44
Q

How are enzymes used to create textiles?

A

Enzymes are utilised in the processing of fibres (e.g. polishing cloth)

45
Q

How are enzymes used to create paper?

A

– Enzymes assist in the pulping of wood for paper production

46
Q

What is lactose? What can break it down?

A

Lactose is a disaccharide of glucose and galactose which can be broken down by the enzyme lactase

47
Q

Why is lactose-free milk needed?

A

Historically, mammals exhibit a marked decrease in lactase production after weaning, leading to lactose intolerance

48
Q

Where is incidence of lactose intolerance particularly high?

A

Incidence of lactose intolerance is particularly high in Asian, African and Aboriginal populations

49
Q

Where is lactose intolerance less common and why?

A

Incidence is lower in European populations (due to a mutation that maintains lactase production into adulthood)

50
Q
  1. How can lactose-free milk be made (general)?
A

Lactose-free milk can be produced by treating the milk with the enzyme lactase

51
Q
  1. How is the lactase obtained?
A

The lactase is purified from yeast or bacteria and then bound to an inert substance (such as alginate beads)

52
Q
  1. How is the lactase used to create lactose-free milk?
A

Milk is then repeatedly passed over this immobilised enzyme, becoming lactose-free

53
Q

How are scientists attempting to combat the problem of lactose intolerance?

A

Scientists are currently attempting to create transgenic cows that produce lactose-free milk

This involves splicing the lactase gene into the cow’s genome so that the lactose is broken down prior to milking

54
Q

What are the 4 main ways in which lactose-free products can be useful?

A

As a source of dairy for lactose-intolerant individuals
As a means of increasing sweetness in the absence of artificial sweeteners
As a way of reducing the crystallisation of ice-creams
As a means of reducing production time for cheeses and yogurts

55
Q

Why is lactose-free milk sweeter?

A

broken down into glucose and galactose - monosaccharides are sweeter tasting

56
Q

How does lactose-free dairy products help in reducing crystallisation?

A

monosaccharides are more soluble, less likely to crystalise

57
Q

How do lactose-free dairy products reduce production time?

A

bacteria ferment monosaccharides more readily