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protein Flashcards

1
Q

what elements make up protein

A

carbon, hydrogen, oxygen, nitrogen

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2
Q

what is the smallest unit of a protein

A

amino acid

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3
Q

what is created when amino acids are joined by peptide links

A

a polypeptide chain

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4
Q

what are the 5 components of an amino acid

A

an amino group (NH2), a carboxyl group(COOH), a central carbon, a single hydrogen and a variable group that changes

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5
Q

how many essential and non essential amino acids are there

A

20, 10 essential and 10 non-essential

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6
Q

how are essential amino acids obtained

A

through food as the body cannot make them.

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7
Q

how many essential amino acids do children and adults require

A

10 for children and 8 for adults

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8
Q

name three amino acids

A

lysine, leucine and isoleucine

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9
Q

what are the two essential amino acids for children

A

histidine and arginine

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10
Q

how are non essential amino acids obtained

A

they are manufactured in the body

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11
Q

name three non essential amino acids

A

alanine, cysteine and serine

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12
Q

what results when two amino acids join together

A

peptide links are formed and there is a loss of water (condensation reaction)

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13
Q
A
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14
Q

what occurs in the formation of a peptide link

A

the COOH group of one amino acid loses an OH and the NH2 group of another loses a H which form H2O that is lost. the remaining CO-NH bond, the new molecule is a dipeptide.

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15
Q

how many amino acids join together to make a polypeptide chain

A

20

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16
Q

how many amino acids join together to make a protein

A

50

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17
Q

what is the reverse of the condensation reaction

A

hydrolysis

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18
Q

what occurs during hydrolysis

A

the addition of water and enzyme action that occurs during digestions when proteins are broken back down into amino acids

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19
Q

what is the primary structure of protein

A

the order or sequence of amino acids in protein chains

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20
Q

what is the secondary structure of protein

A

involves the folding of the primary structure into two dimensional shapes, polypeptide chains either fold in on themselves or crosslink with another chain.

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21
Q

what is the purpose of protein secondary structure

A

gives proteins their unique properties eg: elasticity of gluten

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22
Q

what are the two main types of cross links

A

disulfide and hydrogen

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23
Q

what is a disulfide bond

A

occurs when two suflurs from two amino acids join together from either a single polypeptide or two different chains

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24
Q

what is a hydrogen bond

A

occurs when the hydrogen from the amino group joins with an oxygen of another amino acids carboxyl group

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25
Q

what is the tertiary structure of protein

A

involves the folding of the secondary structure into two or three dimensional shapes

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26
Q

what is the fibrous shape of protein

A

polypeptide chains are arranged in straight, spiral or zigzag two dimensional shapes

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27
Q

what are the properties of fibrous shape protein

A

insoluble in water and not easily dentaured

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28
Q

what are examples of fibrous shape protein

A

gluten, elastin and collagen

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29
Q

what do globular shape proteins look like

A

polypeptide chains are arranged in spherical three dimensional shapes

30
Q

what are the properties and examples of globular shape proteins

A

soluble in water and easily dentaured, examples: ovalbumin and lactalbumin

31
Q

what is a conjugated protein

A

when a protein combines with a non protein molecule

32
Q

what are the two subgroups of plant protein

A

glutenins and prolamines

33
Q
A
33
Q

what are the sub groups of conjugated proteins

A

lipoproteins(lecithin) and phosphoproteins (caseinogen)

34
Q

what is biological value of protein

A

a measure of protein quality that is determined by the number of essential amino acids

35
Q

where are HBV proteins found

A

mostly animal sources besides soya beans

36
Q

what are LBV proteins and where are they found

A

they lack one or more essential amino acids and are mostly found in plant sources besides gelatin

37
Q

what is an example of food with 100% biological value

A

eggs

38
Q

what is the supplementary role of protein

A

when two LBV foods are eaten together to provide all the essential amino acids

39
Q

what is an example of supplementary role of protein

A

bread lacks lysine but is high in methionine whereas beans are lacking methionine but are high in lysine

