Emulsifi cation 155heating. Casein can impart a pale color and
soft texture to meat products. In intensively
heated products, this disadvantage is out-
weighed by the good binding properties, and
prevention of jelly and fat separation (Heinz
2007 ). Barbut (2006) compared the effects of
adding dry caseinate, whole milk, skim milk,
and regular and modifi ed whey protein
powders in emulsifi ed chicken meat batters.
Caseinate and modifi ed whey contributed
more to enhancing the textural properties of
the meat batters compared with the other
dairy proteins. Overall, the most cost - effec-
tive ingredient appeared to be the modifi ed
whey, which also provided the best moisture
retention.
Blood plasma is rich in proteins (8% – 9%)
and these proteins have a higher water - bind-
ing capacity than meat proteins. Moreover,
the pH of blood plasma is slightly alkaline
(7.5 – 7.8), which is also benefi cial to the
water - binding capacity. Flakes of plasma ice
are particularly suitable for raw - cooked meat
products where water or ice has to be added
(Heinz 2007 ).Polysaccharides
Polysaccharides are polymers of monosac-
charides. They are mainly used for their
thickening and gelifying properties due to
their high molecular weights and their
extended structure. Indeed, large highly
extended linear biopolymers increase the
viscosity more effectively than small compact
branched biopolymers. Most polysaccharides
are predominantly hydrophilic and are
therefore not particularly surface active,
except a small number of polysaccharides
(gum Arabic) or some modifi ed starches
(McClements 1999 ). Polysaccharides
increase water binding and fat binding, thus
improving products ’ juiciness and texture.
Plant products rich in polysaccharides are
used as fi llers for cost reduction and volume
addition. Previous studies have reported that
emulsion stability was increased due to theprotein has a positive impact on blood
cholesterol content, and whey proteins
contain bioactive compounds that may have
a positive effect on cardiovascular disease)
(Jimenez - Colmenero et al. 2006 ). Their
functional properties are determined by
their molecular weight, conformation, fl exi-
bility, polarity, and interactions (McClements
1999 ). Three typical confi gurations were
defi ned for proteins in aqueous solution:
globular, rod - like, and random - coil.
Membranes formed by globular proteins tend
to be more resistant to rupture than those
formed from random - coil proteins. In prac-
tice, many biopolymers have some regions
that are random coil, rod - like, or globular,
and they can change from one conformation
to another if their environment is altered
(McClements 1999 ).
Globular proteins form relatively thin but
dense interfacial layers that have high visco-
elasticities. When globular proteins unfold,
they expose amino acids capable of forming
disulfi de bonds with their neighbors and thus
an interfacial membrane that is partly stabi-
lized by covalent bonds. This occurs when
emulsion ages or when proteins are heated
(i.e., when β - Lactoglobulin is heated to
70 ° C). Examples of globular proteins used
in comminuted meat products are plasma
or lactoserum proteins ( α - lactalbumin, β -
Lactoglobulin, lysozyme), which mainly
have a stabilizing role when they form a geli-
fi ed network during heat treatment (Delaitre
1988 ).
Native and modifi ed dairy proteins are
known for their stabilizing role (Barbut
2006 ). Different fractions can be extracted.
They have various protein compositions and
thus different functional properties. Caseins
are amphiphilic and unfolding molecules that
mainly play a role in emulsifying and viscos-
ity. They rapidly adsorb and stabilize a newly
formed oil/water interface. Because the
caseins exist in open structures, they are not
as sensitive to structural alterations; for
example, the caseins are very stable to