A PROJECT REPORT

ON
“EFFECTS OF USING EGG PROTEIN IN BAKING AND IT’S
CONSEQUENCES IN CONFECTIONERY”

Under the supervision of

Mr. Ankit Mishra
(SUPERVISORS NAME)

DISSERTATION REPORT SUBMITTED TO

IHM RIG
IN PARTIAL FULFILLMENT OF THE REQUIREMENT FOR THE
AWARD OF
RESEARCH PROJECT

STUDENT NAME:-MANISH PANDEY

ROLL NO:-1841317044

CERTIFICATE OF THE GUIDE

This is to certify that the project work entitled EFFECTS OF USING EGG PROTEIN IN BAKING
AND IT’S CONSEQUENCES IN CONFECTIONERY submitted in partial fulfillment for the award
of the degree of b.sc in hospitality and hotel administration by NCHMCT , noida in
collaboration with IGNOU, New delhi having is an authentic work carried out by him under
my complete guidance. The matter embodied in this project work has not been submitted
earlier for the award of any degree or diploma to any other institution to the best of my
knowledge and belief.

SIGNATURE OF PRINCIPAL SIGNATURE OF GUIDE

NAME OF THE EXAMINER SIGNATURE OF EXAMINER

TABLE OF CONTENTS

1.GENERAL INTRODUCTION 04

2.EGG BREAKDOWN 08

3.LITERATURE REVIEW
EGG WHITE PROTEIN 15
BLOOD PLASMA PROTEIN 18

4.FUNCTIONALITY OF EGG PROTEIN IN BAKING 28

5.AIMS AND OBJECTIVE 32

6.RESEARCH METHODOLOGY 33

7.DATA COLLECTION AND ANALYSIS 34

8.RESULT AND DISCUSSION 35

9.CONCLUSION 42

10.BIBLIOGRAPHY 44
 INTRODUCTION
Shelled eggs might be mostly sold by the dozen, but they are not a smart choice
for most bakers. Not only is it time consuming to break eggs, but there’s always
that chance of shell getting into the recipe. Further, shelled eggs are inconsistent
in size and even composition, based on time of year and the hen’s diet; therefore,
most bakers rely on egg products, which come dry, liquid and frozen. They can be
separated into whites and yolks, and even blended with other ingredients for
enhanced functionality.

“Eggs have 20-plus functions, from adhesion to aeration and from binding to
browning,” said Toby Moore, bakery professional, AIB International.

Eggs influence overall appearance, flavor and color as well as texture, batter
quality, moisture/water activity and overall likability in baked foods.

“There are a whole host of different egg products that offer different functionality,
and it’s important to communicate with your egg product supplier to be sure
you’re using correct egg product to ensure the application is receiving the
maximum benefits from the egg’s functionality,” he added. “Egg whites, for
example, are available as standard, high whip — sometimes called angel whites
— and high-gel, and each contributes a different functionality to various
applications.”

Standard egg whites would be appropriate for frittata bites. High whip, on the
other hand, would be best for meringue. In complex systems such as nutrition
bars, high-gel egg whites not only assist with adhesion and texture, but they also
contribute protein.

Egg products are pasteurized to ensure food safety. They’re easy-to-use and
provide batch-to-batch consistency.
“Egg functionality is unique and difficult, if not impossible, to fully replicate,
especially with a single ingredient,” Mr. Moore said.

Research supported by the American Egg Board and conducted by CuliNex

explored typical baked foods made with egg products and compared them to
similar products made using egg replacers. Results showed that in many
applications, there’s a discernable difference with the real-egg product superior in
many features.

“Let’s consider sugar cookies, although many other cookie formulations that rely
on eggs for binding, flavor, leavening and texture would have similar results,” Mr.
Moore said. “The areas of sugar cookie quality most negatively affected when
eggs are removed are aroma, color, flavor and texture. Without eggs creating
proper spread and rise, the cookie batter is too thin and spreads too much in the
heat of the oven. Also, aroma is reduced as well as flavor intensity, indicating that
eggs contribute to the characteristic sweet baked good aroma and flavor of sugar
cookies.”

Eggs are an integral ingredient in most cakes. They provide leavening, binding,
aeration and contribute to texture, flavor, color and aroma.

“Eggs contribute to the color, rise and uniformly open cell structure, which
influences eating quality, mouthfeel and texture,” Mr. Moore said. “They also
provide a sweet, eggy baked aroma and flavor. The tender crumb and eating
quality of the cake is also due to eggs.

“When eggs are absent, the cake is fragile. The cake breaks readily upon handling
and forms a gummy mass in the mouth.”

It’s just not sponge cake without eggs. The same is true of angel food cake, a cake
designed on its creative use of egg whites to achieve a highly aerated structure
that is tender in the mouth and has a fluffy texture with neutral sweet baked
flavor. Without egg whites, that aeration doesn’t happen.

“The batter is four-times denser and much lower in viscosity, indicating that
without egg whites there is no batter aeration,” Mr. Moore said. “This results in a
squat, firm, chewy, pasty-tasting, gel-like substance rather than the expected angel
food texture and mouthfeel.”
Meringues, macaroons and macarons also rely on aeration from egg whites. As
their name suggests, the whites also allow for a clear, clean canvas to add flavor
and color. And while historically designed to be delicate sweet treats, these
classics have been turned into savory snacks by innovative bakers.

“We developed superfood pesto puffs, which are crisp, savory meringues packed
with spinach, kale, basil, almonds, parmesan cheese, and garlic,” Mr. Moore said.
“They are low in calories, packed with vitamins and minerals and a source of
protein.”

Outer Aisle, Santa Barbara, Calif., relies on whole eggs to make gluten-free, low-
carb, bread alternatives. In combination with cauliflower, Parmesan cheese and
nutritional yeast, the company produces pizza crusts and sandwich thins in a range
of flavors. Crepini, New York, makes grain-less wraps and thins based on eggs
and cauliflower.

Egg-based ingredients offer a wealth of functionality and flavor in the baked

foods that use them. These recognizable ingredients in an industrial format
provide bakers with a convenient road to improved product quality.

EGG BREAKDOWN
The eggs most commonly used in baking are chicken eggs and that
is what we are talking about here today. Eggs are such an important
part of the baking process that its important to understand what
exactly we’re dealing with.

EGG MAKEUP

An egg is made up of two main parts: the egg white and the yolk. The
egg white is mostly made up of water and proteins while egg yolks is
very fatty and nutrient dense. Eggs also contain a thin white strand
called the chalaza. The chalaza works to center the egg yolk and for
almost all baking purposes is fine to leave in the egg, though some
bakers prefer to remove it when making things like custard.

