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A Level Food Technology > PROTEINS > Flashcards

PROTEINS Flashcards

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1
Q

What is a protein

A

Long chain of amino acids

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2
Q

What is a protein

A

Long chain of amino acids

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3
Q

How does protein provide energy

A

Excess protein is converted into glucose which is stored in the liver as glycogen - secondary source of energy

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4
Q

What is a protein

A

Long chain of amino acids

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5
Q

How does protein provide energy

A

Excess protein is converted into glucose which is stored in the liver as glycogen - secondary source of energy

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6
Q

Functions of protein

A

Growth and repair

Secondary source of energy

Maintains body producing enzymes/hormones

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7
Q

Sources of protein

A

Nuts

Pulses

Meat

Eggs

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8
Q

Example of protein deficiency

A

Kwashiorkor
- common in children after weaning

Symptoms

  • bloated abdomen
  • muscle wasting
  • stunted growth

Treatment
- balanced diet (more vitamins and minerals

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9
Q

Effects of excess

A

Excess calories from protein stored as tissue leads to overweight

Strain on organs (kidneys/ liver/ bowel)

Protein foods often high in saturated fat leads to CHD

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10
Q

What is protein complementation?

A

The mixture of LBV proteins as they are incomplete proteins

Two ensure that all essential amino acids are received, two incomplete sources compensate each other’s inadequate supply

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11
Q

Examples of protein complementation

A

Beans on toast

Rice and peas

Rice and kidney beans

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12
Q

What are essential amino acids

A

Amino acids that CANT be made by our bodies - must EAT them

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13
Q

What are non- essential amino acids

A

CAN be made by our bodies

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14
Q

Chemical structure of protein

A

Amino/ Acidic
Alkaline Part
Part

H             H          O 
|               |           ||
N      -     C    -     C  -  OH 
|               |            
H             R

R = Variable (changes for each amino acid)

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15
Q

What does amphoteric mean?

A

Amino acids are amphoteric because they contain at least one alkaline group and one acidic group displaying acidic and base properties

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16
Q

What are HBVs (high biological value proteins)

A

Proteins that contain all essential amino acids

17
Q

Examples of HBVs

Animal sources

A

Meat

Fish

Soya

Dairy

Eggs

18
Q

Chemical structure of protein

A

Amino/ Acidic
Alkaline Part
Part

H             H          O 
|               |           ||
N      -     C    -     C  -  OH 
|               |            
H             R

R = Variable (changes for each amino acid)

19
Q

What are LBVs (low biological value proteins)

A

Proteins that don’t contain all essential amino acids

20
Q

Examples of LBVs

Plant sources

A

Peas

Beans

Lentils

Nuts

Grains

Rice

21
Q

Chemical structure of protein

A

Proteins are large molecules built up of long chains of amino acids

Only 20 of 80 found in foods
8 of 20 are essential

Each amino acid contains at least one acidic group and one amino (alkaline) group

22
Q

What is a peptide link

A

Chemical bond linking two amino acids along a peptide chain

23
Q

What is a dipeptide link

A

When two amino acids join together

24
Q

What is a tripeptide bond

A

3 amino acids

26
Q

What is a Polypeptide chain

A

Long chain of amino acids joined together

More than 3

27
Q

What is condensation polymerisation

A

Molecule of water is eliminated during the formation of a peptide link

28
Q

Primary physical structure of protein

A

Sequence of amino acids in protein chain

Amino acid and carboxyl group take part in condensation reaction to form a peptide bond

Peptide bonds strong and can only be broken a strong acid/ enzyme

29
Q

Secondary physical structure of protein

A

Amino acids linked by various amino acids to give shape - spiral

Hydrocarbon chain different in each amino acid

30
Q

Tertiary physical structure of protein

A

Coiled/ folded chain of amino acids coiled/ folded further

More bonds form between the parts of polypeptide chain

31
Q

Globular protein - tertiary

A

Rounded in shape but not necessarily spherical

Amino acid chain folded/ molecule kept in shape by cross linkage within amino acid chain

Easy for water molecules to penetrate empty spaces within protein molecules

Example - ovalbumin in eggs

32
Q

Fibrous protein - tertiary

A

Organised arrangement/ molecules closely packed together

Cross links between between adjacent amino acids

Difficult for water molecules to penetrates the structure

Not soluble in water

Examples - gluten found in wheat

Not affected by heat

Elastic - straight fibrous protein
Inelastic - coiled in a spiral fibrous protein

33
Q

Denaturation of protein

A

Physical structure of protein is altered in irreversible way

Protein become less soluble/ more viscous

Process which proteins/ nucleic acids lose tertiary/ secondary structure by external stress

34
Q

Coagulation in protein

A

Irreversible

Involves denaturation of protein - from soluble to insoluble

Eggs are heated the egg white proteins coagulate at 60 degrees and whites become opaque forming a gel
Yolk proteins coagulate at 66 degrees and yolk thickens

Become less soluble and more viscous
Unfolded to form clumps when bonding - setting/ hardening

35
Q

Effect of heat on protein

A

Only globular proteins

Heat causes secondary structure of proteins to denature
Molecule unfolds and changes shape
Sequence of amino acids stays the same

Denaturation breaks the cross linkages maintain the shape of molecule - irreversible

Insoluble/ more viscous
Form clumps when bonding

36
Q

Effect of acids/ alkalis on protein

A

Fibrous proteins affected

A Level Food Technology (16 decks)

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