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weak compared to the affinity in the presence of stabilizing anions (e.g., F ,

SO 4 2 -). 302
Heat induced changes on conformation also change binding behavior of proteins.
Upon heat treatment at 75C for 10 and 20 min, the binding affinity of /3-lg for
2-nonanone was reduced and the number of sites for binding was increased.303 This
was related to conformational changes and aggregation of /3-lg.

Measurement of Flavor Binding

Methods for the measurement of flavor binding have recently been reviewed by
Wilson.304 Flavor binding is usually determined by equilibrium measurements using
headspace analysis, membrane dialysis, and solvent extraction techniques.

4.4 Some Selected Processing Effects on the Functional

Properties of Major Milk Proteins
The functional properties of milk proteins depend on the molecular structure, and
consequently on every factor which may modify the molecular structure, including
the source of the milk, the type of protein (caseins and whey proteins), and the
processes used for the preparation or isolation of the milk proteins.29'305"307 Cheftel
and Lorient,17 Kinsella,14 Harper,308 and especially Schmidt et al?09 have suggested
that essentially every step in the processing of milk protein products is important,
either directly or indirectly, in determining the final functional properties of milk
proteins. Major processing steps that have been reported to affect the functional
properties of major milk proteins are given in Table 4.11. However, in many instances, the mechanisms(s) by which a processing step changes functionality is not
understood.
In this section, the effect on proteins and their functional properties of two processing effects (heat treatments and filtration processes) are briefly discussed.

4.4.1 Effects of Heat Treatments

Heat processing is generally considered to be one of the most important single factor
influencing functionality, more particularly, whey protein functionality.64'308"314
However, much of the effect of heat thermal treatment depends on the degree of the
treatment and on media conditions (pH, presence of ions such as Ca2 + ). Some of
the contradictory results could possibly be explained by differences in heat treatment
parameters (Lorient et al 1991).29

4.4.1.1 Effects on Caseins

Caseins in micellar form, and especially sodium casemates, are exceptionally thermostable; typically, milk withstands heating at 1400C at pH 6.7 for 20 minutes before
coagulation occurs and sodium caseinates withstands heating at 1400C for at least

Table 4.11

PROCESSING-RELATED VARIABLES THAT MAY AFFECT

THE FUNCTIONAL PROPERTIES OF CASEIN AND WHEY
PROTEIN PRODUCTS
Effect on Functionality
Caseins
Whey Proteins

Processing Variables
Thermal treatment
Forewarming
Milk pasteurization
Milk sterilization
Evaporation and concentration
Dehydration
Pretreatment before fractionation
Lipid removal
pH adjustment
Fractionation and isolation
Technique used
Miscellaneous factors (pumping, storage, etc.)
Cheese processing
Starter used
Coagulant used
Process modifications (cooking temperature,
calcium chloride, water washing, etc.)
Storage factors
Casein or whey storage conditions
Casein or whey protein product storage
conditions
Sanitation factors
Microbiological load
Antimicrobial agent added

Direct
(a)

Indirect
(b)

+
+
+
+
+

Direct
(a)

Indirect

+
+

+
+

(+)

(+)
+

+
+

+
+
+

+
+
+

(+)
(+)

(+)
(+)

+
+

+
+

(b)

+
+
+
+

+
+
+

+
+

a: Direct protein conformation or denaturation effect,

b: Indirect protein effect or effect on compositional factors
+ : Variable has an effect; : Variable has no effect.
Adapted from Refs. 9, 64, 308, 309, 312.

60 minutes.312 The remarkable stability of caseins at high temperatures is principally

due to the low levels of secondary and tertiary structures.
From a physicochemical point of view, heating or cooling milk above or below
physiological temperature causes a shift in the calcium phosphate equilibrium which
affects some properties of milk, especially rennet coagulability. On cooling, colloidal
calcium phosphate (CCP) dissolves, and some casein, especially /3-casein, dissociates from the micelles,315'316 contributing to the increase in the rennet coagulation
time (RCT) of milk observed during cold storage. Conversely, on heating, the soluble
/3-casein reassociates with the micelles and the RCT is reduced.312 Furthermore, heat
treatments in the range of 80-150C, such as preheating of milk, in-container sterilization, and UHT processes, induce changes in caseins such as (1) dephosphory-

Table 4.12 SOME HEAT-INDUCED CHANGES IN

MILK PROTEINS
Protein Type or Structure

Modifications

Caseins

Dephosphorylation
Proteolysis
Covalent bond formation

Micellar structure

Zeta-potential
Hydration changes
Association-dissociation

Whey proteins

Unfolding-aggregation
Disulfide interchange

lation, (2) proteolysis, (3) covalent bond formation, and (4) changes in casein micellar structures, etc. (Table 4.12) which differ only in rate and not in nature.312
1. Casein is completely dephosphorylated in 5 h at 1200C and approximately
50% dephosphorylation occurs within 1 h.317 Milk concentration increases the rate
of dephosphorylation; preheating has no effect on the rate of dephosphorylation of
unconcentrated milk but reduces the rate for concentrated milk.318 Dephosphorylation, which reduces protein charge, might be expected to affect the heat stability of
milk but its specific contribution has not been quantified.313
2. Although the nature of the proteolysis products formed on heating has not
been studied in detail,312 some authors have reported the appearance of glycopeptides
in milk heated at temperatures >50C, 319 and of peptides similar to the glycomacropeptide after a treatment at 1200C for 20 minutes.320 Furthermore, formation
of nonprotein nitrogen from milk proteins at temperatures >100C is almost linear
with time; 10 to 20% of total nitrogen is solubilized after 5 h at 1200C317 or 60
minutes at 135C.321
3. During heat treatment of proteins, reactions can occur between reactive side
chains of some amino acids, such as Iysine and cysteine, and other amino acid
residues, carbohydrates, or lipids. The browning that occurs when milk is heated at
temperatures > 1000C is a consequence of the Maillard reaction between the carbonyl
group of lactose and the e-amino group of lysine.
4. Heating milk causes a number of changes in casein micelles such as the aggregation of casein micelles during UHT sterilization.322""324 This increase in casein
micelle size probably results from the combined effects of the heat denaturation of
whey proteins and their deposition onto micellar surfaces and from the increase in
micellar calcium which may lead to calcium bridges between micelles.324 The increase in micelle size during heating is also accompanied by a large increase in the
number of very small particles.325'326 These particles may be formed by the breaking
up of casein micelles327"329 due to the removal of colloidal calcium by soluble citrate.
The citrate is normally neutralized by soluble calcium but calcium phosphate precipitates when the milk is heated. Finally, at normal pH, milk coagulation occurs at
14O0C after about 20 minutes. The heat stability of milk, which is considerable

