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Casein and Caseinate: Methods of Manufacture

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DOI: 10.1016/B978-0-12-384947-2.00122-7

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Sarode A.R., Sawale P.D., Khedkar C.D., Kalyankar S.D. and Pawshe R.D. (2016) Casein and Caseinate:
Methods of Manufacture. In: Caballero, B., Finglas, P., and Toldrá, F. (eds.) The Encyclopedia of Food and
Health vol. 1, pp. 676-682. Oxford: Academic Press.

© 2016 Elsevier Ltd. All rights reserved.

 Author's personal copy
Casein and Caseinate: Methods of Manufacture
AR Sarode, College of Dairy Technology, Pusad, India
PD Sawale, Sardarkrushinagar Dantiwada Agricultural University, Sardarkrushinagar, India
CD Khedkar, College of Dairy Technology, Pusad, India
SD Kalyankar, Government College of Dairy Technology, Udgir, India
RD Pawshe, College of Food Science & Technology, Amravati, India
ã 2016 Elsevier Ltd. All rights reserved.
Introduction
Casein is the most important protein component in milk, both
quantitatively and nutritionally, accounting for about 80% of
milk’s total nitrogen. It was used in industries producing paper,
textiles, paint, leather, fiber, and other materials. Edible casein
and caseinates are also long established dairy byproducts with
uses in many foods. Casein is a very rich source of essential
amino acids, with the only possible exception of cysteine. It is a
phosphorylated and glycosilated complex synthesized by
mammary glands. It is constituted of three different polypep-
tide chains (as1, as2, and ß) held together by noncovalent
interactions. Casein fractions are organized in micellar aggre-
gates that also contain bivalent cations (calcium and smaller
amounts of magnesium), ranging 20–300 nm in diameter.
This structure allows highly stable dispersion of hydrophobic
fractions in a colloidal state by the action of hydrophilic
bonds.
The amount of casein in whole milk varies according to the
animal breed and stage of lactation. It is generally in the range
24–29 g l
1. Casein contains 0.7–0.9% phosphorus, cova-
lently bound to the protein by a serine ester linkage.
Consequently, casein is known as a phosphoprotein. All the
amino acids that are essential for humans are present in casein
in high proportions, with the possible exception of cysteine.
Thus, casein is considered to be a highly nutritious protein. It
exists in milk in complex groups of molecules called as
micelles. The micelles consist of casein molecules, calcium,
inorganic phosphate, and citrate ions, and they have a typical
molecular weight of several hundred million daltons.
In terms of physical chemistry, the casein micelles exist in
milk as a very stable colloidal dispersion. As a protein, casein is
made up of hundreds of individual amino acids, each of which
may have a positive or a negative charge, depending on the pH
of the milk system. At some pH value, all the positive charges
and all the negative charges on the casein remain in balance
(i.e., the net charge on the protein is zero); this pH value is
known as the isoelectric point (IEP), which is 4.6 for casein.
The IEP is the pH at which the protein is least soluble. Milk has
a pH value of about 6.6, at which the casein micelles have a net
negative charge and are quite stable. Casein consists of several
individual casein components (as1-, as2-, b-, and k-casein),
each having slightly different properties.
Casein is precipitated from skim milk by acidifying it to
produce acid casein, or the milk is treated with rennet to
produce rennet casein. The precipitated casein curd is sepa-
rated from the whey, washed, and dried. The water-soluble
derivatives of acid caseins, produced by reaction with alkalis,
are called caseinates. Edible casein is a long-established dairy
676 Encyclopedia of Food and Health
The Encyclopedia of Food and Health, (2016), vol. 1, pp. 676-682
byproduct used as an ingredient in many food products,
including dairy products. The general development of food
technologies and their applications has increased the produc-
tion of and demand for casein. Its manufacture differs from
that of nonedible casein (also called industrial casein) in that
casein for food is produced under sanitary conditions. Further,
during its manufacture, food-grade chemicals are used and
sufficiently heat-treated to make the casein safe for human
consumption. The intensive investigation into manufacturing
technologies over the years and the introduction of efficient
plant designs have immensely improved the technology for
edible casein production.
Production of Caseins: A Scenario
The world production of caseins and caseinates is hard to define
due to lack of a significant data. However, it could be
430 000–460 000 tons. The largest producers of caseins are New
Zealand (150 000 tons), Netherlands (85 000–10 000 tons),
and Germany (25 000–40 000 tons). The world market for
casein or caseinates used in the food industry fluctuates
between 200 000 and 2 500 000 tons. The United States is
the biggest importer of caseins. The demand for food-grade
casein in the US is about 25 000 tons per annum, and the
corresponding demand for caseinates is around 30 000 tons.
About 20% of this demand is for nutraceutical applications.
Casein is also utilized for the manufacture of imitation cheeses.
Japan is the second largest importer of casein.
The production of edible casein is only economically
feasible when the whey is efficiently and economically utilized.
This has been one of the main reasons why edible casein is not
produced on a large scale. Most of the requirements of this
byproduct, even for industrial uses, were met through import.
During 1999–2014, a few new large, automatic, and continu-
ous manufacturing plants have begun to produce edible casein,
lactose, and whey protein concentrates. The production of
caseinates has not picked up in many dairying countries,
including India, however, because of its high drying cost, low
bulk density, and high packaging, storage, and transportation
costs.
Casein Manufacturing Processes
Processes for the manufacture of edible casein from milk are
well known all over the world (Figure 1). The efficient separa-
tion of fat from milk is essential. For this, filtered and warmed
milk (40–45  C) should be separated in a hermetic cream
http://dx.doi.org/10.1016/B978-0-12-384947-2.00122-7
 Author's personal copy
Casein and Caseinate: Methods of Manufacture 677