EGG SIZING

Large eggs are by far the most common used for baking. Eggs are
labeled by size according to their weight and therefore all large eggs
contain a fairly similar amount of yolk and white and small differences
won’t matter for everyday baking. Sometimes, recipes do list egg
amounts by weight and when this happens this is a fairly good
indication that precise measurements of the egg are very necessary
for the recipe.
If using farm fresh eggs, the sizes can vary greatly in a carton. If you
are making a recipe that only calls for 1 or 2 eggs, likely the size isn’t
going to matter a great deal. Substituting 1 medium egg for 1 large
egg is likely going to work out just fine. However, this can become
incrementally more crucial as you make large batches of things.
Substituting 10 large eggs is not quite as direct as substituting 1.
Below is a chart of common egg sizes for your reference as well as a
chart for how to substitute for large batches.

CHICKEN EGG STANDARD VOLUME

SIZE VOLUME YIELD

Small 2.5 TBSP (38 ml)

Medium 3 TBSP (43 ml)

Large 46 ml (3.25 ml)

Extra-Large 56 ml (1/4 cup, 4 TBSP)

Jumbo 60 ml (1/4 cup, 4 TBSP)

EGG SUBSTITUTING CHART

HOW AMOUNT AMOUNT AMOUNT AMOUNT
MANY OF SMALL OF MED OF X- OF JUMBO
LARGE TO USE TO USE LARGE TO TO USE
EGGS USE
RECIPE
CALLS FOR

1 1 1 1 1

2 3 2 2 2

3 4 3 3 2

4 5 5 4 3

5 7 6 4 4

WHITE VS BROWN EGGS

The only difference between brown eggs and white eggs is the breed
of chicken they come from. There is no difference nutritionally
between a brown egg and a white egg.

Brown eggs have long been associated with the eggs from chickens
that are raised more naturally (organic & free range) and therefore
must be better eggs, however white eggs can just as easily come
from chickens that are also raised this way.

FUNCTIONS OF EGGS IN BAKING

ROLE OF THE WHOLE EGG

The whole egg is made up of a great deal of water as well as protein

and fat. These three components work together to perform quite a
few different functions in baking.

 Whole eggs work to bind baked goods together because of the protein
content and how it gels as the egg heats up. This adds structure and
strength to baked goods.
 Because whole eggs contain so much water content they also help with
the leavening. You’ll remember from the last lesson about how leavening
works in baking that steam is a powerful source of leavening. As the water
evaporates off of the eggs it helps to lighten and leaven our baked goods.
 Whole eggs also add flavor, color, and richness to our baked goods.
The higher the ratio of egg in a recipe the more yellow in color and the
more “eggy” it will taste.
 Whole eggs also add tenderness and moisture to baked goods.

ROLE OF EGG WHITE

The egg white, also known as the albumin is about 2/3 the total
volume of the egg and is made up of mostly water and some
protein. Because of this makeup, egg whites perform play very
different roles in baking than egg yolks which are filled with fat.

 Egg whites can be whipped to create an egg white foam. This foam is
filled with tons of air which helps to lighten and leaven baked goods. If
you made the angel food cake from the sugar lesson then you definitely
saw this in action. Egg white foams leaven everything from cakes to
souffles and can be used as a stand alone as meringue.
 Egg whites are very neutral in flavor so they really do not contribute to
the flavor of your baked good like the yolks do.
 Because egg whites contain a great deal of water and no fat they tend
to have a drying effect on baked goods. However, the can be used in
 conjunction with a high ratio of sugar, like in the angel food cake, to keep
baked goods moist.

ROLE OF EGG YOLK

An egg yolk makes up the other 1/3 of the egg and contains a high
percentage of fat as well as protein and water. When recipes call for
yolks only it is typically because the fat content as well as the yolks
ability to emulsify is desired. It is also important to note that yolks
prevent egg whites from whipping into a foam which is why they need
to be carefully separated when a recipe calls for it.

 Egg yolks add richness to baked goods due to the fat content.
 Egg yolks are great emulsifiers meaning they work to combine liquid
and fats into one cohesive mixture. This is evident in baking mayonnaise
and hollandaise sauce, but in baking it creates a smoother and more
homogeneous batter or dough.
 Egg yolks add flavor and color to baked goods.
 Egg yolks also thicken mixtures when they are heated because the
proteins begin to denature and gel . You can see this very clearly in
 custards like pastry cream. When the mixture begins to heat up it thickens
greatly.

USING EGGS IN BAKING

TEMPERATURE OF EGGS

The general rule of thumb in baking is to use eggs at room

temperature. There are very few instances where a cold egg is
desirable in baking and eggs absorb into batters more readily at room
temperature.

This matters more in some recipes than it does in others. Typically if

you throw cold eggs into something very forgiving like a cookie dough
or a muffin batter you are going to be just fine. But in some recipes,
like pound cake, where most of the leavening happens by the
creamed butter and sugar, it is more crucial to have room
temperature eggs because cold eggs can break the butter/sugar
emulsion you created. Egg whites also gain the most amount of
volume when making an egg white foam if they are around 70
degrees F.
 LITERATURE REVIEW
EGG WHITE PROTEINS
Egg white consists of 88.9% water, 9.7-10.6% protein, 0.03% lipid, 0.5-0.6% ash,
and 0.4-0.9% carbohydrate. About 0.4% of the carbohydrate of egg white is in the
free form, and 98% of the free form is glucose. The major proteins of egg white
are classified as ovalbumin, conalbumin, ovomucoid, lysozyme, and globulins.
The relative amounts of various proteins in egg white and some of their properties
are shown in Table II.

Proteins in Egg Albumen’

Proteins Albumen pl’ Molecular HP’ Tod

(%,dry basis) weight
(cal/rea) (OC
 )
Ovalbumin 54 4.5 44, 500 1110 84.0

Conalbumin 12 6.1 76,000 1080 61.0

Ovomucoid 11 4.1 28,000 920 70.0

Ovomucin 3.5 4.5-5.0 5.5-8.3 x 106 - -

Lysozyme 3.4 10.7 14,300 970 75.0

G2 Globulin 4.0 5.5 3.0-4.5 x 104 - 92.5

G Globulin 4.0 4.8 - - -

Ovoinhibitor 1.5 5.1 49,000 - -

Ficin inhibitor 0.05 5.1 12,700 - -
Ovoglycoprotein 1.0 3.9 24,400 -
Ovoflavoprotein 0.8 4.0 32,000 - -
Ovomacroglobulin 0.5 4.5 7.6-9.0 x 10 - -
Avidin 0.05 10.0 68,300 1060 -

Taken from (Powrie and Nakai

|soeIectric point
.
Average hydrophobicity.

enaturation temperature.