economic importance, is influenced by many compositional factors as well as processing effects.313-330-331 In the case of pH, Rose 332 ' 333 showed that the heat coagulation time-pH profile of most milks (type A) showed a maximum at approximately
6.7 and a minimum at 6.9. The pH effect in milk coagulation is a function of
K-casein concentration on micelle surfaces and the /3-lg concentration in the milk
serum. The minimum appears to be due to the dissociation of K-casein from the
casein micelles at pH >6.9 while the maximum is related to the presence of /3-lg.
Some milk samples from individual cows fail to show minimum and maximum
points on the curve, but instead coagulation time increases as the pH increases from
6.2 to 7.4: such milk is referred to as "type B " . Tessier and Rose 334 eliminated the
minimum in the curve of type A milk by adding K-casein, thus converting it to type
B. They also converted type B milk to type A by salting out some K-casein or by
adding /3-lg.

4.4.1.2 Effects on Whey Proteins

Heating globular proteins causes them to unfold and this unfolding is accompanied
by an endothermal heat effect (heat uptake). This effect may be observed by differential scanning calorimetry as a function of temperature or time.335 Table 4.12
presents the denaturation characteristics of some whey proteins.
1. /3-lactoglobulin. With a denaturation temperature of 78C, /3-lg is the most
stable of the serum proteins. A second thermal change appears near 14O0C caused
by the breakdown of disulphide bonds and additional unfolding of the molecule.335
The heat denaturation of /3-lg is pH dependent. After an acidic heat treatment (pH
2.5,900C, 10 to 15 minutes), /3-lg is still soluble. Two molecular species are present:
one (60%) is soluble at pH 4.5 and is identical to native protein; the other (40%),
insoluble at pH 4.5, has been irreversibly denatured but without aggregation, probably due to the electrostatic repulsions at this pH.336-337 Heating at pH 4.5 (70 to
85C, 15 to 30 minutes) resulted in a denatured /3-lg insoluble throughout the pH
range. Proteins are aggregated due to the formation of intermolecular disulphide
bonds. Heat treatments at neutral pH have also been examined. At 800C, pH 6.8 to
7.5, /3-lg is partially denatured without aggregation and loss of solubility. It seems
that thiol groups, unmasked and activated at pH >6.8, initiate intramolecular disulfide rearrangements that stabilize the molecule.335
2. a-lactalbumin. With a denaturation temperature of 62C, a-la is the least stable
whey protein, but requires the most heat per gram for unfolding. It has long been
assumed that a-la. was the most stable serum protein due to the reversibility of the
heat denaturation at pH 6. Recent studies have clearly shown that the reversible
denaturation of a-la is due to calcium ion dissociation and reassociation from the
protein338 which is a calcium metalloprotein. Solubility studies on purified whey
proteins as a function of pH and temperature showed that a-la is insoluble from pH
3.5 to 5. A solubility minimum is attained at pH 4.2 which corresponds to the
isoelectric point of a-la.339 The partial, reversible thermal denaturation of a-la and
its effect on the solubility of the protein at reduced pH values has been exploited in
the development of a process for whey protein fractionation.340-341

A large variety of heat treatments have been studied to increase the utilization of
whey proteins17'23'26'342"344 as well as the impact of heat treatments inherent to the
processing of milk such as pasteurization. Indeed, even mild heat treatments such
as standard pasteurization have been shown to affect the functionality of whey protein concentrates.345-346 Morr345 reported that pasteurization (72C for 15 seconds)
of cheese whey increased the foaming of a cheese whey concentrate at both pH 4.5
and pH 9.0, whereas the pasteurization of acid whey decreased the foaming of an
acid whey protein concentrate. Mangino et ai346 studying these same products,
found that the binding of alkanes by whey protein concentrates was increased by the
pasteurization of both types of whey.
Lorient et al.29 have studied the emulsifying and foaming properties of purified
a-la and /3-lg as a function of heat treatment and pH. The two proteins show improved emulsifying activity when heated at 700C for 30 minutes at acid or neutral
pH; the activity of /3-lg is always higher. When heated at 900C for 60 minutes,
emulsifying activity is only improved at acid pH. As for foaming properties, the
combined effects of pH and heat treatment appear to be different for the two proteins;
a positive effect when heated at basic, neutral or isoelectric pH for /3-lg, and an
negative effect a-la (especially at pH 2). Conversely, the foaming properties of
a-la are improved at pH 2-5.

4.4.2 Membrane Separation Processes

New developments in membrane separation processes and their application in the
dairy industry have opened up new possibilities both for the production and utilization of milk protein ingredients. The use of classical isolation methods such as
precipitation with acid, heat or chemicals, and isoelectric coagulation, affect the
native state of milk proteins and thus their functional properties. Conversely, the use
of membrane processes for separation or concentration is based on differences in the
physical characteristics of milk components such as their molecular weight. As a
consequence, the native state of the proteins is not altered.347'348
Membrane separation processes are generally divided into four categories according to the molecular size of the retained solutes. Fig. 4.10348 shows schematically
the spectrum of particle sizes encountered in various dairy systems in relation to
alternate filtration-based separation processes available to the dairy industry. Information on recent engineering advances involving these processes may be found
elsewhere.349"352 For the purpose of this monograph, the following names and meanings as defined by Jelen348 are used.
Microfiltration (MF) being more specifically used to remove large particles such
as casein fines, microorganisms, or microbial spores, fat globules, somatic cells,
phopholipoprotein particles, etc. (Fig. 4.10) from whey or milk is not treated in the
following section. However, recent information on the influence of operating parameters, and applications of MF in the dairy industry may be found in Olesen and
Jensen,353 Pedersen,354 and Pearce et al.355

Particle Size
(Hin)
Approx. Molecular
Weight (D)

io !

Particle
Characteristics
Approx. Flux
(L/m2h)
Approx. Operating
Pressure (Bar)

Relative size of
milk systems
components

io' 3

io'<

Ionic

io 3

30

40

30

Ions

io!O5

10*

Molecular

Macromolecular

100

1000

Microparticular

Cellular

300
1

20

Vitamins

Bacteria
Whey Protein Aggregates, Cheese Fines

UF
NF

Yeasts, Molds

Fat Globules

Casein Micelles

Salts

RO

10

510 5

Whey Proteins

Lactose/Derivat.