Skim milk

Pasteurizationa

Rennet clot Isoelectric precipitation

Mineral acid Ion exchange Lactic acid

Heat

Separation of casein curd

Washing

Dewatering

Drying

Tempering

Grinding

Grading

Blending

Bagging
a
Figure 1 Manufacture of the various types of caseins. Milk for the manufacture of rennet casein for nonfood use is not pasteurized.

separator so that the fat in the skim milk is reduced to less than
0.05%. Achieving the microbiological standards for edible
casein also requires the pasteurization of either or both the
milk and the curd. Heat treatment tends to produce a higher
yield of casein. Some researchers hold that the heat treatment
of milk for casein manufacture causes slight insolubility and
other defects.
Separation
To extract the casein from milk, it is first separated by means of
centrifuges to produce cream and skim milk. Skim milk can
thus be considered to be the raw material from which casein
products are made.
Precipitation
solution, and at the IEP of casein (about pH 4.6), maximum
precipitation occurs. At this pH all the calcium is solubilized.
Not only is the calcium from the caseinate molecule removed,
but the calcium phosphate is also liberated in its soluble
form. This allows the plant to wash the soluble salts from
the curd in order to achieve low ash content in the final
product.
Ideally, all the casein in a sample of milk would be precip-
itated simply by adding enough acid to bring the pH value
to  4.6. However, the reaction between the acid and the
caseinate complex is not instantaneous, and the pH tends to
rise slowly with time. Therefore, ample time should be allowed
for achieving equilibrium conditions. When casein is precipi-
tated from skim milk by the direct addition of acid, the tem-
perature and pH of precipitation and the mechanical handling
of the curd during its formation are very important in deter-
mining the subsequent properties of the curd.

