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Leaving Cert Home Ec - > Protein > Flashcards

Protein Flashcards

1
Q

Elements in protein

A

Carbon
Hydrogen
Oxygen
Nitrogen

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2
Q

What element in protein is not in others? Why?

A

Nitrogen for growth

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3
Q

How are amnino acids joined?

A

Peptide links

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4
Q

What’s a chain of amino acids called

A

Peptide chain

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5
Q

What are essential amino acids

A

Amnino Acids which must be obtained from food as they cannot be produced in the body

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6
Q

What are non essential amino acids

A

Amino acids that can be produced in the body

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7
Q

What is condensation reaction

A

When peptide bonds form as amino acids join together

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8
Q

What’s the reverse of condensation reaction?

A

Hydrolysis

Occurs during digestion

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9
Q

What’s the primary structure of protein

A

Primary structure of protein is the sequence and number of amino acids in the chain
Eg insulin is 51 amino acids in a definite order

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10
Q

What’s the secondary structure of protein

A

Folding of a polypeptide chain onto another chain or itself causing a spiral shape
Spiralled proteins are called cross links
2 types disulfide and hydrogen bonds

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11
Q

Examples of cross links

A

Disulphide: two sulphurs join from the same or different polypeptide chains eg in cysteine

Hydrogen bonds: hydrogen from one chain joins with oxygen in a neighboring or same chain eg serine

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12
Q

Functions of cross links

A

Give protein their unique properties eg gluten in elasticy

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13
Q

Name all Essential Amino acids (10)

A 
Phenylalanine
Valine
Threonine
Tryptophan
Isoleucine
Methionine
Leucine
Lysine 
Histidine
Arginine
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14
Q

Amino acids that are just for kids

A

Histidine

Arginine

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15
Q

Explain hydrolysis

A

During digestion a water molecule is added to peptide links causing a reverse to occur: broken into smaller, single amino acids which are more digestible and can be used in the body

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16
Q

Important protein in meat connective tissues

A

Collagen

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17
Q

Important protein in eggs

A

Albumin

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18
Q

Import at protein in wheat

A

Gluten

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19
Q

Animal Sources of protein

A 
Cheese
Chicken
Meat
Fish
Eggs
Milk
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20
Q

Plant source of protein

A 
Soya beans
TVP foods
Nuts
Lentils
Peas
Beans
Cereals
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21
Q

Difference between HBV and LBV proteins

A

HBV contain all essential amino acids where as LBV only contain some

HBV are also known as complete proteins but LBV are known as incomplete

HBV come form animal sources and soya beans and LBV come from ponga sources and gelatine

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22
Q

RDA of protein

A

1 g for KG of body weight

Or

Extra during periods of radios growth eg kids and teenagers, pregnant women, Sick people

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23
Q

Digestion of protein

A

Mouth; food is chewed

Stomach; hydronic acid denatures protein
Enzyme rennin converts caseinogen to casein
Enzyme Pepsin converts proteins to peptones

Small intestine: enzyme trypsin from pancreas converts peptones into peptides
Enzyme peptidase from small intestine converts peptides to amino acids which are ready for absorption in the intestine

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24
Q

Where is protein absorbed?

A

Amino acids are absorbed Through the villi of the small intestine into blodstream to the liver

