Extra Enzymes Flashcards

1
Q

What are catabolic reactions?

A

The breakdown of molecules (hydrolysis)

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2
Q

What are anabolic reactions?

A

The building up of molecules (condensation reaction)

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3
Q

Describe the structure of an enzyme.

A

Globular protein (soluble, spherical), biological catalysts, R groups on the outside, tertiary

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4
Q

What are the two models for enzyme reactions?

A

The Lock and Key Model, The Induced Fit Model

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5
Q

Give an example of an enzyme which emphasises the induced fit model.

A

Lysozyme

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6
Q

Define activation energy.

A

The minimum energy needed for molecules to collide and react

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7
Q

What effect do enzymes have on activation energy?

A

Lowers activation energy, so reactions take place at lower temperatures

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8
Q

What is the equation for % increase in mass?

A

The increase in mass/initial mass x 100

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9
Q

What do extreme changes in pH cause?

A

Enzymes to denature as bonds are disrupted

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10
Q

Define enzyme turnover number

A

The maximum number of substrate molecules an enzyme can convert into products per unit time

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11
Q

What key terms could you use for enzymes?

A

Active site, specific, complementary, successful collisions, enzyme-substrate complex, kinetic energy

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12
Q

Define immobolised enzymes.

A

Enzymes bound to an inert matrix e.g. alginate beads

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13
Q

Describe the process of immobolised enzymes

A

Substrates are added to the top, as they flow down they react with the enzymes, product is released from the bottom

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14
Q

Why are immobolised enzymes stabler?

A

Create a microenvironment allowing them to denature at higher temps and pHs

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15
Q

Give 3 examples where immobolised enzymes are used?

A

In lactose free milk (lactose broken down), HFCS, biosensors

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16
Q

Explain the role of biosensors.

A

Is an enzyme and a transducer which can detect specific molecules by converting chemical signals to electrical (quantitative data). Detects diabetes. Blood put in, urea passes through partially permeable membrane, glucose detected.