Donovan et al (1975) studied the heat denaturation of egg white and its
component proteins by DSC (Table III). In this study, egg white at pH 7 gave
major endotherms at 65 and 84.5°C, produced by the denaturation of conalbumin
and ovalbumin, respectively. The stability of conalbumin to heat denaturation in
egg white increased by 4.5°C when pH was increased from 7 to 9. However, this
increase was only 1°C when isolated conalbumin was utilized. Heg et al (1978)
found that the denaturation temperature (Ty) of conalbumin was independent of
pH in the range of 5 to 10, while T^ decreased below pH 5. In this study, Tj was
also found to be independent of NaCI concentrations at all pH values above 4.
Addition of aluminium ion increased the heat stability of conalbumin by 12°C
(Donovan et al 1975). Lysozyme was more stable to heat denaturation at pH 7
than at pH 9.
Ovalbumin maintained its conformational stability in the pH range of
6 to 9, and below pH 6 the denaturation temperature of ovalbumin steadily
decreased (Hegg et al 1979). Later, the work of Arntfield et al (1989) showed that
the denaturation temperature of ovalbumin was not significantly different between
pH 5 to 9. When the calorimetric experiments were carried out in the presence of
NaCI (0.1-0.4 ly/l), only slight increases in the denaturation temperatures of
ovalbumin were observed which implies that NaCI has little influence on the
maintenance of

Denaturation Temperatures of Egg White Proteins’

Denaturation Temperature b
In Egg White Isolated*

Protein pH 7 pH 9 pH 7 pH 9
Ovalbumin 84.5 84.0 84.0 84.0

Lysozyme 74.0 Cd 75.0 72.5

Conalbumin 65.0 69.5 61.0 62.0
Ovomucoid C C 79.0’ 77.0’

Globulins C c 9z.s Nog

aAdapted from Donovan et al (1975).

bDefined as peak in endotherm at 10 oC/min heating rate.
°In water, except where noted.
d
Concealed by denaturation of conalbumin or ovalbumin in egg white.
e
2 M tris buffer at pH 7.10 and pH 8.68.
’0.1 M phosphate buffer, pH 6.8; 0.1 M TAPS buffer (3-(tris
(hydroxymethyl)methyI]amino) propanesulfonic acid), pH 9.0.
*Not determined.

conformational stability of ovalbumin (Arntfield 1989). However, even at a

concentration as low as 17 mM, CaClg destabilized protein structure and
decreased ovalbumin thermal stability by 2-3°C at all pH values above 5.0 (Hegg
et al 1979). Addition of 10% sucrose increased the denaturation temperatures of
major egg white proteins by 2°C, presumably a suppressive effect of this solute on
water activity (Donovan et al 1975). The irreversible transformation of ovalbumin
into its more heat-stable form, S-ovalbumin, during storage of eggs at elevated 16
temperatures was determined by Donovan and Mapes (1976). The denaturation
temperature of S-ovalbumin was 8°C greater than that of ovalbumin.

BLOOD PLASMA PROTEIN

DSC has been used to study thermal stabilities of ligand-serum albumin

complexes (Gumpen et al 1979). The fatty acids, lauric acid and stearic acid,

stabilized the protein molecules and increased the denaturation temperature of

serum albumin. A maximum increase in the denaturation temperature of 30oC

was obtained with lauric acid. The denaturation peak

temperature of ligand-free serum albumin increased from 68 to 83oC with

stearic

acid and to 92oC with lauric acid. pH variations in 0.9% NaCI affected the heat

stabilities of both ligand-free and ligand-rich albumin; the former being more

sensitive in alkaline pH. The fatty-acid-free form of the protein was destabilized

when the salt concentration was decreased below 0.9% and was significantly

stabilized by the addition of more salt, contrary to fatty acid-stabilized protein

which was slightly destabilized by the addition of small amounts of salt.

The effects of pH and ionic strength on defatted and SH-blocked bovine

serum albumin were studied by Yamasaki et al (1990). They found that bovine

serum albumin (BSA) was stabilized in the neutral-alkaline pH range by the

presence of NaCI, but was destabilized in the acidic pH range. The enthalpy of

denaturation was maximum in the pH range 5.6-7.0. The stabilizing effect of

NaCI on BSA was attributed to its neutralizing effect at low concentration on

the electrostatic forces in the pH range 5.6-7.0.

FOAMING PROPERTIES

Foams are defined as colloidal dispersions in which gas bubbles are

dispersed in a liquid or semi-solid phase that contains a soluble surfactant

(Cheftel et al 1985). A surface-active agent is necessary to maintain the

interface against coalescence of gas bubbles by lowering the interfacial tension

at the gas/liquid interface and forming an elastic protective barrier between gas

bubbles. Many foams are unstable, and the main destabilizing mechanisms are:

1) drainage of lamella liquid due to gravity and pressure difference; 2) gas

diffusion from small to large bubbles; and 3) rupture of the liquid lamellae

separating gas bubbles (Cheftel et al 1985).

Some proteins can form protective films at gas/liquid interfaces. In

protein- based foams, two adjacent bubbles consist of two adsorbed protein

films separated by a thin liquid layer called "lamellae.“ The three main foam

formation methods that have been used in studies of proteins are (Halling 1981,

Cheftei et al 1985): 1) bubbling gas through a porous sparger (such as sintered

glass) into an aqueous solution of a low protein concentration (0.01-2% w/v); 2)

whipping/beating an aqueous protein solution (1-40% w/v) in the presence of a

bulk gas phase; and 3) shaking an aqueous protein solution (foam formation

resembles whipping). The later method has been used only rarely because of

difficulty in standardizing of the method.

Foaming properties of proteins depend upon the intrinsic physical properties of

protein such as molecular size, shape, conformation, flexibility, rigidity,

compactness, surface polarity, charge, hydrophobicity, etc., (Kinsella 1981).

These, in turn, are affected by the processing history, and by the physical and

chemical environment in which the protein is used. In a protein foaming system,

foam formation involves three sequential stages: 1) diffusion of the soluble

proteins to the air-water interface and adsorption at the interface; 2) unfolding

and rearranging of polypeptides (polar moieties toward the water) at the

interface; and

3) interactions between the polypeptides to form a continuous film (Kinsella 1981,

Morrisey et al 1991).

The effect of protein conformation on the surface properties of proteins

were
determined using three well-defined proteins by Graham and Phillips (1975).

Interfacial adsorption and foaming properties of §-casein (non-structured

flexible random coil), lysozyme (highly ordered, rigid, inflexible, globular),

and BSA (less ordered, more flexible, globular) were compared under

standard conditions and at several protein concentrations. §-casein rapidly

adsorbed at the surface and attained a stable film pressure. It took much longer

for albumin to reach a constant film pressure, and lysozyme adsorbed very

slowly. The relative foaming abilities (time to reach half maximum volume)

of §-casein, albumin, and lysozyme

were 4, 12, and over 30 min, respectively.