Process for
Separation

io- !

Traditional Filtration

MF

Figure 4.10 Spectrum of application of membrane separation processes in the dairy industry.
(Adapted from Ref. 348.)

4.4.2.1 Reverse Osmosis (RO)

In reverse osmosis (RO), a purified liquid is separated from the feed solution, which
contains solutes (usually low molecular weight salts) or other liquids. The use of
RO is increasing in the dairy industry for many reasons. First, the concentration of
food process356 streams to 10 to 25% total solids can, in some cases, be accomplished
at lower cost with RO than with evaporation. Second, low temperature concentration
by RO minimizes loss of volatile flavor components and adverse changes in heatsensitive food components. RO can also be used to treat effluent streams to produce
reusable water.
Fouling is a major problem for the RO of whey. Calcium salts, especially calcium
phosphate, are primary foulants.357'358 Whey pretreatments (acidification, heat treatment) to remove or reduce the effects of calcium salts have been studied to improve
performance. However, as explained in a preceding section, the effect of these treatments on whey functionality must be considered.

4.4.2.2 NanoMtration (NF)

The main emerging applications for the dairy industry of NF is for the partial demineralization of whey-like materials.359"360 Since NF is used mainly for the removal of mineral ions that contribute to the osmotic pressure in dairy systems,361*362
the operating pressure reported for some of the experimental uses is lower than the
pressures used in RO.

4.4.2.3 Ultrafiltration (UF)

The traditional application of UF is for the separation and fractionation of individual
milk proteins from lactose and minerals. There are many other industrial uses, consistent with the size exclusion specificity of the process, including the standardization
of milk protein content,363 the production of milk concentrates (casein, casemates,
coprecipitates, etc.),347 or the production of cheese.358'364"369 Information on various
recent applications of UF in the dairy industry may be found elsewhere.347-363'369-370
In the subsequent sections only some classical examples on the use of this process
for protein concentration and the resulting functional properties are dealt with.
1. Ultrafiltration of milk. The composition of ultrafiltered whole or skim milk
retentate as a function of the concentration factor varies in the following ways:
increase in the content of total solids, fat (for whole milk), and protein, and decrease
in the lactose content. Depending on the degree of concentration, there is a corresponding variability in the composition of the concentrate. Distribution of the individual nitrogen fractions is modified during UF. The proportions of casein and whey
protein increase with the concentration factor due to the corresponding decrease in
all the other nitrogen fractions (NPN). Green et al?lx reported that with an increasing
concentration factor the proportion of casein in the micellar form decreases to a
small extent (from 98.8 to 86.1% of total casein). This phenomenon may be due to
an increased interaction with fat in the more concentrated milk. However, Shrilaorkul
et al.372 also noted a decrease in the average diameter of the casein micelles in
ultrafiltered skim milk (3X; 5X) and related it to the change in the composition of
casein and minerals, particularly calcium and phosphate. Casein micelle size distribution in milk is important as it is related to the stability of milk to heat and rennet
coagulation373 and affects the rheological properties of milk products.
Retentates resulting from the UF of milk display different properties from those
of the original milk. There is a change in flow properties (increased viscosity) with
the increasing content of solids. A problem associated with this high degree of
viscosity is that air bubbles in the retentate are not released quickly and may become
incorporated into the product giving a spongy texture.367 Concentration by UF 6X
causes formation of aggregates that do not break upon dilution even during prolonged
storage and can only be disrupted by homogenization at pressures in excess of 200
bars.374
The heat stability of milk protein concentrates is also different, as they are more
susceptible to denaturation than whey proteins.375 With a heat treatment at 75C for
5 minutes of denaturation increases from 31% in skim milk to 64% in UF retentates
with a concentration factor of 4.4:1. 376 However, the soluble milk proteins resulting
from the UF of milk will usually keep their original functional properties to a large
extent and the functional properties of the concentrates may even be improved as a
result of the higher protein content.
2. Application of UF to cheesemaking. The main application of UF technology
in cheesemaking is for the standardization of protein content, especially for the
production of Camembert in France377 and UF Feta in Denmark.378 The application
of UF technology in cheesemaking is usually linked to the expectation of obtaining

an increased yield due to a better recovery of fat and protein. However, if in most
cases UF technology allows substantially better yields, in some cases there has been
no yield improvement over traditional cheesemaking.366 Apart from extra yield, UF
technology has other potential advantages compared to thermoseparation technology.
The UF process is simple, allows on accurately control total solid content, and is
less sensitive to pH variations.369
The important factor is the kind of cheese being made and the amount of syneresis
that must take place in the cheesemaking process after UF is complete. Cheesemaking parameters such as calcium and lactose concentration have to be considered when
UF milk is used. Cheeses made from precheese normally possess a stronger buffering
power than that associated with traditional cheese of the same type, making it more
difficult to attain the optimum low pH which controls texture, quality, and spoilage
bacteria.358
UF can also be used to concentrate the milk to total protein concentration ratios
not exceeding 2:1, after which cheesemaking proceeds in the traditional manner. The
resulting cheeses usually satisfy existing standards of identity, but yield increases
are modest.
3. Ultrafiltration of whey. Whey is ultrafiltered to concentrate the native whey
proteins to obtain powders with varying protein content. Although whey protein
concentrates have been produced since 70, their full potential has not been realized
due to variations in functional properties.379"383 A recent survey of commercial whey
protein concentrates (WPC) and whey protein isolates (WPI), confirmed a high degree of variability in gross composition, individual protein composition, physicochemical properties, and flavor of WPC.385 A number of whey pretreatment methods
have been developed to improve UF membrane flux rates and increase overall recovery. Some pretreatments have led to real improvement such as (1) the clarification
procedure for acid and sweet wheys developed by de Wit et a/.379'384 involving the
precipitation of bacteria and lipids at pH 4.6; (2) microfiltration prior to UF to clarify
and remove the fouling components;386'387 and (3) delipidation by thermocalcic aggregation.341-388'389 Pretreatments are important because they can modify the protein
retention ratio and consequently the composition and the functional properties of the
WPC.389 WPC composition is also altered by the concentration factor reached during
the UF and the diafiltration step which lowers the lactose/protein and salt/protein
ratios.
For whey protein concentrates produced by UF processes, pretreatment processes
induce protein/calcium interactions, and storage can induce changes in protein
conformation due to differences in the functionality of whey protein products.309
Mangino et at.346 found that ultrafiltration increased the hydrophobicity of the whey
protein concentrates as measured by alkane binding. Harris et al.390 reported that
ultrafiltration caused a slight increase in surface hydrophobicity.

