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the same as those used in modified milk production. Imitation milk powder production is used in a manner similar to modified milk powder and has multiple
advantages:
1. It has low productions costs (as the price of vegetable fat and protein is much
lower than for the corresponding milk components).
2. It serves well those parts of the world where there are no cattle and no milk
production.
3. It has a longer shelf life compared to milk powder.
4. It has a wide variation in composition, depending on the availability of ingredients.
Other dry dairy products include anhydrous milkfat, dried dairy beverages, dietetic dry products, coffee whiteners, dry fermented milk products, dry cream, dry
cheese products, dry ice cream mix, dry buttermilk, and single cell protein.

4.6 Dried Dairy Ingredients

4.6-1 Whey Powder
Whey, a by-product from cheese and casein manufacture, was traditionally returned
to the farmers as animal feed or as a fertilizer for spreading in the fields. Today,
large cheese factories are common and world cheese production continues to rise. It
is not economical to use whey in the traditional manner. Industrial processors have
been using heat concentrating and drying to make whey a more profitable entity. In
addition to the traditional dry whey products, there are other dry products derived
from whey as shown in Fig. 4.15.
The basic advantage of processing whey into powder is that there is no residue,
whereas the drawback is the need for expensive equipment and a large energy consumption. Converting whey into powder requires a large processing capacity but the
price of the final product is low in comparison with other dried or concentrated
products (for example, whey protein concentrates).
Whey can be transformed into powder by different techniques and the quality of
the product varies with the technology applied (Fig. 4.16). 3AU
For example, different processing procedures affect caking tendency (0 to 100%),
lactose crystallization rate (0 to 95%), free water content (1 to 4%), and so on. Caking
tendency is affected by the degree of lactose crystallization, as well as the number
and size distribution of the crystals.
Procedure a (flow chart in Fig. 4.16), in addition to resulting in a highly hygroscopic product, also uses a great amount of energy because whey can only be concentrated up to 45% of total solids in the evaporator.
By introducing lactose crystallization between evaporation and drying (Fig. 4.16,
Procedure b), powder quality and process economy are improved. Crystallization
starts in flash coolers or specially designed vacuum coolers and continues in crystallization tanks for 4 to 24 h, with constant agitation during filling and emptying of

CHCCSC
MILK

CHCCSC PRODUCTO
IN
RV
l CR

FB DRYING

SCfARATO
lN

PROCESSN
IG

ICAtACTOSO
l ASC
URCA CACTOSVL URCA
RCACTOR
GLUCOSC-GALACTOSC
PCRMCATC

WMCV

FG
lS

ULTRA FILTRATION

FC
l LO

FROTCN
I

LACTOSC
FCRMCNTATO
lN
CRYSTALLIZATION
CVAFORATN
tC
FAT
SCPARATO
I N OISTILLATION
VCAST

SCFARATO
IN
MOTMCR LQ
I UOR

CLCCTROOIALVSS
i

ALCOHOL
FAT
SPRAY
DRYING

RCCONSTtTUTO
lN

MOTHCR LIQUOR

POWDER

CHCCSC

SKIM MILK
NON-HVCROSCOFC
I
WHCV
FAT CNRC
t HCO
WHCY
CLCCTROOA
I LVSCO
WHCV

SCF
FROTCN
l
WHCV
FCRMCATC

Figure 4.15 Dry dairy products derived from whey. (Courtesy of A/S NIRO Atomizer.)
SCP = Single cell protein

ORDINARY
WHEY POWDER

PRECRYSTALLIZED
WHEY POWDER

Pretreatment

WHEY POWDER
(STRAIGHT THROUGH)

NON-CAKING

NON-CAKING
WHEY POWDER
(BELTPROCESS)

Pretreatment

Pretreatment

Pretreatment

Evaporation

Evaporation

Evaporation

Evaporation

42-45% TS

about 40% TS

about 40% TS

50% TS

Highconcentration
50-60% TS

Highconcentration
50-60% TS

Precrystallization

Precrystallization

Precrystallization

4-16 h

16-24 h

16-24 h

Spray drying

Spray drying

Spray drying

I 1 = 18O0C

ti = 2000C

tj= 1850C

Spray drying
q= 15O0C

Postcrystallization
Fluid-bed
drying

Fluid-bed
drying

Fluid-bed
cooling

Pneumatic
transport/cooling

Pneumatic
transport/cooling

Fluid-bed
cooling

[a]