Molecular flexibility is an important structural factor governing the foaming

properties of proteins (Kato et al 1985). Flexible proteins unfold, adsorb, and

spread rapidly at the interface facilitating foam formation. When the

molecular flexibility of serum albumin or lysozyme is reduced by the

introduction of additional intramolecular cross-linking, there is corresponding

losses of foamability and foam stability (Kato et al 1986a). Prior denaturation

of globular proteins, such as ovalbumin and lysozyme, by heat without loss of

solubility leads to enhanced foamability due to increased flexibility as

determined by susceptibility to protease digestion (Kato et al 1986b), and to

an increase in surface hydrophobicity and protein-protein interactions (Kato et

al 1989). Mitchell (1986) attributed the beneficial effect of heat denaturation

on foaming properties of proteins to two factors, increased surface activity on

denaturation and stabilization by solid particles.

It has long been recognized that many properties of proteins can be

related to the proportion of amino acids having non-polar side chains.

Townsend and Nakai (1983) showed that foaming capacity increased with

Bigelow’s average hydrophobicity (this parameter was evaluated by adding

together the side chain hydrophobicity of the individual non-polar amino acid

residues and then dividing by the total number of residues in the protein) and

the relationship between surface hydrophobicity and foaming properties were

much less significant (Kato et al 1983).

The stabilities of foams reflect the rheological properties of interfacial films of

proteins. Foam stability requires formation of a thick, cohesive, elastic, viscous,

continuous, and air-impermeable protein film around each gas bubble through

hydrophobic and possibly hydrogen and electrostatic interactions (Kinsella

1981). The formation of cohesive films around gas bubbles is facilitated by

some degree of surface denaturation which encourages protein-protein interaction

and enhances cohesive forces between proteins in the film. However, complete

denaturation cauces membrane fragility and foam collapse; therefore, it is not

desirable.

Besides the intrinsic physical properties of proteins, several other

factors, such as protein concentration, pH, solubility, salt, sugars, and lipids,

can affect the foaming properties of proteins (Kinsella 1981, Halling 1981).

Foam volume and stability usually increase with increasing protein

concentration (Kinsella 1981, Halling 1981). Increased stabilities at higher

protein concentrations were attributed to the formation of thicker interfacial

films (Kinsella 1981) and to the increase in liquid viscosity brought about by

protein (Halling 1981). However, Dickinson and Stainsby (1982) stated that

there was no correlation between foam stability and film thickness. Halling

(1981) also suggested that in solutions which contain more than one protein an

important surface role of a minor component may account for the continued

increase of foam stability at higher protein concentrations. The dependence of

both foam capacity and stability on viscosity was attributed to three factors by

Mitchell (1986): a high viscosity will 1) slow down the rate of drainage of

lamellae; 2) decrease the rate at which the bubbles move through the solution,

thereby increasing the time for protein adsorption and unfolding; and 3) be

indicative of a more unfolded protein in solution.

Since pH of the dispersing medium has a direct effect on the net charge and

conformation of the protein, it consequently affects foaming properties,

especially foam stability. Generally, completely soluble proteins show good

foam stability at their pis due to electrostatic intermolecular attractions at the

pl increase the thickness, elasticity, viscosity, and rigidity of the protein films

adsorbed at the air/water interface (Kinsella 1981). Egg white has maximum
foam stability at either its natural pH (8-9) or around the pl of its component

proteins (4-5) (Halling 1981). Plasma exhibited better foaming properties at

pH 4.8, around the pl of its component proteins, than at its natural pH (8-9)

(Tybor et al 1975).

The relationships between protein solubility and foaming properties are

rather complex. Although some studies show a correlation between protein

solubility and foam formation or stability, others do not. These studies are

listed in the review of Halling (1981).

Since ions can affect the solubility, viscosity, unfolding, and aggregation

of proteins, they can also affect foaming properties. NaCl weakens interpeptide

attractions and reduces surface viscosities and rigidities of protein films

(Cumper 1953). NaCI usually increases foaming capacity but may reduce film

strength that cause decreased foam stability (Kinsella 1981). However, some

proteins give better foams with finer bubbles as ionic strength increases

(Cumper 1953).

Sucrose and other sugars increase viscosity and, therefore, improve foam

stability. Foam stability of egg albumen was related to its glyco-residues

(Kinsella 1981).

Presumably the glyco-residues of egg albumin are exposed to the

lamellar water and increase the viscosity of this water thereby retarding

drainage. Foaming properties of proteins can be significantly reduced

by the presence of polar lipids (e.g., phospholipids) which compete for

the air-water interface and disrupt the interfacial film by causing

reorientation of the hydrophobic surface of protein (Kinsella 1981,

Halling 1981).

EMULSIFICATION PROPERTIES

An emulsion is a dispersion of two immiscible or sparingly soluble

liquids, usually an oil phase and a water phase, separated by a third component,

an emulsifier. Many food products are emulsions and protein constituents often

play a major role in stabilizing these colloidal systems. Proteins reduce

interfacial tension by diffusing and adsorbing at the interface between dispersed

oil droplets and the continuous aqueous phase.

Emulsifying properties are important in many food applications of ingredient

proteins, and these are commonly determined as emulsifying capacity (EC)

and emulsifying activity (EA). EC is determined by stirring an aqueous

protein solution while oil is added steadily. After a certain volume has been

added, the emulsion in the mixture undergoes a sudden change referred to as

either "inversion" or "breaking". This is the end point of titration, and the

volume of oil added is taken as a measure of the emulsifying capacity. The EC

denotes the maximum amount of oil that is emulsified under specified

conditions by a standard amount of protein. EA requires small quantities of

protein and is determined by a turbidimetric technique. In this method, the

emulsion is prepared by homogenizing a measured amount of oil and aqueous

protein solution together in a blender. The emulsion is diluted and the

turbidity of the diluted emulsion is determined at 500 nm. The

EA of proteins is expressed as the absorbance at 500 nm of diluted emulsions.

The
absorbance is proportional to the total interfacial area (m2/g, defined as
emulsifying

activity index) and, hence, the inverse square of droplet size (Pearce and

Kinsella 1978, Halling 1981).

A number of studies have been done on the relationship between protein

structure and emulsification properties (Kato and Nakai 1980, Voutsinas et al

1983, Kato et al 1983, 1985, 1986a, 1986b, 1989, 1990). Proteins with high

surface hydrophobicities and high solubilities have good emulsifying properties

(Kato and Nakai 1980, Halling 1981, Voutsinas et al 1983, Kato et at 1983). A

significant correlation (P < 0.01) was obtained between emulsifying activities

and the hydrophobicities of proteins (Kato and Nakai 1980). The dependence

of emulsifying properties on surface hydrophobicity, compared with the

dependence

of foaming properties on overall hydrophobicity, has been interpreted by Nakai

(1983) as implying that the protein was more unfolded at the air-water interface.