4.5 Conclusion
Certain techniques that can be used to modify the functional properties of dairy
proteins such as cross-linking with transglutaminase, succinylation, phosphorylation,

amidation and esterification, thiolation, glycosylation, etc.,261-391 396 will not be discussed because, as far as we know, they have not gone beyond the experimental
stage.26-308
Chemical treatments can be used to substantially modify the functional properties
of milk proteins.397 However, there is some doubt as to the negative effects on
nutritional value as well as to the presence of trace amounts of the chemicals remaining after the treatment which limits the use of chemically modified proteins for
the present.
The development of physical treatments for the concentration and separation of
milk proteins will allow the industrial-scale production of enriched protein fractions
that are relatively pure and that have specific nutritional properties. The physiological
or functional properties of certain sequences,5'6'396'398"403 and the infinite possibilities for generating new sequences by enzymatic hydrolysis makes it possible to
envisage significant advances in high value-added industries (parapharmaceutical,
cosmetic).7-404 The transformation of milk proteins into a wide range of food ingredients will allow the use of previously surplus protein, will meet the requirements
of the food industry in terms of functionally specific ingredients and will allow the
dairy industry to compete a better footing with other protein sources. Competition
from vegetable proteins has become very stiff, with proteins from vegetable sources
already in a dominant position for many food ingredients:26 it is primordial that the
dairy industry will be able to provide ingredients with superior functional properties
to once again become the principal source of ingredients for the food industry.405
Consequently, to optimize the use of milk protein as a food ingredient, more
research is still needed on:
1. Investigation of individual functional properties and factors affecting them;
2. Obtaining a better understanding of the manner in which protein/ingredient interactions affect the properties of foods that contain milk protein products;
3. Standardization of methods for testing functionality both in aqueous systems and
in model food systems, with more attention to standardization of model food
systems in the future; and
4. Processing-induced effects on functionality, with emphasis on fractionation, concentration, drying, and storage.

4.6 Acknowledgments
We would like to thank Dr. Michel Britten, Dr. Sylvie Gauthier, Dr. Yves Pouliot,
and Dr. Jean-Christophe Vuillemard for reading the manuscript and for their helpful
comments. Their excellent advice, however, was not always followed and we must,
therefore, accept full responsibility for any remaining errors and shortcomings. We
would also like to thank Mrs. Raymonde Gosselin for typing the manuscript and
Mr. Gene Bourgeau for editorial assistance. Finally, we also thank editors and authors who have given permission to copy tables and figures from published works.
Furthermore, although this chapter was a team effort, we would like to underline
more specifically that, under the supervision of Paul Paquin (Director of the Dairy

Sciences Research Center, Universite Laval, Quebec), Olivier Robin was responsible
for the section dealing with "Protein-Protein and Protein-Surface Interactions," and
Dr. Sylvie Turgeon for the section dealing with "Some Processing Effects."

4.7 References
1. Cochet, D. 1991. Nutrition et sante": une attente du consommateur, un objectif de l'industrie laitiere.
U Lait 71:123-131.
2. Odergaard, M. 1991. La situation laitiere du monde. Rev. Laitiere Frangaise 512:66-69.
3. Kinsella, J. E., D. M. Whitehead, J. Brady, and N. A. Bringe. 1988. Milk proteins: possible relationships of structure and function. In P. F. Fox (ed.), Developments in Dairy Chemistry. 4. Functional Milk Proteins, pp. 55-95. Applied Science Publishers, London.
4. Fligner, K. L., and M. E. Mangino. 1991. Relationship of composition to protein functionality. In
N. Parris and R. Barford (eds.), pp. 1-12. ACS Symp. Ser. 454, American Chemical Society,
Washington D.C.
5. Perraudin, J. 1991. Proteines a activity's biologiques: lactoferrine et lactoperoxydase. Connaissances
re*ce"mment acquises et technologie d'obtention. Le Lait 71:191-212.
6. Maubois, J. L., J. Le*onil, R. Trouve\ and S. Bouhallab. 1991. Les peptides du lait a activity physiologique. 3. Peptides du lait a effet cardiovasculaire: activity antithrombotique et antihypertensive.
Le Lait 71:249-261.
7. Cotte, J. 1991. Le lait, une matiere d'avenir pour Ia cosme"tique. Le Lait 71:213-224.
8. Pour-El. A. 1979. Preface. In A. Pour-El (ed.), Functionality and Protein Structure, pp. ix-xii. ACS
Symp. Ser. 92, American Chemical Society, Washington D.C.
9. Cheftel, J. C , J.-L. Cuq, and D. Lorient. 1985. Proteines Alimentaires, pp. 45-94, 156-192.
Lavoisier Tec. Doc., Paris.
10. Lorient, D. 1988. Les proprie"te*s fonctionnelles: interface entre propri6t6s physiques, physicochimiques et sensorielles? In D. Lorient, B. Colas, and M. Le Meste (eds.), Proprietes Fonctionnelles
des Macromolecules Alimentaires, pp. 1 - 7 . Les Cahiers de 1 'ENS.BANA6, Lavoisier Tec. Doc.,
Paris.
11. Israelachvili, J. N. 1985. lntermolecular and Surface Forces with Applications to Colloidal and
Biological Systems, Academic Press, New York.
12. Damodaran, S. 1989. Interrelationship of molecular and functional properties of food proteins. In
J. E. Kinsella and W. G. Soucie (eds.), Food Proteins, pp. 21-51. American Oil Chemists' Society,
Champaign.
13. Kato, A. 1991. Significance of macromolecular interaction and stability in functional properties of
food proteins. In N. Parris and R. Barford (eds.), Interactions of Food Proteins, pp. 13-24. ACS
Symp. Ser. 454, American Chemical Society, Washington D.C.
14. Kinsella, J. E. 1984. Milk Proteins: physicochemical and functional properties. CRC Crit. Rev.
Food Sci. Nutr. 21:197-262.
15. Kinsella, J. E. 1976. Functional properties of proteins in foods: a survey. CRC Crit. Rev. Food Sci.
Nutr. 7:219-280.
16. de Wit, J. N. 1981. Structure and functional behaviour of whey proteins. Neth. Milk Dairy J.
35:47-64.

