Protein Flashcards

1
Q

Element

A

Carbon
Oxygen
Hydrogen
Nitrogen

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2
Q

Basic structure amino acid

A

Labelled

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3
Q

Formation of peptide link

A

Oxygen and hydrogen from first amino acid in the carboxyl group joins with the first hydrogen in the amino group in their second amino acid which forms water
The end of carbon and oxygen in the first amino acid in the carboxyl group joins with nitrogen and a seven hydrogen in the amino group and the second amino acid which forms the peptide link and the process is called condensation process

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4
Q

Essential amino acid

A

Cannot be made in the body and must be obtained from food

Example histidine, argarinine

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5
Q

Non-essential amino acid

A

Made in the body and not essential to go from food

Example proline

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6
Q

Three structures of protein

A
  1. primary structure
  2. secondary structure
  3. territory structure
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7
Q

Primary structure

A

Order a number of amino acid in the protein chain

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8
Q

Secondary structure

A
Coiling of primary structure giving spiral shape
Held in place by either=
1. disulphide bond 
Or 
2. hydrogen bond
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9
Q

Tertiary structure

A

Folding of the secondary structure
A) fibrous eg gluten base difficult to tear
Or
B) globular eg albumin in egg white

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10
Q

Classification of proteins

A
  1. simple proteins

2. conjugated proteins

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11
Q

Simple proteins

A

Animal - fibrous e.g. collagen in meat
- globular e.g. albumin in egg white
Plant - glutenins e.g. gluteninin in wheat is soluble in acid and alkaline
- prolamins e.g. zein in maze is soluble in alcohol

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12
Q

Conjugated proteins

A
  • Protein combines with non-protein molecule
  • e.g. lipoprotein e.g. lechtin in egg yolk
  • e.g. phosphoprotein e.g. caesinogen in milk
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13
Q

High biological value protein

A

Contains all the essential amino acid in the correct proportion needed by the body
e.g. eggs milk cheese meat

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14
Q

low biological value protein

A

Does not contain all essential amino acids in the correct proportion a divided body
e.g. wheat maize rice

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15
Q

Complimentary/ supplementary value protein

A

Two low biological value protein foods combined together so all essential amino acids are in the correct proportion a divided body
e.g. beans (lysin) on toast (methionine)

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16
Q

Properties/characteristics

A
Denaturation
 Mailard reaction 
solubility 
elasticity 
Gel formation
Foam formation
17
Q

Denaturation

A
Invertible change in protein structure 
Caused by 
heat eg fried eggs
chemicals eg lemon juice curdle milk
agitation eg whipping eggs white foam
enzymes eg renin causes casein in milk form curd cheese
18
Q

Mailard reaction

A

Amino acid+sugar+dry heat= browning

Eg toast

19
Q

Solubility

A

Insoluble in water accept albumin in egg white

20
Q

Elasticity

A

Fibrous protein elastic

e.g. gluten and bread

21
Q

Gel formation

A

Collagen heated from gelatine setting agent used in cheesecakes jelly and sweet
can absorb large amount of water when heated

22
Q

Foam formation

A

Egg white whisked
form temporary foam trapping air
Oven sets as permanent foam

23
Q

Digestion

A

Stomach- gastric juice - rennin/ Pepsin
pancreas- pancreatic juice - trypsin
small intestine- intestinal juice - peptidase

24
Q

Dry and moist heat effect on protein

A
  • coagulation eg egg white coagulate at 60’C and yolk at 68’C
  • colour change (myoglobin (red pigment) to haematin(brown pigment)
  • overcooking (indigestible)
25
Q

Dry heat affect on protein

A

Mailard reaction eg roast beef

26
Q

Moist heat effect on protein

A

Tenderising meat= collagen in meat coverts to gelatine causing fibres to tenderise eg pulled pork

27
Q

Stomach

A

Gastric juice
= rennin - caesogin - casein
= pepsin - protein - peptones

28
Q

Pancreas

A

Pancreatic juice

= trypsin- peptones - peptides

29
Q

Small intestine

A

Intestinal juice

= peptidase - peptides - amino acids

30
Q

Deamination

A

Excess amino acids broken down by the body in the liver
=NH2 - ammonia + urea = excreted as urine through kidneys
=COOH - oxidised for heat and energy