An important use of surplus skim milk is in the production of

casein. Casein exists in milk as a calcium caseinate–calcium-
phosphate complex. When an acid is added to the milk, this
complex is dissociated. As the pH of the milk is lowered, the
calcium is displaced from the casein molecules by hydronium
ions, H30þ, and the calcium phosphate associated with the
complex is converted into soluble Ca2þ ions and H2PO4

ions. At about 5.3 pH, the casein begins to precipitate out of
Enzymatic coagulation
In the case of the enzymatic coagulation of casein, the pH of
the milk does not change. Instead, the coagulation depends on
the addition of a specific enzyme, chymosin/rennin, which
cleaves a highly charged portion from the k-casein, called
glycomacropeptide. This action causes the remainder of the
k-casein (now called para-k-casein) to lose its considerable

The Encyclopedia of Food and Health, (2016), vol. 1, pp. 676-682

 Author's personal copy
678 Casein and Caseinate: Methods of Manufacture
power in stabilizing the micelles in milk, and the result is the
formation of a three-dimensional gel network or coagulum of
casein in the presence of calcium ions. This reaction is essential
for the manufacture of virtually all cheeses and in the produc-
tion of rennet casein.
Acid coagulation
Casein precipitated by acid usually includes the name of the
acid in its description, as with hydrochloric acid casein and
lactic acid casein. Any of the acid precipitation processes can be
used to produce edible casein. The choice of the method for
reducing the pH of skim milk to precipitate casein is governed
by the cost of acid. The lactic fermentation process is attractive
in terms of its cost effectiveness. For lactic acid casein, the
pasteurized skim milk is cooled to 22–26  C and inoculated
with a 0.5% starter of mixed lactic starters and incubated for
14–16 h, during which time the pH reduces to 4.6, producing a
coagulum. The coagulum is cooked to 50–55  C to create a
curd firm enough for subsequent processing. The acid and heat
help in the syneresis of whey.
The use of mineral acids has the advantage of completely
continuous operation with no holding time for coagulation.
Hydrochloric acid is a superior coagulating agent. When sulfuric
acid or hydrochloric acid is used to precipitate curd, it should be
diluted before being added to the skim milk; otherwise, the local
action of the acid may injure the curd, even though the agitation
is rapid. Within reasonable limits, the more dilute the acid the
better the quality of the casein produced.
Temperature of precipitation
The kind of curd formed is sensitive to heat. Curd precipitated at
temperatures below 35  C is very soft and fine, and conse-
quently, it is slow to settle and difficult to wash without loss.
Precipitated at temperatures between 35 and 38  C, the curd is
coarse, provided stirring is not too fast. Stirring is necessary to
distribute the acid uniformly, but rapid stirring at temperatures
below 38  C produces a curd so fine that it settles very slowly
during drainage and washing, and it may be lost to some extent
in the whey and washings. The curd can be made firm either
by heating to a temperature above 38  C or lowering the pH
to 4.1. Curd precipitated at about 43  C has a texture resembling
chewing gum, being stringy, lumpy, and coarse, containing prac-
tically no fine particles, and separating cleanly from the whey.
High-grade casein, which is low in ash and readily soluble,
is made by the grain-curd process in which the pH and tem-
perature are closely controlled. The best product is made by the
use of hydrochloric acid, but lactic and sulfuric acids may be
used successfully. The temperature of the skim milk should be
held close to 35  C for hydrochloric acid curd. The pH 4.1 is
adjusted by adding dilute acid slowly with continuous stirring.
It produces a granular curd that is easy to drain and wash.
Draining of Whey
After precipitation, curd gets settled. Whey should be removed
from contact with the curd as soon as possible. The longer the
curd remains in contact with the whey, the more difficult it is to
wash out acids, salts, whey protein, and lactose, as the freshly
broken curd tends to anneal itself, thereby enclosing these
constituents within a protein film.
The Encyclopedia of Food and Health, (2016), vol. 1, pp. 676-682
Washing of Casein Curd
The washing of casein curd is one of the most important steps
in casein manufacture as most quality improvement in casein
is achieved through efficient washing. Large portions of lac-
tose, minerals, and acids are trapped within the curd, which
prevents their ready removal during washing of the curd. It is
necessary to allow sufficient holding time during each washing