17. Cheftel, J. C, and D. Lorient. 1982. Les proprie^s fonctionnelles des prote*ines laitieres et leur
amelioration. Le Lait 42:435-483.
18. Fox, P. F., and D. M. Mulvihill. 1982. Milk proteins: molecular, colloidal and functional properties.
J. Dairy Res. 49:679-693.
19. Fox, P. F., and D. M. Mulvihill. 1983. Functional properties of caseins, casemates and casein
coprecipitates. In Physicochemical Aspects of Dehydrated Protein-Rich Milk Products, pp.
188-259. Proc. IDF Symp., Helsing0r.
20. de Wit, J. N. 1984. Functional properties of whey proteins in food systems. Neth. Milk Dairy J.
38:71-89.
21. Kinsella, J. E., and P. F. Fox. 1986. Water sorption by milk proteins. CRC Crit. Rev. Food Sci.
Nutr. 24:91-139, also in IDF Bulletin (1987), 209:219-280.
22. Modler, H. W. 1985. Functional properties of nonfat dairy ingredients: a review. Modification of
products containing casein. J. Dairy Sci. 68:2195-2205.
23. Modler, H. W. 1985. Functional properties of nonfat dairy ingredients: a review. Modification of
lactose and products containing whey proteins. J. Dairy Sci. 68:2206-2214.
24. Morr, C. V. 1985. Functionality of heated milk proteins in dairy and related foods. J. Dairy Sci.
68:2773-2781.
25. Leman, J., and J. E. Kinsella. 1989. Surface activity, film formation, and emulsifying properties of
milk proteins. CRC Crit. Rev. Food Sci. Nutr. 28:115-138.
26. Vuillemard, J.-C, S. Gauthier, and P. Paquin. 1989. Les ingredients a base de prote"ines laitieres:
obtention, propri6ts et utilisations. Le Lait 69:323-351.
27. Paquin, P., and E. Dickinson. 1990. Emulsion and foams interactions protein/lipids at interface.
Proc. XXIII International Dairy Congress. 2, pp. 1492-1507, Montreal.
28. Tomberg, E., A. Olson, and K. Persson. 1990. Structural and interfacial properties of food proteins
in relation to their function in emulsions. In K. Larsson and S. E. Friberg (eds.), Food Emulsions,
2nd edit., pp. 247-326. Marcel Dekker, New York.
29. Lorient, D., D. Closs, and J.-L. Courthaudon. 1991. Connaissances nouvelles sur les propri6t6s
fonctionnelles des prot6ines du lait et de ses d&iv6es. Le Lait 71:141-171.
30. Pour-El. A. (ed.). 1979. Functionality and Protein Structure. ACS Symp. Ser. 92, American Chemical Society, Washington D.C.
31. Cherry, J. P. (ed.). 1981. Protein Functionality in Foods. ACS Symp. Ser. 147, American Chemical
Society, Washington D.C.
32. Cherry, J. P. (ed.). 1982. Food Protein Deterioration: Mechanisms and Functionality. ACS Symp.
Ser. 206, American Chemical Society, Washington D.C.
33. Dickinson, EM and G. Stainsby. 1982. Food Colloids. Applied Science Publishers, London.
34. Dickinson, E., and G. Stainsby (eds.). 1988. Advances in Food Emulsions and Foams. Elsevier
Applied Science, London.
35. Mitchell, J. R., and D. A. Ledward (eds.). 1986. Functional Properties of Food Macromolecules.
Elsevier Applied Science, London.
36. Brash, J. L. and T. A. Horbett (eds.). 1987. Proteins at Interfaces: Physicochemical and Biochemical Studies. ACS Symp. Ser. 343, American Chemical Society, Washington D.C.
37. Fox, P. F. (ed.). 1988. Developments in Dairy Chemistry. 4. Functional Milk Proteins. Elsevier
Applied Science, London.

38. Lorient, D., D. Colas, and M. Le Meste (eds.). 1988. Proprietes Fonctionnelles des Macromolecules
Alimentaires. Les Cahiers de l'ENS.BANA6, Lavoisier Tec. Doc., Paris.
39. Kinsella, J. E., and W. G. Soucie (eds.). 1989. Food Proteins. American Oil Chemists' Society,
Champaign.
40. Parris, N., and R. Barford (eds.). 1991. Interactions of Food Proteins. ACS Symp. Ser. 454, American Chemical Society, Washington D.C.
41. Harris, P. (ed.). 1990. Food Gels. Elsevier Applied Science, London.
42. Larsson, K., and S. E. Friberg (eds.). 1990. Food Emulsions, 2nd edit., Marcel Dekker, New York.
43. Swaisgood, H. E. 1982. Chemistry of milk proteins. In P. F. Fox (ed.), Developments in Dairy
Chemistry. 1. Proteins, pp. 1-59. Applied Science Publishers, London.
44. Eigel, W. N., J. N. Butler, C. A. Ernstrom, H. M. Farrell, V. R. Harwalkar, R. Jenness, and R. Mc.
L. Witney. 1984. Nomenclature of the proteins of cow's milk: 5th revision. J. Dairy Sci. 67:
1599-1631.
45. Fox, P. F. 1988. The milk protein system. In P. F. Fox (ed.), Developments in Dairy Chemistry. 4.
Functional Milk Proteins, pp. 1-53, Applied Science Publishers, London.
46. Ribadeau-Dumas, B. 1989. Structure and variability of milk proteins. In C. A. Barth and E.
Schlimme (eds.), Milk Proteins: Nutritional, Clinical, Functional and Technological Aspects, pp.
112-123. Springer-Verlag, New York.
47. Papiz, M. Z., L. Sawyer, E. E. Eliopoulos, A. C. T. North, J. B. C. Findlay, R. Sivapragadarao,
T. A. Jones, M. E. Newcomer, and P. J. Kraulis. 1986. The structure of p-lactoglobulin and its
similarity to plasma retinol-binding protein. Nature (London) 324:383-385.
48. Monaco, H. L., G. Zanotti, P. Spadon, M. Bolognesi, L. Sawyer, and E. E. Eliopoulos. 1987.
Crystal structure of the trigonal form of bovine p-lactoglobulin and of its complex with retinol at
2.5 A resolution. /. MoI. Biol. 197:695-706.
49. Southward, C. R. 1988. Uses of casein and casemates. In P. F. Fox (ed.), Developments in Dairy
Chemistry. 4. Functional Milk Proteins, pp. 173-244. Applied Science Publishers, London.
50. de Wit, J. N. 1988. The use of whey proteins products. In P. F. Fox (ed.), Developments in Dairy
Chemistry. 4. Functional Milk Proteins, pp. 323-345. Applied Science Publishers, London.
51. Haylock, S. J., and W. B. Sanderson. 1991. Milk protein ingredients: their role in food systems.
In N. Parris and R. Barford (eds.), Interactions of Food Proteins, pp. 59-72. ACS Symp. Ser. 454,
American Chemical Society, Washinton D.C.
52. Franks, F. (ed.). 1975 Water: A Comprehensive Treatise. 4. Aqueous Solution of Amphiphiles and
Macromolecules. Plenum Press, New York.
53. Franks, F. (ed.). 1975 Water: A Comprehensive Treatise. 5. Water in Disperse Systems. Plenum
Press, New York.
54. Becher, P. (ed.). 1983. Encyclopedia of Emulsion Technology. 1. Basic Theory, Marcel Dekker,
New York.
55. Becher, P. (ed.). 1985. Encyclopedia of Emulsion Technology. 2. Applications, Marcel Dekker,
New York.
56. Bird, R. B., R. C. Armstrong, and O. Hassager. 1987. Dynamics of Polymeric Liquids. 1. Fluid
Mechanics. John Wiley & Sons, New York.
57. Creamer, L. K. 1991. Some aspects of casein micelles structure. In N. Parris and R. Barford (eds.),
Interactions of Food Proteins, pp. 148-163. ACS Symp. Ser. 454, American Chemical Society,
Washington D.C.