[b]

[C]

Figure 4.16 Four different procedures of spray drying whey.

the tanks. For crystallization nuclei, pulverized a-lactose monohydrate (0.1%) or

crystallized whey powder (8.2%) is used. Quick cooling in flash coolers is accomplished at temperatures up to 300C which transforms /3-lactose into the a-form. The
mass is further cooled in the crystallization tank to 100C at a rate of 3C/h. During
procedures b, c, and d (Fig. 4.16), 50 to 75%, 75 to 85%, and 85 to 95% of the
lactose crystallize, respectively.
Whey powder is composed of large agglomerated particles in Procedures c (100
to 500 /xm) and e (up to 3000 /xm). It has excellent free-flowing characteristics

a)

c)

b)

Figure 4.17 Dead-end (a) versus cross-flow (b) ultrafiltration. (c) Cross section of asymmetric membrane of hollow fiber type.
and is not hygroscopic, with no caking tendencies. It is used extensively in food
processing.
In all four procedures, reverse osmosis may be used for partial whey concentration
(up to 25% total solids), prior to evaporation. This is an energy saving measure. It
must be emphasized that the two concentrating plants may be located in different
places.

4.6.2 Whey Protein Concentrates

There are several industrial methods suitable for the production of various whey
protein concentrates (WPC). The interest in whey processing is a result of two factors. One is a worldwide shortage of high-quality animal proteins that whey proteins
may alleviate, and the other is the problem with the disposal of whey. The high
biological oxygen demand (BOD) of whey makes this cheese by-product a pollutant
so that it is more desirable to process it than to dump it.
In addition to traditional methods such as evaporation and drying, modern methods used in industrial whey processing include ultrafiltration, microfiltration, reverse
osmosis (hyperfiltration), and demineralization (electrodialysis, ion exchange). The
most commonly used membrane method in dairying is ultrafiltration. Its industrial
application was aided by the introduction of cross flow instead of dead-end filtration
and the invention of asymmetric membranes27 (Fig. 4.17).
During the ultrafiltration of whey, low molecular weight compounds such as
lactose, minerals, nonprotein nitrogen, and vitamins are separated in the permeate,

whereas proteins are concentrated in the retentate. This permits a WPC with 20 to
60% protein in total solids and low quantities of lactose and mineral matter to be
obtained. Permeate, a by-product of this processing, is used for producing lactose,
alcohol, single cell protein, yeast, galactose, glucose, cattle feed, and various pharmaceuticals.
As ultrafiltration proceeds, an increased protein content of up to 98% may be
achieved by adding water to the feed.28 This proceure is called diafiltration. The
optimal moment to start diafiltration is when the total solids content has been reached
at which the ultrafiltration flux is still relatively high. That level of total solids must
be kept constant during diafiltration in order to minimize the water quantity needed.
To obtain 80% protein in total solids, the latter should reach a level of approximately
22 to 25%. The scheme of continuous WPC production is shown in Fig. 4.18.28
Sweet whey is first subjected to clarification (removal of casein fines, fat separation, and pasteurization). After pasteurization, the whey is cooled to 60 to 65C
and held at this temperature for 30 to 60 min before cooling to 500C for ultrafiltration.
This heat-and-hold treatment has the function of stabilizing the calcium phosphate
complex, and thus reduces the fouling of the membranes during ultrafiltration. Further reduction of the mineral content in WPC is achieved by adjusting pH of the
whey to pH 5.7 to 6.0 with HCl. In this way, the solubility of calcium is increased,
followed by its greater portion in the permeate. After ultrafiltration, the retentate is
pasteurized, evaporated, and dried. Although in Fig. 4.18 evaporation is included in
the process, a better solution is to directly dry the product. Depending on the protein
content, total solids may be increased from 22 to 25% up to 44% during ultrafiltration, and WPC may be dried directly as obtained from the ultrafiltration plant. This
provides a better quality of high protein product. To reduce or avoid protein denaturation, lower temperatures than those for drying milk are used: 160 to 1800C for
the inlet temperature and less than 800C for the outlet air temperature (Fig. 4.18).

