EGGS

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 OBJECTIVES

Students are able to:

1. draw, label & describe the structure of eggs

2. describe the chemical composition & explain the function

of EWP & EYP

3. Identify the chemical reactions that occur during storage

& processing of eggs & egg products

4. Provide solutions to problems faced during processing &

storage of eggs & egg products.
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 General Functions & Composition
• Give characteristic structure, texture & appearance to
many foods/food pdts
• Form elastic films when beaten, incorporating air
needed for leavening in cakes
• Yolks are the emulsifying agents in mayonnaise, salad
dressing etc.
• Egg composition:
Part %
shell 11%
white 58%
yolk 31%
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 Chemical composition of
Egg white & Egg yolk

Egg white Egg yolk

water 88 48
protein 11 17.5
fats 0.2 32.5
minerals 0.8 2.0

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Structure of a
Chicken’s Egg

Albumen

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Shell
• Porous structure, mainly CaCo3 (94%)
• Shell contains pores for exchange of gases
• Two shell membranes, inner and outer, are found
immediately within the shell
• Keratin-like membranes that acts as chief defenses
against bacterial invasion
• Air-cell/sac – at the blunt end of the egg, formed by the
separation of the the two shell membranes as the
content shrinks on cooling

Egg white (Albumen)

3 layers:
• thin layer (outer thin albumen) next to shell,
• thicker viscous (thick albumen) layer within it
• thin layer (inner thin albumen) surrounding yolk
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Egg yolk
• Made up of concentric layers of light and dark colour
• Yolk colour ranges from light yellow to deep orange,
depending on hen's food
Germinal disc
• Is attached to the yolk - where fertilization takes place
Chalazae
• Dense, whitish cord-like strands of egg white (mostly mucin)
on opposite sides of the yolk. Their function is to support
/anchor the yolk in the centre of the albumen. Chalazae may
vary in size and density, but do not affect either cooking
performance or nutritional value
Vitelline Membrane
• Surrounds and holds the yolk, separates itt from egg white
• The fresher the egg, the stronger the membrane
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EGG WHITE
• Fresh egg white: pH + 7.6
• After a few days of storage: pH increases to 9.0 - 9.4
• Difficulty in peeling of hard boiled eggs is due to low pH
• Egg white solid contains mainly proteins

Egg white proteins

1. Ovalbumin
• Major egg white protein, a phosphoglycoprotein
• Contains all the SH groups of egg white
• Very susceptible to denaturation. Denatured by heat,
adsorption at surfaces, or in films, shaking or by other
denaturing agents
• Denatured albumin contributes to foam structure, thus
maintains structure of baked foods. If ovalbumin is used
alone, a long whipping time is necessary, other proteins are
needed, such as ovomucin
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2. Ovomucin
• A glycoprotein. Approx. 2% of egg white proteins, > in thick egg
white than in thin egg white
• Contributes to:
i) jelly-like/gelatinous structure of egg white (ie. gives thickness)
ii) Contributes to the structure of foam. If damaged, foam props
will be affected
Damage can be due to mechanical or shear stress
(eg by blending & homogenisation) which can
decrease length of ovomucin fibres
Eg of effect of homogenised/blended egg white: cake of lower
volume

3.Globulins
• Excellent foaming agent when beaten in the presence of air.
Foam is stabilised by ovomucin
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4. Ovomucoid
• Inhibitor to trypsin (~12% of egg white proteins)
• Has unusual heat stability. Can be heated to 100º with little
viscosity change or denaturation
5. Lysozyme
• Acts as an anti-bacterial agent
6. Conalbumin
• Chelates metals such as Cu n Fe. Eg when it binds with Fe, egg
inhibits microorganisms that require Fe. Conalbumin + Fe
pink colour in processed egg white, but colour disappears when
conalbumin is denatured
• Heat-sensitve but less susceptible to surface denaturation than
ovalbumin
7. Avidin
• A glycoprotein that binds biotin (a Vit B complex)
8. Flavoprotein
• Forms complex with riboflavin (Vit B2) 10
 EGG YOLK
 pH of fresh egg yolk: 6.0-6.3. A few days after storage,
pH 6.5-6.8
 Contain proteins, present mainly as Lipoproteins.
 4 types of proteins, 3 of which are Phosphoproteins:
i) Simple protein – Livetin (H2O – soluble)
ii) Phosphoproteins – Vitellin, Vitellenin, Phosvitin
Vitellin + lipid Lipovitellin High density LP,
22-26% lipid

Vitellenin + lipid Lipovitellienin Low density LP,

40-50% lipid

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 Contain lipids:
i) TAGs – 46% of yolk solids. Eg of FAs: 16:0, 18:0,
18:1, 18:2
ii) Phospholipids – 20%.
Mainly lecithin/phosphatidylcholine & cephalin/
phosphatidylethanolamine
iii) Sterols – mainly cholesterol ~3%

Much of the lipids occur in combination with proteins

Functional Properties of egg yolk lipoproteins:

1. Gelation of egg yolk during freezing process
2. Act as emulsifier (lecithin)

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 CHANGES IN EGG QUALITY
DURING STORAGE

1. Loss Of Weight
• Due to evaporation of moisture through the shell
2. Loss Of Gases (Co2)
• As CO2 is lost, the pH of egg white
• Change is from: 7.6 8.9 – 9.4
freshly laid egg

• Occurs more rapidly at higher storage temp.