58. Dalgleish, D. G. 1990. Casein micelles: surface properties and aggregation. In Proc. XXIII International Dairy Congress. 3, pp. 1513-1533. Montreal.
59. Walstra, P. 1990. On the stability of casein micelles. / . Dairy Sci. 73:1965-1979.
60. Paquet, D. 1989. Revue bibliographie: Ia fraction prote*ose-peptones du lait. Le lait 69:1-21.
61. Payens, T. A., and H. J. Vreeman. 1982. Casein micelles and micelles of a and P casein. In K. L.
Mittal and E. J. Fendler (eds.), Solution Behavior of Surfactants: Theorical and Applied Aspects.
L, pp. 543-571. Plenum Press, New York.
62. Clark, A. H., and C. D. Lee-Tuffnell. 1985. Gelation of globular proteins. In J. R. Mitchell and
D. A. Ledward (eds.), Functional Properties of Food Macromolecules, pp. 203-272. Elsevier
Applied Science, London.
63. Dumay, E. 1988. De"naturation thermique de Ia (3-lactoglobuline et propriete's ge*lifiantes des concentre's prote*iques de lactose"rum. In D. Lorient, B. Colas and M. Le Meste, (eds.), Proprietes
Fonctionnelles des Macromolecules Alimentaires, pp. 67-87. Les Cahiers de TENS.B AN A. 6,
Lavoisier Tec. Doc., Paris.
64. Pearce, R. J. 1989. Thermal denaturation of whey protein. IDF Bulletin 238:17-23.
65. Lumry, R. 1973. Some recent ideas about the nature of the interactions between proteins and liquid
water. J. Food Sci. 38:744-755.
66. Kuntz, I. D., and W. Kaufman. 1974. Hydration of proteins and polypeptides. Adv. Protein Chem.
28:239-345.
67. Chou, D. H., and C. V. Morr. 1979. Protein-water interactions and functional properties. J. Am.
Oil Chemists' Soc. 56:53A-62A.
68. Rockland, L. B., and G. F. Stewart (eds.). 1981. Water Activity Influences on Food Quality. Academic Press, New York.
69. Damodaran, S., and J. E. Kinsella. 1982. Effects of ions on proteins conformation. In J. P. Cherry
(ed.), Food Protein Deterioration: Mechanisms and Functionality, pp. 327-357. ACS Symp. Ser.
206, American Chemical Society, Washington D.C.
70. Simatos, D., J. L. Multon (eds.). 1985. Properties of Water in Foods in Relation to Quality and
Stability. Martinus Nijhoff Publishers, Dordrecht.
71. Franks, F. 1988. Protein hydration. In F. Franks (ed.), Characterization of Proteins, pp. 127-154.
Humana Press, Clifton.
72. Hardman, T. M. (ed.). 1989. Water and Food Quality. Elsevier Applied Science, New York.
73. Morr, C. V. 1989. Beneficial and adverse effects of water-protein interactions in selected dairy
products. J. Dairy Sci. 72:575-580.
74. Kneifel, W., P. Paquin, T. Abert, and J.-P. Richard. 1991. Water-holding capacity of proteins with
special regard to milk proteins and methodological aspects: a review. 7, Dairy Sci. 74:2027-2041.
75. Schnepf, M. 1989. Protein-water interactions. In T. M. Hardman (ed.), Water and Food Quality,
pp. 135-168. Elsevier Applied Science, New York.
76. Fennema, O. 1977. Water and protein hydration. In J. Whitaker and S. Tannenbaum (eds.), Food
Proteins, pp. 50-90. AVI Publishers Co., Wesport.
77. Mulvihill, D. M., and P. F. Fox. 1988. Physicochemical and functional properties of milk proteins.
In P. F. Fox (ed.), Developments in Dairy Chemistry. 4. Functional Milk Proteins, pp. 131-172.
Applied Science Publishers, London.
78. Kneifel, W., T. Abert, and W. Luf. 1990. Influence of preheating skimmilk on water-holding
capacity of sodium salts of casemates and coprecipitates. / . Food Sci. 55:879-880.