stage in order to permit the diffusion of these whey compo-
nents. The diffusion rate depends on the size and permeability
of the curd particles and the purity, amount, and rate of move-
ment of the wash water. Smaller size and better permeability of
the curd particles are important for efficient washing. Three
separate washes of casein curd are required with contact times
of 15–20 min each. As soon as the whey is removed the wash
water should be added in equal quantity to the whey that has
drained off. The curd should be well stirred in the wash water,
either by rakes or by mechanical agitators, but care should be
taken not to break the curd into fine particles. Firm and friable
curd particles are required to avoid creation of excessive fines.
Rubbery and plastic curds cannot be washed effectively. Effi-
cient washing can be achieved through the removal of as much
whey as possible at the whey off stage. The temperature and pH
of wash water are important factors affecting quality of casein.
Temperature of wash water
Casein curd acts like a sponge in the water, contracting to expel
water when heat is applied (termed as syneresis) and relaxing
when the water temperature is lowered. Heating leads to hard
and rubbery curd, while cold water softens it and causes the
curd to be fragile and readily broken. The temperature of the
first wash should be the same as the precipitation temperature
in order to produce good curd shrinkage. With lactic casein,
higher temperatures (70  C or above) are necessary at some
stage of washing to reduce the bacteria, which multiply during
the incubation of milk with starter. The temperature of the
final wash water should be adjusted to 32–40  C for better
expulsion of water during subsequent pressing.
pH of wash water
The pH of the water should be around 4.6 for the first two
washings to avoid the formation of a gelatinous layer over the
curd particles in excessively acid water, as well as the softening
and dispersion of the curd in alkaline waters. The gelatinous
layer, if formed over the curd particles, inhibits the drainage of
salts and lactose from the curd. Making the pH of the wash
water the same as that of casein helps maintain the equilib-
rium. Dilute sulfuric acid is preferred for this purpose because
casein is much less soluble in this acid than it is in hydrochloric
acid. The third wash should be given with neutral water.
Pressing of Casein Curd
The efficient pressing of washed casein curd is important for
minimizing the energy required for the removal of the remain-
ing water by drying. Inadequate pressing leads to the formation
of lumps of curd on subsequent grinding. It also produces a
hard, impervious surface that resists the escape of moisture from
the inside, a condition known as case hardening. The mechan-
ical removal of water is cheaper than thermal vaporization.
 Author's personal copy
The batch pressing operation is usually an overnight operation
(not less than 12–15 h) with 34 kg cm
2 pressure. The propor-
tion of water in washed curd and its ease of removal depend on
the type of curd made. The appropriate pH and a temperature of
41  C produce a firm, friable curd that drains and presses well.
The final moisture content is usually 55–60%.
Milling and Drying of Casein
Pressed curd is prone to microbial attack and, therefore, should
be shredded and dried as promptly as practicable. Pressing
produces particles of uniform size and surface for drying.
Uneven drying leads to large particles or lumps that dry on
the outside, forming a hard, impervious outer surface that
prevents the diffusion of the remaining moisture from the
interior of the particles.
The ground curd is spread on trays. It should be spread
evenly, and no more than 0.9–1.1 kg of curd should be placed
on a tray of 75  75 cm. The bottom tray on each truck should
have a finer mesh than the others, or it should be covered with
a cloth to catch fine particles that may sift through the other
trays. The proper control of the temperature and humidity of
the air coming in contact with the curd are essential for the
efficient drying of casein. The inlet air temperature of 52–57  C
is suitable for any type of curd. Once started, drying should not
be interrupted until the moisture content is about 8%. Properly
dried casein has the same fine, granular characteristics as the
properly ground curd from which it is made.
Tempering, Grinding, Sieving, and Bagging of Casein
Tempering: It is the holding of casein for a period of 24 h to allow
efficient cooling, hardening, and even distribution of moisture
throughout the batch. Casein shows variation in moisture con-
tent during a day’s run, as it comes from the drier. The most