4.6.3 Casein Products

4.6.3.1 Casein
Casein is the major milk protein. In addition to the protein moiety, it also contains
phosphorus, calcium, and citrate in the structure of its micelles.29"31
As the initial pH value of milk is decreased from 6.5, casein starts losing its
colloidal dispersibility and stability and begins to precipitate at pH 5.3. Maximum
precipitation takes place at pH 4.6, which is the isoelectric point of casein. Casein
may also be precipitated by proteolytic enzymes. Depending on the reagent used,
the following kinds of casein are produced.32"35
1. Acid casein is obtained by precipitating milk with an acid such as hydrochloric,
sulfuric, or lactic acid.
2. Sweet casein results from the action of chymosin.
3. Low-viscosity casein is produced by treating milk simultaneously with proteolytic enzymes and an acid.

Bag Filter
Powder So
li s
Evaporato
in

Spray Dryn
ig
Fluid Bod]

ChMM Factory from

Permeate Storage
Bufer lank
Whey Storage

Dyctone,

Beggn
ig

Pasteurziato
in
Clarification
Storage
SET
Separao
tin< !Wh.yCr.am
Heat
-transported

Pasteurziato
in
Retentate Storage

Hod
ln
ig lank
U
T
tR
O
tiFN
DU
IAR
FA
IUFR
AA
TT
IC
*.

Figure 4.18 Processing plant for production of WPC from sweet whey.

The basic operations in the production of casein are the same irrespective of the
type of casein produced. The flow chart of acid casein production, together with
sodium casemate production, is shown in Fig. 4.19.
The precipitation of casein in skim milk is initiated by changing the pH value of
the milk using hydrochloric, sulfuric, or lactic acid. The nature of the coagulum
(curd) obtained by direct precipitation of skim milk depends on the temperature of
precipitation, the intensity of agitation, and the final pH value of the precipitate. The
best results are obtained by atomizing a diluted acid solution such as 1.3 to IA N
HCl in a countercurrent direction to the flow of the milk maintained at 30 to 35C.

Skim milk

pH 4.6, lactic acid

fermentation,
HCl, H2SO4

Rennet
treatment

Casein curd

Casein curd

Draining, washing
pressing, milling
drying

Draining, washing
pressing, milling
drying

Acid casein

pH6-7
NaOH, KOH, Ca(OH)2

Rennet casein

Spray drying
Caseinate
Figure 4.19 Production of commercial casein and caseinate products.

In the next step, steam is injected into the mixture in order to rapidly increase its
temperature to cause coagulation, that is, 40 to 45C. The mixture is subsequently
directed into an inclined tube where it coagulates.
Skim milk may also be coagulated in a two-section plate heat exchanger. Acid is
injected into the skim milk after it passed through the first section of the heat exchanger, where it was heated to 300C by heat recuperated from whey processing.
The acidified skim milk is then heated to 45C by hot water in another section of
the heat exchanger. The yield of casein may be as high as 99%.
The procedure is the same regardless of the type of the acid used. Hydrochloric
and sulfuric acids are most commonly used. The selection of a particular acid depends on economic factors. Preference has been given to hydrochloric acid because
it is usually available at a lower cost than sulfuric acid.
An economical, high-capacity production of casein is based on the use of lactic
acid as a precipitating agent. Lactic acid can be produced inexpensively by the
fermentation of lactose. In New Zealand, almost all acid casein is produced in this
way, using cultures of Streptococcus lactis and/or Streptococcus cremoris.
Initially, this process, as well as all subsequent wet operations, were carried out
in cheese vats. The skim milk was inoculated at 25 to 27C with 0.5 to 1.5% of a
mixed lactic acid bacteria starter culture. The coagulation of the skim milk was