79. Van der Berg, C, and S. Bruin. 1981. Water activity and its estimation in food systems: theoretical
aspects. In L. B. Rockland and G. F. Stewart (eds.), Water Activity: Influences on Food Quality,
pp. 1-61. Academic Press, New York.
80. Ru'egg, M. 1985. Water in dairy products related to quality, with special reference to cheese. In
D. Simatos and J. L. Multon (eds.), Properties of water in Foods in Relation to Quality and Stability,
pp. 603-635. Martinus Nijhoff Publishers, Dordrecht.
81. Labuza, T. 1985. Water binding humectants. In D. Simatos and J. L. Multon (eds.), Properties of
water in Foods in Relation to Quality and Stability, pp. 421445. Martinus Nijhoff Publishers,
Dordrecht.
82. van der Berg, C. 1985. Development of B. E. T.-like models for sorption of water on foods. Theory
and relevance. In Simatos and J. L. Multon (eds.), Properties of water in Foods in Relation to
Quality and Stability, pp. 119-131. Martinus Nijhoff Publishers, Dordrecht.
83. Harwalkar, V. R., and R. J. Brown. 1989. Symposium: water-protein interactions. Introduction.
J. Dairy ScL 72:561.
84. Kuntz, I. D. 1975. The physical properties of water associated with biomolecules. In R. Duckwort
(ed.), Water Relations of Food, pp. 93-109. Academic Press, New York.
85. de Moor, H., and A. Huyghebaert. 1983. Functional properties of dehydrated protein-rich milk
products. In Physicochemical Aspecs of Dehydrated Protein-Rich Milk Products, Proc. IDF Symp.,
pp. 276-301. Helsing0r.
86. de Wit, J. N. 1990. Interactions of milk components with other ingredients in food systems. In
Proc of XXlII International Dairy Congress. 3, pp. 14371455, Montreal.
87. Weisser, H. 1985. Influence of temperature on sorption equilibria. In D. Simatos and J. L. Muiton
(eds.), Properties of water in Foods in Relation to Quality and Stability, pp. 95-118. Martinus
Nijhoff Publishers, Dordrecht.
88. Berlin, E., P. G. Kliman, B. A. Anderson, and M. J. Pallansch. 1973. Water binding in whey protein
concentrates. J. Dairy Sci. 56:685-694.
89. Knightbridge, J. P. and A. Goldman. 1975. Water absorptive capacity of dried milk products.
N. Z. J. Dairy Sci. Technol. 10:152-161.
90. Bech, A.-M. 1980. The physical and chemical properties of whey proteins. Dairy Ind. Int.
11:25-33.
91. Bull, H., and K. Breese. 1986. Protein hydration. 1. Binding sites. Arch. Biochem. Biophys.
128:488-496.
92. Labuza, T. 1977. The properties of water in relationship to water binding in foods, a review.
J. Food Proc. Preser. 1:167-190.
93. Patel, P. D., and J. C. Fry. 1987. The search for standardised methods for assessing protein functionality. In B. J. F. Hudson (ed.), Developments in Food Proteins. 5, pp. 299-333. Elsevier Applied
Science, London.
94. de Wit, J. N., and R. Boer. 1975. Ultrafiltration of cheese whey and some functional properties of
the resulting whey protein concentrate. Neth. Milk Dairy J. 29:198-211.
95. de Wit, J. N., and G. Klarenbeek. 1986. Method for the determination of rehydratation and solubility
of powdered protein-rich milk products. Milchwissenschaft 41:463-467.
96. Riiegg, M., M. Luscher, and B. Blanc. 1974. Hydration of native and rennin coagulated caseins as
determined by differential scanning calorimetry and gravimetric sorption measurements. J. Dairy
Sci. 57:387-393.

97. Korolczuck, J. 1982. Viscosity and hydration of neutral and acidic milk protein concentrates and
caseins. N. Z. /. Dairy Sci. TechnoL 17:135-140.
98. Hermansson, A.-M., and C. Akesson. 1975. Functional properties of added proteins correlated with
properties of meat systems. / . Food Sci. 40:595-602.
99. Farel, H. M. Jr., H. Pessen, and T. F. Kumosinski. 1989. Water interactions with bovine caseins
by hydrogen-2 nuclear magnetic resonance relaxation studies: structural implications. J. Dairy Sci.
72:562-574.
100. Arakawa, T., and S. N. Timasheff. 1987. Abnormal solubility of p-lactoglobulin salting-in by
glycine. Biochemistry 26:5147-5153.
101. Jasinski, E., and A. Kilara. 1985. Flavor binding by whey proteins. Milchwissenschaft 40:596-599.
102. Hermansson, A.-M. 1972. Functional properties of proteins for food-swelling. Lebensm. Wiss. u.
TechnoL 5:24-29.
103. Back, J. F., D. Oakenfull, and M. B. Smith. 1979. Thermal stability of proteins. Biochemistry
18:5191-5196.
104. Anon. 1985. Official method ba 11-65. In Official Methods and Recommended Practices of the
Americam Oil Chemists' Society, 3d edit., AOAC, Champaign.
105. Anon. 1985. Official method ba 10-65. In Official Methods and Recommended Practices of the
Americam Oil Chemists' Society, 3d edit., AOAC, Champaign.
106. Rha, C. K., and P. Pradipasena. 1986. Viscosity of proteins. In J. R. Mitchell and D. A. Ledward
(eds.), Functional Properties of Food Macromolecules, pp. 79-120. Elsevier Applied Science,
London.
107. Rha, C, K. 1978. Rheology of fluids. Food TechnoL 32 (7):77-82.
108. Menjivar, J. A. ,and C. K. Rha. 1980. Viscoelastic effects in concentrated protein dispersions.
Rheot Ada. 19:212-219.
109. Menjivar, J. A., and C. K. Rha. 1980. Characterization of concentrated systems: constraint and
compressibility effects. In G. Astarita, G. Marrucci, and L. Nicolais, (eds.), Rheology. 2. Fluids,
pp. 293-299. Plenum Press, New York.
110. Einstein, A. 1906. Eine neue bestimmung der molekuldimensionen. Ann. Physik. 19:289-306.
111. Einstein, A. 1911. Berichtigung zu meiner arbeit: eine neue bestiummung der molekuldimensionen.
Ann. Physik. 24:591-592.
112. Pradipasena, P., and C. K. Rha. 1977. Effect of concentration on apparent viscosity of a globular
protein solution. Polym. Engng. Sci. 17:861-864.
113. Mooney, M. 1951. The viscosity of a concentred suspension of spherical particles. / . Colloid Sci.
6:162-170.
114. Hermansson, A.-M. 1975. Functional properties of proteins for foods. Flow properties. / . Texture
Studies 5:425-439.
115. Towler, C. 1974. Rheology of casein solutions. N. Z. J. Dairy Sci. TechnoL 9:155-160.
116. Tung, M. A. 1978. Rheology of protein dispersions. J. Texture Studies 9:3-31.
117. Colas, B. 1988. Viscosite" des casernes, casemates et copre'cipite's. Bases physicochimiques et influence des conditions de preparation et d'utilisation. In D. Lorient, B. Colas, and M. Le Meste
(eds.), Proprietes Fonctionnelles des Macromolecules Alimentaires, pp. 88102. Les Cahiers de
l'ENS.BANA-6 (Lavoisier Tec. Doc, Paris.)