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25
What is protein used for in the liver
Maintain and repair liver cells Sent to bloodstream to form new cells, repair damaged cells, make hormones, enzymes, antibodies and blood proteins Excess used for heat and energy
26
Chemical structures of amino acids
``` 1 Hydrogen 1 carbon in middle 1 COOH (acidic carboxyl group) 1 NH2 (alkaline group) 1 R (variable) ```
27
How are peptide links formed
Acidic carboxyl group (COOH) of one amino acid reacts with an alkaline group (NH2) of another amino acid This eliminates a water molecule in a process Called condensation A CONH bond is formed with the remaining elements and a dipeptide link is formed
28
Tertiary structure of proteins
Secondary structure is condensed and compressed to make shapes, cross links form between proteins
29
Shapes in 3rd structure
Fibrous; straight, spiral,zigzag Globular; spherical
30
Properties of fibrous structures
Elastic or non elastic Insoluble in water Polypeptide chains in straight, zigzag or spiral shape
31
Example of fibrous protein
Gluten
32
Properties of globular proteins
Easily denatured Soluble in water Polypeptide chains in sphere 3D shape
33
Example of globular structures
Albumin
34
Classification of proteins
Simple and conjugated Simple - animal and plant Animal - fibrous and globular Plant - glutenins and prolamines Conjugated - lipoproteins and phosphoproteins
35
What’s an example of a fibrous protein
Collagen in meat connective tissue
36
What’s an example of globular protein
Ovalbumin in egg white
36
What’s an example of a glutenin
Glutenin in wheat
37
What’s an example of a prolamine
Zein in maize
37
What’s a conjugated Protein
A protein that forms when a protein combines with another non protein molecule
37
What’s a lipoprotein made of and an example of a lipoprotein
Lipid and protein Eg lecithin in eggs
37
What’s a phosphoprotein made of and an example of a phosphoprotein
Phosphate and protein Eg caseinogen in milk
38
What is the biological value of protein
Measure of quality of protein in food by % Determined by number of amino acids eg 100% protein foods will contain;all essential amino acids
39
Sources of HBV
Eggs Milk Meat Soya beans
40
Sources of LBV
Rice Wheat Maize
41
% biological value in: Eggs Milk Soya bean
100% 95% 74% (Respectively)
42
Proteins present in eggs
Livetin Ovalbumin Vitelin
43
Proteins present in milk
Caseinognen Lactalbumin Lactoglobulin
44
Proteins present in soya beans
Glycinin
45
% of biological value in : Wheat Maize
53% | 40%
46
Proteins present in wheat
Gluten
47
Proteins present in maize
Zein
48
What’s complementary/ supplementary role of protein
Consuming two LBV protein foods together ( each containing different amino acids) to ensure all essential amino acids are obtained eg beans and toast
49
Examples of supplementary value of protein
Hummus and pitta Beans on toast Lentil Dahl and Naan
50
List the Properties of protein
``` Desaturation Elasticity Maillard reaction Solubility Gel formation Foam formation ```
51
What’s denaturation
Irreversible change in shape of protein by physical or chemical means resulting in coagulation
52
Causes of denaturation
Heat - protein chains unfold and bond eg egg whites change from liquid translucent to solid opaque when fried Chemicals - acids or alkalines changes proteins shape eg vinegar based marinate (acidic) tenderises meat Mechanical action - eg whipping causing protein chains to unfold and partial coagulation eg in meringues Enzymes - they change proteins structure eg rennet causes caseinogen in milk to coagulate in cheese making forming curd and whey
53
How is elasticity a property of protein
Fibrous proteins can be elasticy eg gluten Gluten makes dough elastic enough to trap CO2 gas produced by yeast helping it to rise eg bread
54
How is maillard reaction a property of protein
It’s a non enzymic browning caused by a reaction between amino acids and sugar under dry heat creating a brown crust Eg shortbread and roast potatoes
55
How is solubility a property of protein
Most proteins are insoluble in water except collagen in meat (soluble in hot water) and albumin in eggs (soluble in cold water) Used for tenderising meat eg stew
56
How is gel formation a property of protein
Collagen (in bones and skin of meat) is heated and converted into gelatine which can absorb large amounts of heated water. Proteins chains uncoil and water becomes trapped forming a sol ( a semi viscous solution that has trapped water molecules called a gel) Eg for cheesecakes and jelly sweets
57
What’s a sol ?
A solution that contains undissolved particles evenly dispersed throughout liquid
58
How is foam formation a property of protein
When egg white sure whisked protein chains unfold and air bubbles are trapped forming a foam. Heat from whisking begins to coagulate eggs. If not heated to permanently coagulate, foam will collapse Eg meringues
59
Effect of 1.dry, 2.moist and 3.dry and moist heat on protein
1. Maillard reaction 2. Tenderise meat as collagen changes to gelatine 3. Coagulation, colour change and indigestible of over cooked
60
3 types of protein functions
Structural (build body) For growth and repair of cells, muscle and skin Physiologically active proteins (normal functioning) Produce hormones, enzymes, antibodies, blood proteins, nucleoproteins Nutrient proteins (nutritional role) Excess for energy Provide all essential amino acids
61
Deficiency diseases of proteins
``` Restarted growth Delayed healing Malfunctioning body organs and systems Increase risk of illness and infection Lack of energy ```
62
Short function of hormones
Coordinate normal body activities
63
Function of enzymes
Speed up chemical reactions
64
Function of antibodies
Defend bodies from harmful substances
65
Function of blood proteins
Move molecules around body eg plasma
66
Function of nucleoproteins
DNA for genes in chromosomes
67
RDA protein
Depend on body weight 0.75g per kg of body weight
68
Energy value of protein
1g has 4kcal of energy
69
Mouth during digestion of proteins
Breaks food
70
Stomach in digestion of protein
Produces gastric acid which contain rennin, pepsin and hydrochloric acid Rennin breaks down caseinogen into casein Pepsin breaks proteins into peptones Hydrochloric acid denatures
71
Pancreas in digestion of protein
Releases pancreatic juice which contains Trypsin Trypsin breaks peptones into peptides
72
Small intestine function during digestion of protein
In the ileum, intestinal juice is released containing peptidase Peptidase breaks peptides into amino acids to be absorbed by intestine and brought to blood stream
73
Absorption of protein
Amino acids pass through villi into bloodstream Hepatic vein transports amino acids to liver where they’re used to maintain and repair liver cells and passed into body Excess amino acids are deaminated to provide heat and energy
74
Explain deamination
Excess Procyon brought to liver Split in 2 NH2 is changed into ammonia, then urea and excreted by kidneys COOH is oxidised to produce heat and energy
75
Example of disulphide
Cysteine
76
Example of hydrogen bond
Serine

Leaving Cert Home Ec - (41 decks)

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