This was related to the fact that tension at the air/water interface (73 dyn/cm)

was far greater than that at the oil/water interface (13-19 dyn/cm). Kato et al

(1986b) observed an increase in surface hydrophobicity and emulsification

activity upon heat denaturation of ovalbumin and lysozyme under conditions

that did not reduce solubility. As with foaming properties, flexibility of protein

structure is also an important factor governing emulsification properties (Kato et

al 1985, Kato et al 1986a, b). lntramolecular cross-linking of serum albumin and

lysozyme lowered their molecular flexibilities and, therefore, foaming and

emulsification properties decreased (Kato et al 1986a). However, the decrease in

molecular flexibility had a more significant effect on the foaming properties.

Kato et al (1990) related enthalpy of denaturation (determined by DSC) to

foaming and emulsifying properties of heated egg white proteins in the dry state.

Good linear correlations were observed between the decrease in enthalpy and

increased foaming and emulsification properties of these proteins so long as

solubility was not affected.

Emulsification properties of proteins were studied by Hill and Hall

(1987). Bovine blood plasma and serum had higher emulsification capacities

than egg, whey, and soy isolate proteins. Emulsions prepared with blood

plasma proteins were more stable than those prepared with egg. Data from

Tybor et al (1973) indicate that the emulsification capacity of plasma protein

was greatest at pH 9.4, and a maximum response to protein concentration

occurred in the vicinity of 1 g of protein/100 mL. BSA is a good emulsifier

because of its molecular size, charge, surface hydrophobicity, disulfide bonds,

and ability to unfold to a limited extent, re- orient at the interface and undergo

interactions between the protein loops (Morrisey et al 1991).

The effects of ionic strength (0-1.5 NaCl) and pH on the EA of BSA were

investigated by Waniska et al (1981). The EA of BSA was increased at

intermediate ionic strengths (0.1-0.6 N) due to neutralization of surface

charges, reduced electrostatic repulsion, increased rate of protein adsorption,

and greater protein-protein interactions. The EA of BSA increased

progressively with increasing pH from 4 to 9, indicating that as net charge

increased, the ability to form a film was enhanced. The EA of BSA

decreased below pH 4 and above pH

9. Below pH 4 and above pH 9, BSA undergoes conformational transitions

in its tertiary structure which impairs formation of a stable interfacial film

required for emulsion formation.

The importance of native structure and molecular flexibility to the

emulsifying properties of BSA was indicated by Waniska et al (1981).

Reduction of the disulfide bonds of BSA resulted in a more expanded

conformation and a decrease in EA in the pH range 4-10 compared with that of

native BSA, suggesting that native BSA, which has more tertiary structure,

forms a stronger, more cohesive interfacial film than reduced protein. Complete

disruption of the secondary and tertiary structures of BSA by urea (8M)

eliminated emulsifying activity except for slight activity at alkaline pH values.

These studies reflect the importance of the native tertiary and secondary

structures of proteins to the formation of a stable interfacial film which is

required for emulsion formation. Succinylation of BSA markedly improved EA

in the pH range 5-10 compared with that of native BSA.

This may reflect increased molecular flexibility, which facilitates diffusion to the

interface and rearrangement within the interfacial film.

Saito et at (1988) fractionated plasma into albumin-rich, y-globulin-rich

and transferrin-rich fractions. y-GIobulin-rich fraction exhibited the highest

emulsification activity among the fractions, followed by transferrin and serum

albumin.
FUNCTIONALITY OF EGG PROTEIN IN CAKE
BAKING

A cake batter can be considered as a fat-in-water emulsion system and the

baked cake as a heat set foam, in which the egg white proteins play an important

functional role. Cake making can be divided into three main stages (Shepherd

and Yoel 1976): 1) batter preparation 2) baking stage and 3) structure

development.

BATTER PREPARATION

Batter preparation involves mixing ingredients and incorporating air

cells and nucleii into the batter. All the air cells and nuclei which ultimately

create the cake texture are incorporated in this stage, no new cells can be

created by chemical leavening during baking (Carlin 1944). Cake volume is

closely correlated with the amount of air in the batter (Dunn and White 1939,

Ellinger and Speck 1968).

Cakes can be divided into three types depending on the air incorporation into the

batter (Hoseney 1986). The first type utilizes multistage mixing. In multistage
mixing, air is incorporated into the fat phase. This type of mixing produces a

finer texture (due to the large number of air cells incorporated) and more

stable batter because air is in the fat where it has limited mobility. The second

type is a single stage mixing that is applied to box mixes. In this type of

mixing, liquids are added to the mix, and the batter is mixed. Since the mix

contains surfactants that lower the interfacial tension, air is incorporated

directly into the aqueous phase. In the third type of cake, air is directly

incorporated into the aqueous phase by mechanical means using a high-speed

mixing machine.

Single-stage mixing produces very delicate cakes and is not suitable for

commercial cakes.

Egg proteins play a role in stabilizating the emulsion system in cake

batter. Cake emulsion was related to general theories of emulsions by Shepherd

and Yoell (1976), and the possible stabilizing roles of egg in cake batter

systems were identified: the lowering of interfacial tension at water/fat surfaces

by an emulsifier will ease the formation of an emulsion by aiding the

breakdown of larger fat particles to finer-sized particles. The rheological nature

of the interfacial film formed around oil globules will affect emulsion stability.

The surface charge of the fat droplets may be important. Approach of fat

droplets to one another can be resisted by the mutual repulsion of their

electrical double layers, thus, preventing

coalescence. The viscosity of the continuous aqueous phase to which the

egg proteins contribute can also effect emulsion stability.

BAKING STAGE

During the baking stage, cake batter undergoes a number of changes:

when batter temperature reaches to 37-40°C, the fat in the batter melts and air

bubbles are released from the fat phase to the aqueous phase where they are

stabilized by egg protein molecules at the air bubble-water interface (Shepherd

and Yoel 1976). Shepherd and Yoell (1976) reported that when a simple

aerated fat and water system was heated air bubbles coalesced within the fat

phase. Any water-in-oil emulsion portions of the batter in this stage invert to

oil-in-water emulsion. Cake batters undergo bulk flow, up the sides and down

the center as temperature rises. Batter viscosity decreases as batter temperature

increases from ambient to 60°C (Mizukoshi, 1983; Shelke et al 1990). Egg

white significantly increases the batter viscosity both at ambient temperature

and at minimum viscosity during heating (Shelke et al 1990). Air bubbles

incorporated in the batter preparation stage expands due to movement of water

vapor and carbon dioxide (from baking

powder) into the air cells. Diffusion of gas from small bubbles to large bubbles

begins at 49-56oC and ends at 87-98oC (Bell et at 1975).