efficient tempering consists of recirculating the dried casein by
pneumatic conveyers. It has the advantage that the air used for
the transport of the casein assists in cooling the curd.
Grinding: The casein must be cooled before grinding
because warm casein is plastic and causes ‘burn on’ of the
rollers. Grinding and sieving are necessary to produce the high-
est proportion of the product in the size range desired by the
buyer. The grinding is completed by roller mills, pin mills, or
hammer mills. For the production of 60- and 80-mesh casein,
pin mills are much more efficient than hammer mills.
Sieving: The grinding operation is followed by sieving into
various mesh sizes, and then bagging. Common mesh sizes are
30–40 mesh casein, 60-mesh casein, and 90-mesh casein.
Bagging: The casein is packed in sacks or bags of 100 or
200 lb capacity, as prescribed by the grade classification of the
casein. Burlap sacks lined with closely woven cloth or heavy
papers, or three-ply paper bags may be used for bagging of
caseins.
Continuous Casein Manufacture
Due to the advancement of technology and automation, con-
tinuous casein-manufacturing plants have replaced batch pro-
cesses for large-scale production. These plants reduced the
The Encyclopedia of Food and Health, (2016), vol. 1, pp. 676-682
Casein and Caseinate: Methods of Manufacture 679
manufacturing costs for improving the value of milk proteins,
related to that of dried milk, and also elevated the status of
casein for both industrial and food uses. These plants are also
highly labor-saving, because a large casein plant, with contin-
uous hydrochloric acid precipitation and a capacity of
14 000 l h
1, requires only one person to operate it. The sys-
tems are designed to accurately measure pumping rates in
order to ensure a constant flow of milk and acid, mixing acid
with skim milk at controlled temperatures of 25  C or lower.
This ensures equilibrium conditions before coagulation
begins, automatic regulation of steam injection to achieve the
coagulation temperature, and a holding tube capable of
obtaining complete coagulation and a well-settled curd, all of
which lead to less than 1% losses of casein in whey.
After precipitation, casein curd is concentrated by passage
over stationary, inclined and fine mesh screens, which remove
between 70% and 90% of the whey. Several dairy companies
have installed and are successfully operating roller presses and
lately decanters for removing the whey. Hydrocyclones may be
employed to recover fine particles from whey and wash water.
For continuous washing of casein curd, the most common
procedure now adopted is a counter flow which reduces both
the volume of water needed and the loss of casein fines; the
technique involves as many as five washing stages. These stor-
age tanks are of sufficient capacity to permit an average holding
time of 20–30 min. Continuous curd pressing is done in
mechanically driven roller presses, by belt, or by passing the
material through decanters, where water is sufficiently expelled
for subsequent economical drying.
There are a number of types of equipment for the drying of
casein. The most widely used in recent years is a vibratory type
of drier. The curd passes through a mill to reduce it to even-
sized particles, which then travel by means of a vibratory action
over trays of perforated stainless steel, transferring to succes-
sively lower trays. The heated air flows through the beds of
curd from the bottom to the top, thus encountering layers of
curd of increasing water content and providing improved effi-
ciency of heat utilization.
Method of Manufacture of Caseinates
The caseinate is prepared from freshly precipitated acid casein
curd or from dry acid casein by reaction with dilute alkali
solutions (Figure 2). Sodium caseinate is the most commonly
used form of casein, and it is used in wide range of processed
food products as a source of protein, and for their physico-
chemical, nutritional, and functional properties. Next to
sodium caseinate, calcium caseinate is common and finds its
use in both pharmaceutical preparations and as a food ingre-
dient. It functions as supplier of both calcium and protein. The
specifications for this product vary with its end use, but they
frequently include a limitation of calcium content to within
the range of 1.0–1.5%.
Manufacturing Process
The fresh acid casein curd is preferred over dried casein as a raw
material because the former yields caseinates with blander
 Author's personal copy
680 Casein and Caseinate: Methods of Manufacture
Starting materiala
Mixing with water
Wet milling
Mixing
Dissolving with agitation and heating
Dryingb
Blending
Bagging
Figure 2 Conventional method for the manufacture of caseinates.