completed within 16 to 18 h. The temperature of the coagulum was then increased

to 50 to 600C by steam injection. The coagulum was cut with cheese knives and the
curd was agitated to facilitate syneresis until the final temperature was reached. The
whey was then drained and the curd was washed with water.
In 1963, Muller and Hayes36 designed a process for the manufacture of low
viscosity casein to be used in the paper industry. Such casein can be produced by
enzymatic coagulation of milk. Viscosity of a comparable regular acid casein solution is 2 Pa-s whereas a 15% solution of enzymatically produced casein has viscosity
of 0.3 to 0.4 Pa-s. In a continuous manufacturing procedure, approximately 40% of
the volume of the skim milk to be processed is treated with pepsin and then blended
with the remaining skim milk. Curd is formed following acid injection into the blend.
After the coagulation of the curd is completed, it is important to separate the whey
from it as soon as possible. This can be accomplished by draining the whey from
the holding tank through a decanter or an inclined dewheying screen.
The freshly precipitated casein, from which whey has been separated, is washed
in order to remove residual acids, salts, whey proteins, and lactose. The curd should
be washed at least three times, with each washing lasting 15 to 20 min in order to
ensure that the lactose content in the final product is reduced to a minimum. In the
countercurrent flow arrangement, the volume of the washing water is approximately
one half of the volume used in the parallel flow washing. The dry matter content of
the washed curd is approximately 45%.
In a continuous washing process, the curd is moving through a set of several
tanks. To separate the curd from the washing water, the top of each tank is equipped
with a 90-mesh draining screen, inclined 60 from the vertical line which separates
the curd from the washing water.33
In order the preserve the desired curd characteristics during washing, it is important to maintain the pH value of the washing water at 4.6, which is the isoelectric
point of casein. If water pH is lower than 4.6, a gelatinous layer may form on the
curd particle surface and obstruct the washing. Continuous casein pressing may be
accomplished by using a centrifuge, a screw press equipped with a pair of rotating
screws pressing and moving the curd, or a mechanically driven roller press equipped
with a pair of stainless steel rollers.
The curd is usually milled before drying in order to obtain particles of a uniform
size. These will dry evenly through the entire casein mass, thus avoiding incomplete
drying of a part of them and scorching of others. Vibrating dryers (fluid-bed dryers)
of the type used to dry other milk products are used most frequently to dry casein.
Recently, a new drying procedure called "attrition" drying has been designed.
The dryer consists of a rotor and a stator. The curd is ground during this procedure,
exposing a large surface to hot air circulating in the dryer and making the drying
proceed very rapidly. The resulting powder particles have irregular shapes with a
large number of cavities and readily disperse in water.
The objective of tempering is to cool the casein and to evenly distribute the
moisture in it. Hot casein, which has an uneven moisture distribution, is plastic and
very difficult to grind.

Table 4.4 APPROXIMATE PERCENTAGE COMPOSITION OF COMMERCIAL

CASEIN AND CASEINATE PRODUCTS
Components
Protein, N X 6.38 (min)
Ash (max)
Sodium
Calcium
Phosphorus
Lactose (max)
Fat (max)
Moisture (max)
pH

Sodium
Caseinate

Calcium
Caseinate

Acid
Casein

Rennet
Casein

94.0
4.0
1.3
0.1
0.8
0.2
1.5
4.0
6.6

93.5
4.5
0.05
1.5
0.8
0.2
1.5
4.0
6.8

95.0
2.2
0.1
0.08
0.9
0.2
1.5
10.0

89.0
7.5
0.02
3.0
1.5
1.5
12.0
7.0

Coprecipitate
89-94
4.5

1.5
1.5
5.0
6.8

Grinding produces uniform dimensions of the casein particles. They range from
300 to 600 /im in diameter. Particles obtained by attrition drying are considerably
smaller, that is, to 150 //,in in diameter.33
Ground casein is classified according to particle dimensions. It is sifted through
a series of gradually increasing mesh number sieves. Classified casein is packaged
in bags that are of the same kind as those used for milk powder packaging.
The approximate composition of commercial casein and casein products is presented in Table 4.4.
Casein is used in many industries such as the paper industry, the manufacture of
water-based paints, the production of adhesives, the food industry, the manufacture
of plastics, the production of casein fibres, the tanning industry, and the manufacture
of animal feeds and pet foods.