STRUCTURE DEVELOPMENT

In the final stage, cake structure develops due to coagulation of egg

protein and partial gelatinization of starch. Cake setting starts between 60-70oC
and this initial viscosity increas.e is caused by protein denaturation (Shepherd

and Yoel 1976) and a rapid viscosity increase starts between 80-85°C due to

starch gelatinization (Shelke et al 1990). Viscosity increase in a heated batter

prevent coalescence, migration and loss of air cells before the batter sets.

Expansion of air bubbles becomes very rapid at 70-80°C (Bell et al 1975,

Shepherd and Yoel 1976). The presence of egg proteins in the membranes

around air bubbles provides elasticity which supports the rapid expansion

(Shepherd and Yoel 1976). All of the movements in the batter cease at 99-

100oC in high ratio cakes, and the structure becomes fixed.

Donovan (1977) used DSC to investigate the baking process as applied to the

manufacture of angel food cake. He found that sucrose used in the standard

angel food cake batter increased the denaturation temperatures of egg white

proteins

and gelatinization temperature of starch by about 13 and 30°C, respectively.

Gelatinization of starch and denaturation of the major portion of egg

white proteins occured near 95oC, at approximately the maximum temperature

attained by the cake when it reaches maximum volume in the oven.

B.AIMS AND OBJECTIVES
 To find out the importance of egg protein in baking and confectionary
 To find out the impact of egg protein in bakery and confectionary
 Use of plant based protein instead of egg protein for the vegan market
 Use of bovine blood plasma
 Functional properties of egg protein and blood plasma protein in cake
making
 Processing blood plasma for food applications
C.RESEARCH METHODOLOGY
The methodology is based on data from the well founded sources with personal
observation. Secondary data is collected from journals ,books and articles. To
examine the role of egg protein in baking and its effects on confectionary ,accurate
search has been done by online sources and social websites.

:-DATA COLLECTION AND ANALYSIS

Primary analysis
 Eggs provide structure to baked goods because of the aggregation (also known as
thickening or gelling) of the protein. Think of the proteins as tightly wound springs.
As the eggs are cooked the protein unwinds and then reconnects with other proteins
to give structure to baked goods and custards.
Secondary data
1. The collection of the data from Websites, Articles, Research papers published
in various conference
The data was collected from various published and unpublished records human
nutrition and food protein

Statistical Analysis

The data were analyzed with Statistical Analysis System (SAS 1990).

When the F test was significant at the 0.05 or 0.01 level, means were compared by

the Least Significant Difference test. Multiple linear regression analyses were run

by using the stepwise procedure with forward, backward, and maxR options

between cake volume and the functional properties of proteins (Raeker and

Johnson 1994a).

RESULT AND DISCUSSIONS

EGG WHITE AND BLOOD PLASMA CAKES

When frozen blood plasma is allowed to thaw at SOC, fibrinogen stays in a

solid phase and can be separated by centrifugation (Ware et al 1947). This

fibrinogen-free plasma is called serum. Therefore, in the present work we term the

centrifuged plasma as serum and after spray and freeze drying, as spray- and

freeze-dried serum to differentiate them from blood plasma samples.

Volume and crowning profile (symmetry index) of the cakes prepared with

egg white, blood plasma, serum, and their fraction proteins are given in Table l.

Spray- and freeze-dried egg whites gave cakes with similar volumes and crowning
profiles. Cakes made with egg whites had slightly higher volumes than cakes made

with freeze- and commercial spray-dried blood plasma. However, cakes made with

egg whites produced significantly more crowning than those produced with blood

plasma samples (Fig. 1). Freeze-dried blood plasma produced cake with

properties similar to those of commercial spray-dried blood plasma. Removal of

fibrinogen from blood plasma increased cake volume and the crowning profile of

cakes; values were similar to those made with egg white (Table I, Fig. 2).

In general, blood plasma cakes had coarser and darker crumb structures than

those of egg white cakes. Freeze-dried blood plasma gave the coarsest crumb

structure. Commercial spray-dried blood plasma produced denser crumb structure

than serum samples, which had loose, fragile, and crumbly texture.

Cakes made with spray-dried egg white had smoother texture than cakes made

with freeze-dried egg white.

Cakes Prepared with Egg White Protein Fractions

Significant differences were observed in the volumes of the cakes when

different protein fractions were used (Table I, Fig. 3). In agreement with Johnson

and Zabik (1981), egg white globulins produced cakes with the largest volumes

followed by ovalbumin. In comparison with whole egg white, ovalbumin produced

similar cake properties, whereas egg white globulins produced significantly higher

volume and more crowned profile. Previously, Johnson and Zabik (1981) reported

that angel food cakes made with lysozyme and conalbumin were smaller in volume

because of less air inclusion and instabilities of the foams. However, in our study,

we attributed the small cake volumes of conalbumin and lysozyme to their lower
denaturation temperatures (Raeker and Johnson 1994a). Early denaturation of these

proteins at the bubble surface probably decreased film elasticity and

prevented cake expansion during baking.

Ovomucoid produced cakes with very small volume, even less than cakes prepared

without any protein. Cakes fell in the middle, which resulted in negative values for

profile crown. Ovomucoid cakes expanded normally during baking, but then

collapsed in the last stage of baking. This shows that ovomucoid did not coagulate

during baking in the oven. Lack of heat coagulation of the protein film around the

air cells at maximum expansion was likely the reason for small cake volumes.

Ovomucoid has been reported to remain soluble in dilute solutions when its

biological activity is completely destroyed by heat (Lineweaver and Murray 1947).

A 20% solution of ovomucoid was found to gel between pH 8 to 10 if placed in a

boiling water bath for 5 to 15 min. Because the pH of the cake batter is around 7,

our results show that ovomucoid remains soluble during baking, and therefore, by

itself, could not support cake structure. However, in egg white, ovomucoid,

because of its resistance to heat coagulation during baking, may increase flexibility

and viscoelasticity of the films around the gas bubbles and contribute to the

stability of egg white foam during baking.

Foaming properties of the proteins played significant roles in determining the

texture of the finished cakes. From observations, cakes prepared with lysozyme had

very dense crumb structures followed by conalbumin. The previous study of Raeker

and Johnson (1994a) showed that lysozyme did not produce foam.