a
Either fresh, acid casein curd, or dried casein; busually spray- or roller-
dried.
flavor than does the latter. Caseinates prepared from dry casein
will also incur the additional manufacturing costs associated
with the drying, dry processing, bagging, and storage of the
casein prior to its conversion to sodium caseinate. However, in
countries that import casein, buyers may still prefer to pur-
chase casein and produce their own sodium caseinate. Casein
should have a low calcium content (0.15% dry basis) in order
to produce a caseinate solution with a low viscosity, and a low
lactose content (0.2% dry basis), with the goal being sodium
caseinate with the best color, flavor, and nutritional value.
Control of the curd characteristics is also important to ensure
rapid dissolution.
Sodium Caseinate
The manufacture of sodium caseinate consists of the formation
of a casein suspension, solubilization of casein using sodium
hydroxide, and drying the sodium caseinate produced.
Casein Suspension and Solubilization
The main difficulties experienced in the conversion of acid
casein to sodium caseinate are as follows:
(a) The very high viscosity of sodium caseinate solution of
moderate concentration limit the solids content for spray
drying to 20%.
(b) The formation of a relatively impervious, jelly-like, viscous
coating on the surface of casein micelles impedes their
dissolution on the addition of alkali. To overcome the
former difficulty, it is essential that the pH and tempera-
ture are controlled during conversion, because these influ-
ence viscosity. The latter challenge can be overcome by
reducing the particle size by passing the casein and water
mixture through a colloid mill prior to the addition of
alkali.
The Encyclopedia of Food and Health, (2016), vol. 1, pp. 676-682
After the final casein wash, the curd is dewatered to about 45%
solids and then mixed with water (to 25–30% solids) prior to
entering the colloid mill. The temperature of the emerging
slurry, which has a pasty consistency, should be below 45  C,
because it has been observed that milled curd can
reagglomerate at higher temperatures.
Addition of Alkali and pH Control
The common alkali used in the production of sodium casein-
ate is sodium hydroxide in the form of 2.5 M solution. The
quantity of alkali required is generally 1.7–2.2% by weight of
the casein solids. Other alkalis such as sodium bicarbonate or
sodium phosphates may be used, but the amounts required
and their costs are both greater than those of sodium hydrox-
ide. Hence, they are used only for specific purposes, such as the
manufacture of citrated caseinate. The addition of the dilute
alkali, preferably by dosing into the recirculating line just prior
to the pump, must be carefully controlled with the aim of
reaching a final caseinate pH of 6.6–7.0.
Dissolving
The viscosity of sodium caseinate solutions can be expressed as
a logarithmic function of the total solid concentration. Each
dissolving vat, therefore, must be equipped with a powerful
agitator and a high speed recirculating pump. In addition to
concentration, temperature, and pH, the calcium content of
the curd, the type of alkali used, and seasonal and genetic
factors also affect the viscosity of the product. Once the alkali
has been added to the casein, it is important to raise the
temperature as quickly as possible to 60–70  C, in order to
reduce the viscosity. During the dissolving operation, the
incorporation of air should be kept to a minimum, because
caseinate solutions form very stable foams.
Drying
The homogeneous sodium caseinate solution is usually spray-
dried in a stream of hot air. In order to ensure efficient atom-
ization of the sodium caseinate solution, the solution must
have a constant viscosity as it is fed to the drier. It is common
practice to minimize the viscosity by preheating the solution to
a temperature of 90–95  C just prior to spray drying. Care
should be taken to minimize the time for which the caseinate
solution is at high temperature.
Other Caseinates
The manufacture of potassium and ammonium caseinates is
very similar to that of sodium caseinate, although, in the case
of ammonium caseinate, a lot of the ammonia is evaporated
from the solution during the drying process. A solution of
sodium caseinate, like those of potassium and ammonium
caseinates, has a straw-like color, and it is completely different
in appearance from milk. Solutions of calcium caseinate, on
the other hand, are very white and opaque (even whiter than
milk), and they are less viscous than solutions of the other
caseinates. Calcium caseinate solutions are produced by
 Author's personal copy
Casein and Caseinate: Methods of Manufacture 681