4.6.3.2 Sodium Caseinate

Casein consists of electrically charged proteins. The charges form polar regions along
the polypeptide chain. This makes casein an ampholyte that is capable of reacting
either with hydroxides or with acids depending on the pH value of the medium.
Casein reacts with various metal ions and forms caeinates such as sodium caseinate,
calcium caseinate, and others.
Sodium caseinate is commonly manufactured by a continuous process32"35 in
which thoroughly washed acid casein is used as the starting material. In addition to
raw casein, dry acid casein is also suitable as the starting material in the production
of sodium caseinate. Irrespective of the starting material used, 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 (Fig.
4.19). Raw acid casein is milled in a continuous mill and subsequently suspended
in a hot water tank.
The casein suspension is pumped from the holding tank into another tank while
the sodium hydroxide solution is simultaneously injected through a mixer. Water is

also added in order to maintain the total solids content of the caseinate solution
below the 20 to 22% level. The total solids content of the solution destined for spray
drying is 25 to 31% lower than that of milk, which is usually in the 45 to 55% range.
The low dry matter content, dictated by the requirement to maintain a low viscosity
of the sodium casemate solution, increases the production costs. The viscosity of
sodium caseinate solutions is a logarithmic function of the total solids concentration.
In order to increase the solids concentration to a maximum, a relatively high solubilization temperature of 90 to 95C is applied. The viscosity is lowest in the pH
range of 6.6 to 7.0. The raw acid casein must be completely free of lactose; otherwise
conditions favorable to the induction of Maillard reactions leading to the discoloration of the product would develop.
The homogeneous sodium caseinate solution obtained in the preceding operation
is usually spray dried in a stream of hot air. Only rarely is sodium caseinate dried
by roller drying. The total solids content of the solution destined for spray drying
ranges from 20 and 22% and may be exceptionally as high as 25%. The highest
permissible caseinate concentration is determined experimentally for every individual spray dryer.
All sodium caseinate produced commercially is used in the food industry. The
following foods are examples of products containing sodium caseinate: various kinds
of sausages, meat-based instant breakfast and milk-based instant breakfast, modified
milk, whipped cream, coffee whiteners, ice cream, desserts, sauces, soups, casein
bread, doughs, crackers, biscuits, dietetic products, and various protein-enriched
products. The two main reasons for using sodium caseinate as an ingredient in foods
are its functional properties and nutritive value.

4.6.3.3 Coprecipitates
In coprecipitate processing, high-temperature treatment of skim milk leads to the
interaction of the /3-lactoglobulin fraction of the whey proteins with K-casein. The
heat-induced K-casein/3-lactoglobulin complex is then coprecipitated with casein
by an acid, or another chemical agent such as CaCl2, or a mix of the two.32"35 Other
milk proteins are coprecipitated together with the casein-lactoglobulin complex.
Coprecipitates were patented in the 1950s and became more popular in the 1970s.
Their advantage over casein and its compounds is that they also consist of whey
proteins that contain relatively high concentrations of sulfur-containing amino acids.
This factor contributes to the biological value of coprecipitates. In addition, the
coprecipitate procedure increases the recovery of milk proteins.
In order to produce coprecipitates, skim milk is preheated and the final heating
of up to 900C in the second stage is obtained by steam injection into the milk. CaCl2
or acid is also injected through spray countercurrent to the direction of milk flow to
provide full mixing. The mixture is transformed into curd in a holding tube (20 to
25s). The curd is separated from the whey and the coprecipitate is washed, pressed,
and dried. At optimal process conditions it is possible to recover 95 to 97% of the
milk proteins. There are three basic varieties of coprecipitates, each having different
amounts of calcium33: low-calcium coprecipitate (LCC, 0.1 to 0.5% Ca), medium-

calcium coprecipitate (MCC, 1.0 to 1.5% Ca), and high-calcium coprecipitate (HCC,
2.5 to 3.0% Ca). The calcium concentration in coprecipitates can be changed by
changing basic parameters in the production process. A higher pH value at precipitation results in a higher calcium concentration in the product, whereas longer retention time at high temperature decreases calcium concentration.
Coprecipitates with different concentrations of calcium and polyphosphate and
different ratios of serum protein and casein have various uses in the food industry.
They each serve the same purpose as caseinates. The production process of coprecipitates has been developed in order to recover not only casein, which is about 80%
of all milk protein, but other proteins as well. This increases the recovered protein
to nearly 96%.

