CLASSES OF MILK
PROTEINS
FST- 507 DAIRY TECHNOLOGY 3(2+1)
SPRING 2021, BSC. (HONS.) 6TH SEMESTER
INSTRUCTOR: DR. SHEHLA SAMMI, DEPT. OF FOOD SCIENCE AND
TECHNOLOGY, THE UNIVERSITY OF HARIPUR.
INTRODUCTION
• Milk contains hundreds of types of protein, most of them in very
small amounts.
• The proteins can be classified in various ways according to their
chemical or physical properties and their biological functions.
• The old way of grouping milk proteins into casein, albumin and
globulin has given way to a more adequate classification system.
• Table 1 below shows an abridged list of milk proteins according to
a modern system. Minor protein groups have been excluded for the
sake of simplicity.
Conc. in milk g/kg % of total protein w/w
Casein
αs1-casein* 10.7 32
αs2-casein* 2.8 8.4
β-casein 8.6 26
κ-casein 3.1 9.3
γ-casein 0.8 2.4
Total Casein 26 78.3
Serum proteins
α-lactalbumin 1.2 3.7
β-lactoglobulin 3.2 9.8
Serum Albumin 0.4 1.2
Immunoglobulins 0.8 2.4
Miscellaneous (including Proteose-
Peptone) 0.8 2.4
Total Serum proteins 6.4 19
Miscellaneous (incl Membrane proteins) 0.9 2.7
WHEY PROTEIN
• Whey protein is a term often used as a synonym for milk-
serum proteins, but it should be reserved for the proteins in
whey from the cheese making process.
• In addition to milk-serum proteins, whey protein also contains
fragments of casein molecules.
• Some of the milk-serum proteins are also present in whey in
lower concentrations than in the original milk. This is due to
heat denaturation during pasteurization of the milk prior to
cheese-making.
• The three main groups of proteins in milk are distinguished
by their widely different behaviour and form of existence.
• The caseins are easily precipitated from milk in a variety of
ways, while the serum proteins usually remain in solution.
• The fat-globule membrane proteins adhere, as the name
implies, to the surface of the fat globules and are only
released by mechanical action, e.g. by churning cream into
butter.
CASEIN IN
MILK
• Casein is a mixture of several components (Table 2) and is the
dominant class of proteins in milk, constituting about four-fifths of
the milk proteins.
• There are four main subgroups of casein, as1-casein, as2-casein, κ-
casein and β-casein, which are all heterogeneous and consist of
several genetic variants.
• Genetic variants of a protein differ from each
Conc. in milk
other only by a few
% of total protein
amino acids. g/kg w/w
Casein
αs1-casein* 10,7 32
αs2-casein* 2,8 8,4
β-casein 8,6 26
κ-casein 3,1 9,3
γ-casein 0,8 2,4
Total Casein 26 78,3
CASEIN MICELLES
•
The caseins self-associate and form
large clusters called micelles. The
micelles are built up of hundreds and
thousands of individual casein
protein molecules and vary in size
from 50 to 500nm.
• Since the micelles are of colloidal
dimensions they are capable of
scattering light and the white colour
of skim milk is largely due to light
scattering by the casein micelles.
• Casein micelles have important consequences for the
properties of milk. They determine to a large extent the
physical stability of milk products during heating and storage,
are essential in cheese making and determine rheological
properties of fermented and concentrated dairy products.
• Casein micelles are fairly dense aggregates with small
regions of calcium phosphate, which links the micelles
together, giving the micelles an open, porous structure.
Removal of calcium phosphate (CCP – colloidal calcium
phosphate), e.g. by acidification or addition of EDTA or
citrates, leads to disintegration of the micelles. Disintegration
also occurs when pH becomes greater than 9.
• The internal structure of a casein micelle has been
under debate for a long time and is still not fully
understood.
• There are three main models proposed:
• the nanocluster model,
• the dual binding model and
• the sub-micelle model.
A) THE NANOCLUSTER MODEL OF CASEIN
MICELLES.
• tangled web of flexible
casein molecules
forming a gel-like
structure connected
through calcium
phosphate nanoclusters
B) THE DUAL BINDING MODEL
• balance of both
hydrophobic
interactions
between casein
molecules and
crosslinking with
colloidal calcium
phosphate holds
the micelle.
C) SUB-MICELLE
MODEL OF CASEIN
MICELLE
casein micelle is
built up of
smaller
micelles, sub-
micelles some
10-15nm in
diameter, which
are linked
together by
• The micelles are roughly spherical particles with an average
diameter of about 150 nm but with a large spread in size.
• The αs- and β-caseins are mainly concentrated in the middle of
the micelle, while κ-casein predominates on the surface.
• There is a “hairy layer” around the micelle, consisting mainly of
the C-terminal end of κ - casein that protrudes 5-10 nm from
the micelle surface.
• The protruding κ - casein chain is hydrophilic and negatively
charged and gives a major contribution to the steric stability of
the micelles. If the hairy layer is removed e.g. by ethanol
addition or rennet-induced hydrolysis, the colloidal stability of
the micelle is changed and the micelles aggregate or
precipitate.
• Further, it is generally accepted that there are “nanoclusters” of
calcium phosphate, which are roughly 3nm in diameter and contains
most of the phosphate and calcium in the micelle. The forces
holding the micelle together are hydrophobic interactions between
protein groups, cross-links between peptide chains by the
nanoclusters and ionic bonds.
• A casein micelle structure is not fixed, but dynamic. A casein micelle
and its surrounding keep exchanging components. It responds to
changes in the micellar environment, temperature, pH and pressure.
• If the hydrophilic protruding chain end of κ - casein on the surface of
micelles is split, e.g. by rennet, the micelles will lose their solubility and
start to aggregate and form casein curd. In an intact micelle there is a
surplus of negative charges, so they repel each other. Water molecules
held by the hydrophilic sites of κ - casein form an important part of this
balance. If the hydrophilic sites are removed, water will start to leave the
structure. This gives the attracting forces room to act. New bonds are
formed, one of the salt type, where calcium is active, and the second of
the hydrophobic type. These bonds will then enhance the expulsion of
water and the structure will finally collapse into a dense curd.
• The micelles are adversely affected by low temperature, at
which the β - casein chains start to dissociate and the CCP
leaves the micelle structure, where it existed in colloidal
form, and goes into solution. The explanation of this
phenomenon is that b - casein is the most hydrophobic
casein, and that the hydrophobic interactions are weakened
when the temperature is lowered.
• Micelles appear to disintegrate and the voluminosity of the casein
micelles increases. The loss of CCP causes a weaker attraction between
individual casein molecules. These changes make the milk less suitable
for cheese making, as they result in longer renneting time and a softer
curd.
• β - casein is then also more easily hydrolysed by various proteases in the
milk after leaving the micelle. Hydrolysis of β - casein to γ - casein and
proteose-peptones means lower yield at cheese production because the
proteose-peptone fractions are lost in the whey.
• The breakdown of β -casein may also result in formation of bitter
peptides, causing off-flavour problems in the dairy products.