topic 2.5- enzymes Flashcards

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1
Q

what are enzymes?

A

globular proteins that work as biological catalysts, speeding up chemical reactions without being altered themselves

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2
Q

explain enzyme-substrate specificity

A

the shape and chemical properties of the active site and the substrate match each other- this allows the substrate to bind, but not other substances

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3
Q

what does enzyme catalysis involve?

A

molecular motion and the collision of substrates with the active site

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4
Q

state the 3 stages of enzyme catalysis

A
  • the substrate collides with and binds to the active site of the enzyme.
  • while substrates are bound to the active site they change into different chemical substances (=the products)
  • the products separate from the active site, leaving it vacant for substrates to bind again
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5
Q

define a successful collision between an enzyme and a substrate

A

collisions in which the substrate and the active site are correctly aligned to allow binding to take place

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6
Q

give 3 factors that affect the rate of activity of enzymes

A
  1. temperature
  2. pH
  3. substrate concentration
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7
Q

how does temperature affect enzyme activity?

A
  • higher KE; enzymes and substrates move around faster -> increased frequency of collisions between substrate and active site
  • when enzymes are heated, bonds in the enzyme vibrate more and the chance of the bonds breaking increases, meaning the shape of the enzyme and its active site changes (= denaturation)
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8
Q

how does pH affect enzyme activity?

A

most enzymes have an optimum pH- at either side of this pH, the structure of the enzyme is altered, including the active site. beyond a certain pH, denaturation occurs

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9
Q

how does substrate concentration affect enzyme activity?

A
  • if conc of substrates increases, substrate-active site collisions will take place more frequently and the rate of reaction will increase
  • however, as it rises, more and more of the active sites are occupied at any moment, meaning a greater proportion of substrate-active site collisions will be blocked- plateaus.
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10
Q

what happens during enzyme denaturation?

A

the active site is altered so the substrate can no longer bind (enzyme may also become insoluble)

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11
Q

what does catalase do?

A

catalyses the conversion of hydrogen peroxide into oxygen and water

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12
Q

define enzyme immobilisation

A

the attachment of enzymes to another material or into aggregations, so that the movement of the enzyme is restricted, but in such a way that it retains its full activity or most of its activity.

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13
Q

state 3 ways in which an enzyme could be immobilised

A
  • attaching the enzymes to a glass surface
  • trapping the enzymes in an alginate gel
  • bonding enzymes together to form enzyme aggregates
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14
Q

state 4 advantages of immobilising enzymes

A
  • enzyme can easily be separated from the products of the reaction; reaction stopped at ideal time and products not contaminated
  • enzymes retrieved from reaction mixture and can be reused; saves costs
  • increases stability of enzymes to changes in temperature and pH, reducing the rate at which they are degraded and have to be replaced
  • substrates can be exposed to higher enzyme concentrations than with dissolved enzymes, speeding up ROR
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15
Q

how is lactose free milk produced?

A

lactose —(lactase)–> b glucose + galactose

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16
Q

give 4 advantages of lactose free milk

A
  • some people are lactose intolerant
  • galactose and glucose are sweeter than lactose, so less sugar needs to be added to sweet foods containing milk
  • lactose tends to crystallise during ice cream production, giving a gritty texture- glucose and galactose are more soluble so they remain dissolved, giving a smoother texture
  • bacteria ferment glucose and galactose faster than lactose, so the production of yoghurt/cottage cheese is quicker