4.6.4 Lactose
Lactose is a disaccharide consisting of D-glucose and D-galactose. In the chemical
nomenclature, lactose is called 4-O-/3-D-galactopyranosyl-D-glucopyranose. It is the
major component of total milk solids and can be isolated on a commercial scale
from whole whey or from deproteinized whey.37"39 More recently, as the use of
membrane methods for the concentration and fractionation (ultrafiltration, hyperfiltration, etc.) of milk in the dairy industry is being expanded, the permeate obtained
by the ultrafiltration of whey is being used as the starting material in the production
of lactose.
Technological processes used to produce lactose may be divided into two basic
groups:
1. Crystallization of lactose from whey in the presence of whey proteins.
2. Crystallization of lactose from deproteinized whey after the removal of whey
proteins. Crude or refined lactose can be produced by either of these processes.
Lactose manufacture is shown in Fig. 4.20.37
The raw material for lactose production is evaporated in multistage vacuum
evaporators or may be subjected to preliminary concentration by reverse osmosis,
as well. The final concentration of lactose depends on whether proteins are present
in the syrup. If lactose is produced from protein-containing whey, the syrup is evaporated to increase its dry matter content to 60 to 65%. In the production of lactose
from deproteinized whey, the dry matter content of the syrup may be increased as
high as 70%.
Lactose crystallization is initiated in the hot syrup that had been concentrated to
oversaturation. The crystallization is initiated either spontaneously in oversaturated
syrups that are in an unstable crystallization state, or following the introduction of
seed crystals into syrups that are in the metastable crystallization state. The objective
of crystallization is to produce a large number of similar sized crystals (0.2 mm
average diameter) which would be easy to separate from the molasses.
A crystallizer is a double-walled closed tank having a conical bottom. It is
equipped with slow-motion agitators and scrapers which prevent the formed lactose
crystals from sticking to each other and from sedimenting.

Whey
Protein removal

Crystallization nuclei

Evaporation
60-65-70% TS
Water

Crystallization of lactose
^30 0 Ct 2 : 15-200C, 30h

Water

First separation of lactose crystals

600 xg
Water
Molasses

Second separation of lactose crystals

1200 xg
Hot water
Effluent

Dissolving of crude crystalline lactose

105C, 30% TS

Filtration
Evaporation
65-70% TS

Water

Crystallization nuclei

Crystallization of refined lactose

Water
Separation of crystals
Effluent

Drying
70C
Grinding
Packages

Sifting
Packaging
Crude or refined lactose

Figure 4.20 Flow chart of the production of crude or refined lactose.

Refining

- Sediment

Table 4.5 COMPOSITION OF COMMERCIAL LACTOSE PRODUCTS

Lactose
Component (%)
Lactose
Moisture
Protein (N X 6.38)
Ash
Fat
Acid (as lactic acid)

Technical

Row

Edible Grade

Pharmaceutical Grade

98.0
0.35
1.0
0.45
0.2
0.4

94.0
0.3
0.8
0.4
0.1
0.4

99.0
0.5
0.1
0.2
0.1
0.06

99.4-99.85
0 . 1 - 0.5
0.01- 0.05
0.03- 0.09
0.001- 0.01
0.04- 0.03

From ref. 4.