adding a slurry of lime (calcium hydroxide) in water to a casein
curd–water mixture, and the combined slurries react at a rela-
tively low temperature (<45  C) until the neutralization is
completed. Use of higher temperatures before neutralization
is likely to result in the precipitation or coagulation of the
partly reacted calcium caseinate, with the probable dumping
of the contents of the reaction vessel. All caseinate powders
have a white appearance.
Composition of Casein and Caseinates
The typical composition of casein and caseinates is shown in
Table 1. The caseins produced from lactic, sulfuric, or hydro-
chloric acid precipitation are almost indistinguishable from one
another. The rennet casein differs from acid casein particularly
in ash content and pH. During the acidification process, the
calcium and inorganic phosphate, which are associated with the
casein micelles in milk, are dissolved and leached from the curd
leaving only the organic phosphorus and a small residue of
calcium. Rennet casein contains about 3% calcium and approx-
imately 1.4% phosphorus. Sodium and calcium caseinates are
spray-dried products, their moisture content is much lower than
that of the caseins, and their protein content is higher. With a
pH in the range 6.5–7.0, sodium caseinate usually contains
1.2–1.4% sodium, whereas the calcium content of calcium
caseinate is in the range 1.3–1.6% (Table 2).
Properties of Casein and Caseinates
Solubility
Acid and rennet casein are insoluble in water. Virtually all
applications of casein products require them to be dissolved
first. Consequently, before use, acid casein must be dissolved
using an alkali to produce a solution with a pH of 6.5 or
higher. For nonfood, technical applications, acid casein may
be dissolved in other alkalis, such as borax or ammonia,
Table 1 Composition of casein products
Acid Rennet Sodium Calcium
Parameters casein casein caseinate caseinate
usually to a somewhat higher pH (7.5–9.5, or higher) than
that used for edible applications.
Water Absorption and Viscosity
Casein products can absorb substantial amounts of water, and,
as a result, they can modify the texture of dough or baked
products, serve as the matrix former in cheese-type products,
produce specialized plastic materials, or increase the consis-
tency of solutions such as soups. They are good film-formers
and find use in whipping and foaming applications, and in
emulsions of fats or oils in water.
Melting Properties
Casein exhibits melting properties that are unique among pro-
teins. Following limited proteolysis, casein becomes thermo-
plastic and flows when heated. A similar affect can be achieved
by chelating of some of the calcium ions present. These phe-
nomena are the basis for the melting of natural cheeses and the
production of process or imitation processed cheeses. A struc-
ture must exist before a substance can be said to melt. With
caseins, this structure may be obtained by precipitation with
calcium, acid, or the addition of rennin. Casein does not form
thermal gels and has little functionality in applications that
require temperature set.
High heat stability and the ability to melt are the two
properties of caseinates that make them difficult to replace in
many food applications. The demand for casein for use in
products such as cheese analogs (processed cheese,
mozzarella cheese) depends on the formation of a protein
matrix from calcium caseinate, which undergoes thermo-
melting similar to its processed cheese counterpart.
Whipping/Foaming Ability
Caseinates generally produce higher foam overruns, but they
also produce less stable foams than egg white or whey protein
concentrates. The excellent surfactant property of the
amphiphilic casein is also responsible for its use in whipped
toppings, cake mixes, and ice cream.