• Change in egg: CO2 + H2O H2CO3
(carbonic acid)
3. Air Cell Increases In Size
• Due to loss in moisture content
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4. Gradual Thinning Of Egg White (Ref next 2 slides)
• The albumen spreads to cover a relatively wide area
when the egg is broken out of shell
• Ovomucin appears to be an important participant in the
thinning process
5. Flattening of Egg Yolk (Ref next 2 slides)
• The vitelline membrane weakens and stretches
• The network of fibres on the surface of the membrane
that are apparently part of chalaziferous layer, tends to
dissipate as the pH of albumen rises
6. Deterioration Of Odour And Flavour
• Depend upon storage conditions
• Bring about by slight changes in the protein & fat of egg

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 EFFECTS OF PROCESSING
1. Heat
• The terms denaturation, coagulation (and gelation) are used to
describe changes in egg proteins & egg pdts

Denaturation = loss of ordered arrangement due to unfolding of

polypeptide structures of proteins (ie disruption & destruction of
secondary & tertiary structures) that does not involve alteration of AA
sequence
Coagulation = conversion from a fluid to a solid state
Gelation = formation of a gel structure

• Proteins of egg white are readily denatured by heat*

• When heat is applied:
Egg white changes from clear & transparent pourable dispersion  a
white, opaque coagulated solid mass
Coagulation temp of egg white = 56°C;
Coagulation temp of egg yolk = 70°C (begins to thicken at abt 65°C)
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* & also by surface forces due to whipping – refer egg white proteins
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Factors affecting coagulation:

i) Sugar – addition of sugar  coagulation temp of egg

protein,  rate of heat denaturation due to protective
effect of sugar &  stiffness of coagulum
ii) Salt – promotes coagulation (necessary for pdtn of
custard gel
iii) Acidity – egg proteins tend to coagulate as pH . This
depends on IEP of egg protein. Eg. albumin has IEP of
4.6-4.8

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a) Effect of Pasteurisation
Aim:
to destroy pathogenic m/o while still maintaining the functional
propertiesof eggs
Process:
• Whole eggs & egg yolks are heated at temp : 65-67oC for 3½ mins.
• Egg white is pasteurised at 53oC for 2-3 mins.

Effects:
Little or no effect on egg performance, unless pasteurisation
is combined with freezing. If combined with freezing, foaming
power of egg is affected

if egg white is pasteurised at To >53oC, foaming capability of

white is damaged, reducing baking performance (That’s why
liquid egg white was previously not pasteurised, due to
damage to egg white by heat treatment)
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ii) Effect of excessive heating - formation of a
green-grey colour compound on surface of
yolk
• A green-grey coloured forms on the surface of yolk
when eggs are boiled longer than necessary, due to
the formation of ferrous sulphide, FeS (harmless)
Formation of FeS:
Fe (mg/ 100g) S (mg/ 100g)

Egg white: 0.03 211

Egg yolk: 5-6 214

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• Sulphur in egg white < stable than in egg yolk
• When egg white is heated for too long, H2S gas will be
produced in the egg white
• H2S transfers inwards towards the egg yolk (where temp
and P are lower) and then combines with Fe in the egg
yolk
H2S + Fe FeS + H2
» FeS forms on the surface of egg yolk
» Fast cooling can avoid the formation of FeS or
dark greenish colour
» If > 30 mins permanent effect

Solution: Cook eggs just long enough to harden yolk, then

place in cold H2O. Peel eggs as soon as they are cooled to
prevent gas diffusion towards yolk.
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2. Freezing
Process: eggs are pasteurised before freezing at -35oC; frozen storage
at -18 to -6oC

Effects:
Viscosity of egg yolk & whole egg increase, giving gelation due to
aggregation of low density lipoproteins (occurs at To < freezing point.
This alters the functional properties of yolk
Viscosity increase/ gelation is > in egg yolk than in whole egg
Gelation can be reversed by heating after thawing, the heat treatment
will also improve baking performance

Solution:
Apply pre-freezing treatments ie by adding cryoprotection agents eg
10% suc, glu or gal  10%  in gelation ) or by adding proteolytic
enzymes such as trypsin or papain which prevents gelation

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3. Dehydration
Process: drying by spray-drying (most common), tray
drying, plate drying etc

Effects of Dehydration:
• Loss of solubility / dispersibility
• Formation of undesirable colour changes
•  in functionality   in whipping power
• Development of off odour derivatives
•  in foaming power of yolk/whole egg at ambient temp. is
due to breakdown of fat emulsion & formation of free
surface oil

Note: The above effects are due to loss of H2O & changes in the
structure of low density lipoproteins of yolk
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 Before drying:

• Egg white, yolk & whole eggs, are treated by bacterial/ yeast
fermentation or enzymatic oxidation to remove glucose (to
make them stable during storage).
• The enzymes catalyses the oxidation of glucose to gluconic
acid – thus glucose does not participate in Maillard reaction.

If glu is not removed:

Glu + AA/protein non enzymatic browning
(Maillard Rxn)
Glu + cephalin of yolk off flavour formation

• Addition of CHO eg. sucrose to egg before drying

minimizes loss of foaming power & extends shelf-life

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