Enzymes Flashcards

0
Q

What are some the risk factors of heart disease?

A
high sugar diet 
lack of activity 
high cholesterol 
stress 
high blood pressure
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1
Q

What are some the risk factors of cancer?

A
Sunbathing 
Xray
lack of fibre  
radiation 
infection 
reproduction
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2
Q

What are from the risk factors of both cancer and heart disease?

A

Smoking
alcohol
being overweight
genetics

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3
Q

How is food digested in the mouth?

A

Physical digestion by teeth

Amylase- starch -> maltose

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4
Q

What is the role of the stomach

A

Hydrochloric acid to denatured enzymes in pathogens

Protease- proteins -> amino acids

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5
Q

What is the role of the liver and bile duct?

A

Neutralises acid from the stomach

Emulsifies fat

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6
Q

What is the role of the pancreas?

A

Secretes pancreatic juices

Pancreatic amylase

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7
Q

What is the role of the small intestine?

A

Secretes enzymes from lining
Maltese
lactase
sucrase

(Hydrolyses enzymes)

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8
Q

What is the role of the large intestine?

A

Re-absorbs water

Absorbs nutrients

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9
Q

What monosaccharides make up maltase?

A

Glucose + glucose

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10
Q

What monosaccharide makes lactose?

A

Glucose + galactose

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11
Q

What monosaccharides make up sucrose?

A

Glucose + fructose

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12
Q

What is the Benedict’s test?

A

Used for testing reducing sugars

  1. Food sample dissolved in water
  2. And equal volume of Benedict’s reagent is added (copper sulphate)
  3. heat in a water bath
    Blue = none Red = high
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13
Q

What is the test for a none reducing sugar?

A
  1. Carry out the Benedict’s test
  2. Add the same amount of the food sample and hydrochloric acid (hydrolyses disaccharide -> mono)
  3. Reheat the sample
  4. Add sodium hydrocarbonate
    (Neutralises acid)
  5. Retest with Benedict’s reagent
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14
Q

What’s the test for starch?

A
  1. Add sample into a test tube
  2. Add a couple of drops of iodine solution

Starch present= blue/black colour

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15
Q

What do all proteins contain?

A

Nitrogen or sulphur

Peptide bonds

16
Q

What is the primary structure?

A

A sequence of amino acids

17
Q

What is the secondary structure?

A

Chain of amino acid is an alpha helix are a beta pleat

Held together by hydrogen bonds

18
Q

What is the tertiary structure?

A
Folds into 3-D structures
 hydrogen bonds 
 ionic bonds 
disulphide bridges 
hydrophobic interactions
19
Q

What is the quarternary structure?

A
Proteins greater than one polypeptide
Either globular of fibrous
Hydrogen bonds 
ionic bonds
Disulphide bridges
Hydrophobic interactions
20
Q

Why is the order of amino acids important?

A

So the bond such as disulphide bridges can be made
Amino acids need to be in the right place
If the primary structure is incorrect so the tertiary structure and therefore the preteen will not function

21
Q

What is the biuret test?

A

Add an alkali (KOH or NaOH)
Add copper sulphate
^ionisers peptide bonds

Proteins form a violet/purple colour

22
Q

What are the properties of a globular protein?

A
Small molecule 
easily transported 
disulphide bonds 
hormones or enzymes 
Hydrophobic which makes it soluble
23
Q

What are the properties of a fibrous protein?

A
Long strands 
secondary structure 
insoluble 
strong covalent bonds 
collagen (skin) keratin (hair)
24
Q

What is the effect of pH on enzyme reaction?

A

The rate of reaction decreases rapidly due to less enzymes substrate complexes forming as the active site changes as the pH affects the ionic and hydrogen bonds in the tertiary structure

25
Q

What is a competitive inhibitor

A

The inhibitor takes the place of the substrate and forms temporary bonds

26
Q

What is a non-competitive inhibitor

A

The inhibitor binds to the site other than The active site and forms permanent bonds. This changes the shape of the active site

27
Q

What is the lock and key theory

A

The substrate will only fit the specific Active site
complementary
The active site does not change shape

28
Q

what is the induced fit theory

A

The enzyme active site is flexible and changes slightly to fit the substrate
Not quite complementary
Mould around substrate causing strain on bonds

29
Q

How to increase the rate of enzyme reaction

A

More active sites( rate of reaction stops when all active sites are filled)
Increase concentration of substrate