Crude crystalline lactose, which is in the a-monohydrate form, is separated from

the molasses in continuous centrifuges or decanters. Two centrifuges are used in a
sequence. In the first centrifuge, the crystals are separated from the molasses, and in
the other centrifuge, the crystals are washed with water. Molasses, which contain 38
to 48% of dry matter, including 30% lactose (the rest consists of proteins and salts),
may also be recycled. They are diluted with fresh whey or with the wash water to
contain a dry matter content of approximately 15%. Crude lactose has a moisture
content of 10 to 14% and the dry matter contains approximately 99% lactose.
Crude lactose that is not destined for refining is dried at approx. 700C in one of
the numerous types of dryers where the moisture content is reduced to 0.1 to 0.5%.
The subsequent operations consist of grinding, sifting, and packaging and are similar
to those in the production of skim milk powder.
The manufacture of lactose from deproteinized whey differs from the manufacture
of lactose using whole whey. The major difference is the removal of proteins at the
beginning of the operation. The most common method for the removal of proteins
is based on ultrafiltration or heat-induced coagulation by steam injected into whey
acidified to pH 6.2 (Centri Whey).40
The objective of refining lactose is to remove contaminants such as proteins, salts,
and colored substances that may remain in the mix. Refined lactose is almost chemically pure. It contains a minimum of 99.6% lactose and no protein.
The production process is the same as that for crude lactose except the separation
of the lactose crystals and their washing. Refining consists of dissolving the crude
crystalline lactose in water at high temperature, adding specific chemicals (e.g., charcoal and/or filtration aids), filtration, evaporation, crystallization of lactose, and separation of the crystals. The subsequent operations such as drying, grinding, sifting,
and packaging are the same as those for crude lactose production.
Agglomerated lactose powder is produced using the same procedures as those
used in the production of instant milk powder. This form of lactose is used in the
pharmaceutical industry.
The average composition of commercial forms of lactose is presented in Table 4.5.

4.7 References
1. Hall, C. W., and T. I. Hedrick. 1975. Drying of Milk and Milk Products. AVI, Westport, CT. 338
pp.
2. Wiegand B. 1985. Evaporation. In R. Hansen (ed.), Evaporation, Membrane Filtration and Spray
Drying in Milk Powder and Cheese Production. North European Dairy Journal, Vanl0se, Denmark,
pp. 91-178.
3. Masters, K. 1984. Spray Drying Handbook, 4th edit. George Godwin, London. 696 pp.
4. Caric\ M. 1990. Technology of Concentrated and Dried Dairy Products, 3rd edit. Naucna Knjiga,
Beograd, Yugoslavia, 293 pp. (in Serbian).
5. Kiermeier, F., and E. Lechner. 1973. Milch und Milcherzeugnisse. Paul Parey, Berlin, Germany,
443 pp.
6. Food and Drug Administration. 1978. Standards, Food and Drugs: Evaporated Milk, 131.130, 153
pp.
7. Swaisgood, H. E. 1986. Chemistry of milk protein. In P. F. Fox (ed.), Developments in Dairy
Chemistry-1. Proteins, pp. 1 -60. Elsevier Applied Science, London.
8. Holt, C. 1985. The milk salts: their secretion, concentrations and physical chemistry. In P. F. Fox
(ed.), Developments in Dairy Chemistry-3. !Lactose and Minor Constituents, pp. 143-182. Elsevier
Applied Science, London.
9. Kessler, H. G. 1988. Lebensmittel- und Bioverfahrenstechnik. Molkereitechnologie, 3rd edit.
A. Kessler, Freising, Germany, 582 pp.
10. Knipschildt, M. E. 1986. Drying of milk and milk products. In R. K. Robinson (ed.), Modern Dairy
Technology Advances in Milk Processing, Vol. 1, pp. 131-234. Elsevier Applied Science, London.
11. Westergaard, V. 1983. Milk Powder Technology, Evaporation and Spray Drying, 3rd edit. Niro
Atomizer, Copenhagen, Denmark, 147 pp.
12. Hallstr0m, B. 1985. Evaporation versus hyperfiltration. In R. Hansen (ed.), Evaporation, Membrane
Filtration and Spray Drying in Milk Powder and Cheese Production, pp. 289-298. North European
Dairy Journal, Vanl0se, Denmark.
13. Walstra, P. 1983. Physical chemistry of milk fat globules. In P. F. Fox (ed.), Developments in Dairy
Chemistry-2. Lipids, pp. 119-158. Elsevier Applied Science, London.
14. Caric", M. 1988. Nonenzymic browning of dairy products. In Reactions of Nonenzymic Browning of
Food Products, pp. 105-141. Naudna Knjiga, Beograd, Yugoslavia (in Serbian).
15. Morrissey, P. A. 1985. Lactose: chemical and physiochemical properties. In P. F. Fox (ed.), Developments in Dairy Chemistry-3. Lactose and Minor Constituents, pp. 1 -34. Elsevier Applied Science,
London.
16. Masters, K. 1985. Spray drying. In R. Hansen (ed.), Evaporation, Membrane Filtration and Spray
Drying in Milk Powder and Cheese Production, pp. 299346. North European Dairy Journal, VanI0se, Denmark.
17. Pisecky, J. 1983. New generation of spray dryers for milk products, Dairy Indust. Int 48: 21-24.
18. Caric*, M., and M. Kalb, 1987. Effects of drying techniques on milk powders quality and microstructure: a review. Food Microstructure 6: 171-180.
19. Peebles, D. D. 1936. U.S. Patent 2,054,441.
20. Peebles, D. D., and D. D. Clary, Jr. 1955. U.S. Patent 2,710,808.