Moisture (%) 12.0 12.0 3.8 3.8

Protein (%) 90.0 84.0 91.4 91.2
Nutritional Properties
(Nx6.38) The nutritional quality of a protein is primarily determined by
Ash (%) 2.5 7.5 3.8 3.6 its essential amino acid content. For adult man, eight amino
Lactose (%) 1.0 1.0 0.1 0.1
acids are essential. These are isoleucine, leucine, lysine, methi-
Fat (%) 2.0 2.0 1.1 1.1
onine, phenylalanine, threonine, tryptophan, and valine; the
pH – – 6.5–6.9 6.8–7.0
infant requires histidine as well. In comparison with an ideal
reference protein composition that was developed by the FAO
in 1973, casein contains an adequate amount of all the essen-
Table 2 Mineral content of caseinates
tial amino acids, with the possible exception of the sulfur-
Minerals Sodium caseinate Calcium caseinate containing amino acids methionine and cysteine.

Sodium (%) 1.2–1.4 0.1

Calcium (%) 0.1 1.3–1.6 See also: Bioactive Peptides in Foods; Coffee: Analysis and
Iron (mg kg
1) 3–20 10–40 Composition; Milk: Sources and Composition; Protein: Food Sources;
Copper (mg kg
1) 1–2 1–2 Protein Quality and Amino Acids in Maternal and Child Nutrition and
Lead (mg kg
1) <1 <1 Health.

The Encyclopedia of Food and Health, (2016), vol. 1, pp. 676-682

 Author's personal copy
682 Casein and Caseinate: Methods of Manufacture
Further Reading
Carie M (1994) Casein. In: Concentrated and dried dairy products, pp. 199–225.
New York: VCR Publishers, Inc.
Fadaei V (2012) Milk proteins-derived antibacterial peptides as novel functional food
ingredients. Annals of Biological Research 3(5): 2520–2526.
Frisher H, Meisel H, and Schlimme E (2011) OPA method modified by use of N,
N-dimethyl-2-mercaptoethylammonium chloride as thiol components. Fresenius’
Journal of Analytical Chemistry 330: 631–633.
Mocanua AM, Moldoveanub C, Lucia Odochianb L, Cristina MP, Apostolescua N, and
Neculauc R (2012) Study on the thermal behavior of casein under nitrogen and air
atmosphere by means of the TG-FTIR technique. Thermochimica Acta 546: 120–126.
Pedersen L, Parlar S, Kvist K, Whiteley P, and Shattock P (2014) Data mining the
ScanBrit study of a gluten- and casein-free dietary intervention for children with
autism spectrum disorders: behavioural and psychometric measures of dietary
response. Nutritional Neuroscience 17(5): 207–213.
Southward CR (1994) Utilization of milk components: casein. In: Robinson RK (ed.)
Modern dairy technology. Advances in milk processing, vol. 1, 2nd ed.,
pp. 375–432. London, UK: Chapman Hall.
The Encyclopedia of Food and Health, (2016), vol. 1, pp. 676-682
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Swaisgood HE (2003) Chemistry of the caseins. In: Fox PF and Sweeney PLH (eds.)
Advanced dairy chemistry – 1, proteins, 3rd ed., pp. 139–201. New York: Kluwer
Academic/Plenum.
Wang J, Su J, Jia F, and Jin H (2013) Characterization of casein hydrolysates derived
from enzymatic hydrolysis. Chemistry Central Journal 7: 62–66.
Whiteley P, Shattock P, Knivsberg AM, et al. (2013) Gluten- and casein-free dietary
intervention for autism spectrum conditions. Frontiers in Human Neuroscience
6: 344–350.
Relevant Websites
http://ajpendo.physiology.org/content/300/3/E610 – American Journal of Physiology.
http://journal.chemistrycentral.com/content/7/1/62 – Chemistry Central Journal.
http://www.nutritionj.com/content/11/1/35 – Nutrition Journal and BioMed Central.
http://scholarsresearchlibrary.com/archive.html – Archives of Applied Science Research
Journals.