40
Q

what are the properties of protein

A

denaturation, elasticity, maillard reaction, solubility, gel formation and foam formation

41
Q

what is denaturation of protein

A

involves the unfolding of a protein chain which is irreversible, it is brought about by physical or chemicals means like heat chemicals, mechanical actions and enzymes. It results in the hardening or setting of protein foods known as coagulation

42
Q

what is a culinary application of denaturation of protein by heat

A

albumin in egg white coagulates at 60 degrees and the colour changes from transparent to an opaque and it becomes a solid

43
Q

what is a culinary application of denaturation of protein by chemicals

A

Vinegar based marinade tendersies meat by denaturation

44
Q

what is a culinary application of denaturation of protein by mechanical action

A

the beating of eggs to make meringues

45
Q

what is a culinary application of denaturation of protein by enzymes

A

the enzyme rennin in rennet causes caseinogen in milk to coagulate during cheese making forming curds and whey

46
Q

what is a culinary application of elasticity of protein

A

gluten makes yeast dough elastic enough to trap CO2 gas produced by yeast helping it to rise

47
Q

what is a culinary application of the maillard reaction of protein

A

shortbread biscuits

48
Q

what is the maillard reaction

A

the non enzymic browning of food due to a reaction between amino acids and sugar under dry heat. it produces an attractive brown colour and a crust with an appetising flavour

49
Q

what is a culinary application of solubility of protein

A

moist heat tenderises meat by converting collagen to gelatine eg during stewing

50
Q

what is a culinary application of gel formation of protein

A

setting cheesecakes and jelly sweets

51
Q

what is the gel formation of protein

A

when collagen is heated and converted to gelatine which can absorb large amounts of water which becomes trapped as the protein chains are heated, this forms a sol which forms a gel

52
Q

what is the foam formation of protein

A

when an egg white is whisked, protein chains unfold and air bubbles form , the protein traps air, creating a foam which is temporary until heated

53
Q

what is a culinary application of foam formation of protein

A

meringues

54
Q

what are the effects of dry and moist heat on proteins

A

coagulation, colour changes and overcooking causes protein to be indigestible

55
Q

what are the effects of dry heat only on proteins

A

maillard reaction

56
Q

what are the effects of moist heat only on proteins

A

tenderising meat

57
Q

what are the biological functions of structural proteins

A

production of cell membranes, muscle tissue and skin, cell repair and replacement and growth

58
Q

what are the biological functions of physiologically active proteins

A

production of hormonal proteins, enzymes, antibodies, blood proteins and nucleoproteins

59
Q

what are the biological functions of nutrient proteins

A

provide the body with essential amino acids and excess are use as an energy source when carb and fat reserves are used

60
Q

what is a result of a deficiency of structural proteins

A

retarded growth and delayed healing

61
Q

what is a result of a deficiency of physiologically active proteins

A

body organs and systems malfunction, easily infected

62
Q

what is the recommended daily allowance of protein

A

0.75g per kg of body weight

63
Q

how many kcal in 1 g of protein

A

4 kcal

64
Q

what occurs in the stomach to break down proteins

A

HCL denatures proteins, rennin breaks down caseinogen to casein and pepsin breaks down proteins into peptones

65
Q

what occurs in the pancreas to break down proteins

A

pancreatic juice is secreted into the duodenum which contains trypsin which breaks down peptones into peptides

66
Q

what occurs in the small intestine to break down proteins

A

the ileum secretes intestinal juice which contains peptidase that breaks down peptides into amino acids which can now be absorbed and utilised

67
Q

what is the order of breakdown of proteins

A

protein->peptones->peptides->amino acids

68
Q

what happens to amino acids when they enter the liver

A

they are used to maintain and repair liver cells and passed into the bloodstream and body tissues to form new cells, hormones, enzymes and antibodies

69
Q

what is deamination

A

the process by which excess amino acids are broken down in the liver, the amino group is converted to ammonia then urea and excreted and the carboxyl group is oxidised to produce heat and energy

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