Milk Proteins

Dr.A.P.Gandhi
.
Milk proteins have excellent nutritional and functional properties. Their solubility in
water and ability to act as emulsifier makes them a universal ingredient in all the
nutraceutical/pharmaceutical/industrial applications including making edible films and
coatings.
Protein characteristics
Total milk proteins
Milk contains on an average 3-4% protein. The two major types are casein and whey
proteins. Non fat dry milk (NFDM) has become increasingly important in the dairy
industry. It is composed of approximately 52% lactose, 36% protein (casein plus whey
proteins) and 8% minerals. Presently it is used in instant breakfast beverages, baked
products, confectionery, frozen deserts, cheeses and comminuted meat products.

Caseins:
Casein represents approximately 80% of the total proteins. It is mainly the
phosphoprotein with pI of 4.6 at 20 oC. It contains four principal
components namely alpha s1, alpha s2, and beta and k caseins. The
primary and secondary structures of these proteins affect their functional
properties. Casein contains low levels of cysteine with the exception of k
caseins. The alpha s1 and alpha s2 casein have even distribution of
hydrophilic residues. Their approximate molecular weight is23500 and pI
is 5.1. They represent 48% of the total casein fraction and more
phosphorylated. These caseins also readily bind with calcium. Beta casein
represents 30-35% of the total casein with an mw of 24000 and pI 5.3. It is
highly hydrophobic. The amphiphilic structure of beta casein allows it to
act effectively as a surfactant. It is not calcium sensitive. At neutral pH
and high temperature it associates in to thread like polymers. K casein is
approximately 15% of the total casein. Its mw is 19000 and pI is in
between 3.7 and 4.2. It has the ability to polymerize via disulfide bonds.
The amphiphilic nature of k casein results in increased protein surface
activity. In the presence of calcium, k casein associates with alpha s1 and
beta casein to form thermodynamically stable micelles. About 80-90% of
the caseins in milk form colloidally disperse micelles with diameters
between 10 and 250 nm. Caseinates are produced by treating acid
precipitated caseins with alkali (commonly sodium and calcium
hydroxides) at 80-90oC and pH 6.2-6.7. The solubilized caseinates are then
spray dried. Caseinates are soluble above pH 5.5. Sodium or potassium
caseinates are more soluble and often possess better functional properties
than calcium and magnesium derivatives. Sodium caseinate is very heat
stable where as calcium caseinate is heat stable above 10% at 120oC for
15 minutes at pH greater than neutral. Presently caseinates are used in a
variety of foods as well as in paper coatings, glues and plastics.
Whey proteins:
It represents about 20% of the total milk proteins. They are soluble at pH
4.6. Whey proteins contain five protein types. Namely alpha lactalbumin,
beta lactoglobulin, BSA, immunoglobulin and proteose peptones. Liquid
whey is by product of cheese manufacture and the annual production is
rising. Beta lactoglobulin is the major protein (62%). In whey fraction. It
has mw of 18362. It is globular with hydrophobic and SH groups located
in the interior. Oxidation of free SH and thiol disulfides interchange
reactions can be induced by heating whey protein solutions leading to
polymerization of whey protein molecules. Alpha lactalbumin represents
25% of the whey proteins. It is globular with mw of 14000 and has for –s-
s-bonds. It is actively binds with calcium which may stabilize it against
denaturation. BSA is a large globular protein with mw of 66000. The
immunoglobulin and prteose peptones represent the reminder of the whey
proteins. They are thermally unstable. They are amphiphilic and affect the
protein functionality. Whey proteins are currently used in the baked foods,
confectionery and infant food products as well as in animal feed.