Conalbumin and ovomucoid had low foaming capacities and stabilities. Ovomucoid

cakes had very coarse, rough crumb cell structure. Ovalbumin and globulins
produced similar foaming capacities; however, egg white globulin foam exhibited

very good stability, whereas ovalbumin foam was unstable. Consequently, ovalbumin

cakes had somewhat nonuniform cell structure with bigger gas cells, whereas

globulins produced cakes with good texture.

Cakes Prepared with Blood Plasma Protein Fractions

Fibrinogen, the most heat-sensitive protein in plasma (Raeker and Johnson

1984a), produced very small cake volume and flat crowning profile (Table I, Fig.

3). The early denaturation of the protein films surrounding the air cells prevented

them from expanding as the temperature increased during baking.

Albumin, the major protein in blood plasma, produced cakes with slightly

less volume than did whole blood plasma, whereas globulin fractions of plasma

producdd larger cake volumes with more crowned profiles than did whole blood

plasma. Among the globulins, Cohn fraction IV-1 (primarily a-globulins)

produced the largest volume followed by y-globulins and Cohn fraction III

(mixture of §- and y-globulins). In previous research, y-globulins were the most

heat stable proteins, followed by Cohn fraction III (Raeker and Johnson 1994a).

However, a-globulins are a group of 20 glycoproteins, and the amount of

carbohydrate varies from

protein to protein. For example o1- acid glycoproteins contain 42% carbohydrate,

and such high carbohydrate content may increase resistance of the protein to heat

denaturation and, in turn, increase the elasticity of the film around gas bubbles. a-

Globulins (Cohn fraction IV-1) also had very good foaming capacity and stability.

Batter prepared with Cohn fraction IV-1 had the lowest specific gravity among all
proteins showing that more air was entrapped during mixing. Since volume reflects

the amount of air incorporated during mixing and CO2 expansion during baking, it

is not very surprising that this protein produced a large volume cake despite having

a relatively low denaturation temperature of some of the other proteins in the

fraction.

Albumin produced almost the same crumb structure as did whole blood

plasma but the crumb was much less crumbly and denser. In general, cakes prepared

with blood plasma globulins were crumbly and had crumb structures with open cells.

y-Globulins produced better crumb structure than did albumen, Cohn fraction III,

and Cohn fraction IV-1. Cohn fraction IV-1 cakes had the coarsest the most

crumbly, and the most irregular textures. This was an unexpected result because this

protein had very good foaming capacity and stability. Fibrinogen cakes had very

elastic and smooth texture. No blood plasma protein fractions produced cake texture

as fine as did egg white globulins.

Albumin- and IgG-Rich Spray-Dried Plasma Fractions

Albumin- and IgG-rich spray-dried blood plasma fractions were better

emulsifiers than spray-dried plasma (Table II). The IgG-rich fraction emulsified

more oil than did the albumin-rich fraction. Foaming capacities of the lgG-rich

fraction were less than those of the albumin-rich fraction and the whole blood

plasma samples (Table II). Albumin- and lgG-rich plasma fractions had very good

foam stabilities. They maintained more than 85% of their original foam even after

30 min; whole blood plasma was unable to maintain more than 40% of its original

volume.
 The DSC thermograms show that these spray-dried fractions are not pure, and there
are at least two proteins in each fraction (Fig. 4). IgG-rich plasma fraction exhibited
a shoulder around 70°C and a peak at 78.2oC. As shown in Fig.
4, the albumen-rich fraction exhibited one major peak at 71.1oC and one minor
peak at 78.8oC. These denaturation peak temperatures were lower than those
obtained by using lyophilized pure albumin and y-globulins (Raeker and Johnson
1994a).

The albumin-rich spray-dried fraction produced significantly less cake

volume than did freeze-dried albumin and blood plasma (Table II, Fig. 2). Textures

of the cakes made with albumin-rich protein were denser and crumblier than blood

plasma cakes. The lgG-rich spray-dried fraction produced volume and texture

similar to the freeze-dried y-globulin, and cakes made with this protein had finer

crumb structure than cakes made with whole blood plasma.

Relationships Between Cake Volume and Protein Functionality

From the previous study (Raeker and Johnson 1994a), the proteins that gave

only one denaturation peak were chosen to determine the relationship between cake

volume and protein functionality. These proteins were bovine serum albumin, y-

globulin, Cohn fraction III, conalbumin, lysozyme, and ovalbumin.

Although fibrinogen exhibited one very low major and one very high minor
denaturation peak, we assumed that the lower denaturation temperature would
govern the cake properties. Therefore, we also included this protein in this part of
the study. Multiple linear regression equations were generated relating cake
volumes to the denaturation peak temperature, foaming properties (capacity and
stability), and emulsification activity of proteins (Tables III and IV).

There was a highly significant correlation coefficient between cake volume

and denaturation peak temperatures of proteins (r = 0.944, P = 0.001). The MaxR

procedure used in the analysis begins by finding the one-variable model that
produces the highest R2. Then another variable that yields the greatest increase in

R2 is found, and so on. This analysis showed that the protein denaturation peak

temperature produced the highest R2, the square of the correlation between the

actual volumes and the predicted volumes by the model, of 0.891. When

foaming capacity was entered into the model (Table III), R2 was improved by only

2% to 0.916 and contribution to the model from foaming capacity was not

significant (P = 0.33). When

emulsification activity was entered into the model, R2 did not improve, and

emulsification activity in the model was not significant (P = 0.95).

When foam stability instead of capacity was used in the multiple regression

analysis (Table IV), the contribution from foam stability to the model was also not

significant (P = 0.64). These results suggest that the denaturation temperature of

the protein is the only important functional property that determines the volume of

the finished cake.