21. Peebles, D. D. 1958. U.S. Patent 2,s35,586.

22. Pisecky, J. 1985. Technological advances in the spray dried milk. / . Soc. Dairy Technol. 38: 60-64.
23. Caric, M. 1991. Drying technologies developments in dairying, Marschall Rhone-Poulenc International Dairy Science Award Lecture, ADSA Annual Meeting, Logan, Utah, USA.
24. Caric, M. 1993. Concentrated and Dried Dairy Products. VCH Publishers, New York.
25. Corbin, E. A., and E. O. Whittier. 1972. The composition of milk. In Fundamentals of Dairy Chemistry, pp. 1-36. AVI, Westport, CT.
26. Packard, V. S. 1982. Human Milk and Infant Formula. Academic Press, New York, 269 pp.
27. Loeb, S., and S. Sourirajan. 1964. U.S. Patent 3,133,132.
28. Ottosen, N. 1991. Membrane filtration for whey protein concentrate. Marketing Bulletin, APV Pasilac AS, Copenhagen, Denmark, pp. 3-22.
29. Schmidt, D. G. 1986. Association of caseins and casein micelle structure. In Developments in Dairy
Chemistry-1. Proteins, pp. 6186. Elsevier Applied Science, London.
30. Belitz, H. D., and W. Grosch. 1986. Food Chemistry, 2nd edit. Springer-Verlag, Berlin, Germany,
774 pp.
31. Kalib, M., E. Phipps-Todd, and P. Allan-Wojtas. 1982. Milk gel structure XIII. Rotary shadowing
of casein micelles for electron microscopy. Milchwissenshaft 37: 513-518.
32. Morr, C. V. 1986. Functional properties of milk proteins and their use as food ingredients. In P. F
Fox (ed.), Developments in Dairy Chemistry-1. Proteins, pp. 375-400. Elsevier Applied Science,
London.
33. Muller, L. L. 1986. Manufacture of casein, caseinates and co-precipitates. In P. F. Fox (ed.), Developments in Dairy Chemistry-1. Proteins, pp. 315-338. Elsevier Applied Science, London.
34. Mulvihill, D. M. 1989. Caseins and caseinates: manufacture. In P. F. Fox (ed.), Developments in
Dairy Chemistry-4. Functional Milk Proteins, pp. 97-130. Elsevier Applied Science, London.
35. Southward, C. R. 1986. Utilization of milk components: casein. In R. K. Robinson (ed.), Modern
Dairy Technology, Vol. 1, pp. 317-368. Elsevier Applied Science, London.
36. Muller, L. L. and E. J. Hayes. 1963. The manufacture of low-viscosity casein. Austr. J. Dairy
Technol. 18: 184-188.
37. 0stergaard, B. 1988. Lactose from ultrafiltration permeate. Marketing Bulletin, APV Pasilac AS,
Copenhagen, Denmark, pp. 3-14.
38. Modler, H. W. 1984. Functional properties of nonfat dairy ingredients: a review. /. Dairy Sci. 68:
2206-2214.
39. Brinkmann, G. E. 1976. New ideas for the utilization of lactose: principles of lactose manufacture.
Soc. Dairy Technol. 29: 101-107.
40. Anonymous. 1988. Dairy Hand Book, Alfa-Laval, AB, Lund, 219 pp.