TABLE l
@U8IItIb8 Of C&k69 Made with Egg White, Plasma, and Their ProtelnFractlons a
Protein Batter Cake Cake
Volume Profile
Spray-dried egg white 0.757 + 0.011 49.0 + 0.5 9.3 + 0.4
(commercial)
Freeze-drled egg white 0.780 + 0.008 48.4 + 0.6 9.0 + 0.4
Spray-dried blood plasma 0.752 + 0.012 47.8 + 0.4 6.8 + 0.5
(commercial)
Freeze-dried blood 0.761 + 0.006 47.7 + 0.5 7.2 + 0.3
plasma
(no centrifugation)
Spray-dried serum 0.757 0.009 49.8 + 0.8 8.9 + 0.8
(laboratory)
Freeze-dried serum 0.750 + 0.012 48.7 + 1.4 8.9 + 0.8
(after centrifugation)
Eqq white fractions
Ovalbumin 0.793 + 0.016 49.4 + 0.6 9.4 + 0.6
Globulins 0.774 0.013 51.0 + 0.7 10.5 + 1.1
Conalbumin 0.798 + 0.029 45.6 + 0.5 8.3 + 0.5
Lysozyme 0.786 0.021 45.5 + 0.5 7.7 + 1.3
Ovomucoid 0.778 1 0.014 38.6 + 0.6 -1.8 + 0.3
Blood plasma fractions
Albumin 0.781 + 0.013 46.9 0.5 8.0 + 0.3
y-Globulin 0.788 + 0.018 49.5 + 0.7 9.0 + 0.3
Cohn fraction III 0.762 + 0.007 48.5 + 1.0 8.7 0.4
Cohn fraction IV-1 0.741 + 0.002 49.9 + 0.8 10.4 + 1.1
Fibrinogen 0.929 + 0.024 42.2 1.1 3.2 + 1.1
LS o.as 0.025 1.2 1.2
d
Values are the means of three replicates (means 1 SD).
Fig. 1. Cakes prepared with A, egg white; B, blood plasma; C, ovalbumin; and D,
serum albumin.
 CONCLUSION
Various proteins used in this study demonstrated that the temperature at which a
protein denatures during baking is the determining factor in the final shape and
volume of cakes. The higher the denaturation temperature of a protein, the 116
larger the cake volume and the more crowned profile. This high correlation
between protein denaturation temperature and volume indicates that protein
denaturation temperature determined by DSC is a reliable predictor of cake
volume.
Since y-globulin had the highest denaturation temperature and produced
cakes with larger volumes and better texture than did whole blood plasma, the
use of blood plasma as an egg white substitute in cakes can be improved by
fractionating it into its y-globulin- or y-globulin-rich fractions.
Another solution is to separate fibrinogen from blood plasma because it
was responsible for low cake volumes and flat profiles of blood plasma cakes.
This would be a more practical solution because separation of this component
from blood plasma by centrifugation will be low in cost. However, additional
research is necessary to investigate texture and sensory properties of cakes
prepared with fibrinogen-free plasma (serum) because crumb texture of cakes
prepared with serum were fragile.
In general, spray-dried proteins produced a better crumb texture than
did their freeze-dried forms. This was attributed to the better foam stability of
spraydried samples as was shown in the previous study of Raeker and Johnson
(1984a).
BIBLIOGRAPHY
BAKERY AND CONFECTIONARY FDNT 315 3 (1+2)

1. Kent, N.L. Source for Base Recipes: The Williams-Sonoma Collections,

The French Culinary Institute Education Material, Baking with Julia,
Bernard Clayton's Book of Breads, Misc. Food Magazines, Food Sites:
Aarushi Jain

2. www.aarushijain.com/baking_ingredients.html

3. Sun PD, Foster CE, BOYINGRON JC (2004) Overview of protein

structural and functional folds . CURR PROTOC Protein Sci Chapter
17:Unit 17.1

Kang TS, KINI RM (2009) Structural determinants of protein folding. Cell

Mol Life Sci 66:2341–2361
ASSOCIATION OF OFFICIAL ANALYTICAL CHEMISTS. 1984. Official Methods of
Analysis, 14th ed. Association of Official Analytical Chemists Inc.; Arlington, VA.
AOKI, K., SATO, K., NAGAOKA, S., KAMADA, M., and HIRAMATSU, K. 1973. Heat
denaturation of bovine serum albumin in alkaline pH region. Biochim. Biophys.
Acta. 328:323.
BROOKS, J., and RATCLIFF, P. W. 1959. Dried bovine plasma. I.-Storage of
spray-dried plasma and the freeze-concentration of liquid plasma. J. Sci. Food
Agric. 10:486.
GLAZER, A. N., MACKENZIE, H. A., WAKE, R. G. 1963. The denaturation of
proteins II. Ultraviolet absorption spectra of bovine serum albumin and
ovalbumin in urea and in acid solution. Biochim. Biophys. Acta. 69:240.
JOHNSON, L. A., HAVEL, E. F., and HOSENEY, R. C. 1979. Bovine plasma
as a replacement for egg in cakes. Cereal Chem. 56:339.
 JOHNSON, T. M., and ZABIK, M. E. 1981. Egg albumen proteins interactions
in an angel food cake system. J. Food Sci. 46:1231.
KHAN, M. N., ROONEY, L. W., and DILL, C. W. 1979. Baking properties of
plasma protein isolate. J. Food Sci. 44:274.
LEE, C. C., JOHNSON, L. A., LOVE, J. A., and JOHNSON, S. 1991. Effects
of processing and usage level on performance of bovine plasma as an egg white
substitute in cakes. Cereal Chem. 68:100.
LINEWEAVER, H., and MURRAY, C. W. 1947. Identification of the trypsin
inhibitor of egg white with ovomucoid. J. Biol. Chem. 171:565.
GLAZER, A. N., and MCKENZIE, H. A. 1963. The denaturation of proteins
IV. Conalbumin and iron(lll)-conalbumin in urea solution. Biochim. Biophys.
Acta. 71:109.
GORNALL, A. G., BARDAWILL, C. S., and DAVID, M. M. 1949.
Determination of serum proteins by means of biuret reaction. J. Biol. Chem.
177:751.
MACDONNELL, L. R., FEENEY, R. E., HANSON, H. L, CAMPBELL, A.,
and SUGIHARA, T. F. 1955. The functional properties of the egg white
proteins. Food Technol. 9:49.
RAEKER, M. O., and JOHNSON, L. A. 1994a. Functional properties of bovine
blood plasma and egg white proteins. J. Food Sci. (manuscript submitted),
presented at the 53rd Annual Meeting of the Institute of Food Technologists,
Chicago, IL, July 10-14, 1993.
RAEKER, M. O., and JOHNSON, L. A. 1994b. A micro method for cake-
baking. Cereal Chem. (manuscript submitted), presented at the 78th Annual
Meeting of the American Association of Cereal Chemists, Miami Beach, FL,
October 3-7, 1993.
RUEGG, M., MOOR, U., and BLANC, B. 1977. A calorimetric study of the
thermal denaturation of whey proteins in simulated milk ultrafiltrate. J. Dairy
Res. 44:509.
SAS. 1990. SAS User's Guide: Statistics. SAS Institute, Inc., Cary, NC.
SOPHIANOPOULOS, A. J., RHODES, C. K., HOLCOMB, D. N., and VAN
HOLDE, K. E. 1962. Physical studies of lysozyme I. Characterization. J. Biol.
Chem. 237:1107.
 TYBOR, P. T., DILL, C. W., and LANDMANN, W. A. 1975. Functional
properties of proteins isolated from bovine blood by a continuous pilot process.
J. Food Sci. 40:155. WARE, A. G., GUEST, M. M., and SEEGERS, W.H.1947.
Fibrinogen: with special reference to its preparation and certain properties.