118. Hayes, J. F., and L. L. Muller. 1961. Factors affecting the viscosity of solutions of acid-precipitated
caseins. Aust. J. Dairy Technol. 16:265-269.
119. Purri, B. R., U. Mohindroo, and R. C. Malik. 1972. Studies in physico-chemical properties of
caseins. 3. Viscosities of casein solutions in different alkalies. /. Indian Chem. Soc. 49:855-863.
120. Barrat, J.-F., inventor. 1976. Case"inate ameliore et procSde" pour Ie pre"parer. French Patent
2,370,441 of 16.11.1976, LactoseYum France, France.
121. Hayes, J. F., P. M. Southby, and L. L. Muller. 1968. Factors affecting the viscosity of casemates
in dispersions of high concentrations. / . Dairy Res. 35:31-47.
122. Mohanty, B., D. M. Mulvihill, and P. F. Fox. 1988. Hydration-related properties of caseins at pH
2.0-3.0. Food Chem. 27:227-236.
123. Korolczuck, J. 1982. Effect of temperature on viscosity and hydration of casein in neutral and
acidic solutions. N. Z. / . Dairy Sci. Technol. 17:273-276.
124. Buma, T. J. 1980. Viscosity and density of concentrated lactose solutions and of concentrated
cheese whey. Neth. Milk Dairy 34:65-68.
125. Richardson, B. C. 1982. The effect of storage on viscosity of some casein solutions. N. Z. /. Dairy
Sci. Technol. 17:277-282.
126. Grufferty, H. B., and P. F. Fox. 1988. Functional properties of casein hydrolysed by alkaline milk
proteinase. N. Z. J. Dairy Sci. Technol. 23:95-108.
127. Towler, C , L.K. Creamer, and C. R. Southward. 1981. The effect of disulphide-bond reducing
agents on the viscosity of casein solutions. N. Z. J. Dairy Sci. Technol. 16:155-165.
128. Couarraze, G., and J. L. Grossiard. 1983. Initiation a Ia Rheologie, pp. 73-121. Lavoisier Tec.
Doc., Paris.
129. Flory, P. J. 1974. Gels and gelling processes. Introductory lecture. Chem. Soc. London, Faraday
Discuss. 57:7-18.
130. de Gennes, P. G. 1979. Scaling Concepts in Polymer Science, pp. 128-162. Cornell University
Press, Ithaca, New York.
131. Tombs, M. P. 1974. Gelation of globular proteins. Che. Soc. London, Faraday Discuss.
57:158-164.
132. Mulvihill, D. M., and J. E. Kinsella. 1987. Gelation characteristics of whey proteins and (3-lactoglobulin. Food Technol. 9:102- 111.
133. Foegeding, E. A. 1989. Molecular properties and functionality of proteins in food gels. In J. E.
Kinsella and W. G. Soucie (eds.), Food Proteins, pp. 185-194. American Oil Chemists' Society,
Champaign.
134. Bottomley, R. C , M. T. A. Evans, and C. J. Parkinson. 1990. Whey proteins. In P. Harris (ed.),
Food Gels, pp. 435-466. Elsevier Applied Science, New York.
135. Gordon, M., and S. B. Ross-Murphy. 1975. The structure and properties of molecular trees and
betworks. Pure Appl. Chem. 43:1-26.
136. Clark, A. H. 1987. The application of networks theory to food systems. In J. M. V. Blanshard and
P. Lillford (eds.), Food Structure and Behaviour, pp. 13-34. Academic Press, London.
137. Ferry, J. D. 1948. Proteins gels. Adv. Protein Chem. 4:1-78.
138. Edsall, J. T., and H. Gutfreund. 1983. Biothermodynamics: The Study of Biochemicals Processes
at Equilibrium. John Wiley & Sons, Chichester.

139. Mangino, M. E. 1984. Physicochemical aspects of whey protein functionality. /. Dairy Sci.
67:2711-2722.
140. Richardson, R. K., and S. B. Ross-Murphy. 1981. Mechanical properties of globular gels. 1. Incipient .gelation behaviour. Int. J. Biol. Macromol. 3:315-322.
141. Hillier, R. M., and G. C. Cheeseman. 1979. Effect of proteose-peptone on the heat gelation of
whey protein isolates. J. Dairy Res. 46:113-120.
142. Schmidt, R. H. 1981. Gelation and coagulation. In J. P. Cherry (ed.), Protein Functionality in
Foods, pp. 313-147. ACS Symp. Sere. 147, American Chemical Society, Washington D.C.
143. Paulsson, M. P., P. O. Hegg, and H. B. Castberg. 1986. Heat-induced gelation of individual whey
proteins. A dynamic Theological study. / . Food Sci. 51:87-90.
144. Hermansson, A.-M. 1979. Aspect of protein structure, rheology and texturization. In P. Sherman
(ed.), Food Texture and Rheology, pp. 265-282. Academic Press, London.
145. Schmidt, R. H., B. L. Illingworth, and E. M. Ahmed. 1978. Heat-induced gelation of peanut protein/
whey blends. / . Food Sci. 42:613-621.
146. Buccheim, W., and P. Jelen. 1976. Microstructure of heat coagulated whey protein curd. Milchwissenschaft 31:589-592.
147. Hermansson, A.-M. 1979. Aggregation and denaturation involved in gel formation. In A. Pour-El
(ed.), Functionality and Protein Structure, pp. 81-103. ACS Symp. Ser. 92, American Chemical
Society, Washington D.C.
148. Schmidt, R. H., B. L. Illingworth, and E. M. Ahmed. 1978. The effect of dialysis on heat induced
gelation of whey protein concentrates. /. Food Proc. Preser. 2:111-121.
149. Harwalkar, V. R., and M. Kalab. 1985. Thermal denaturation and aggregation of p-lactoglobulin
in solution. Electron microscopy study. Milchwissenschaft 40:65-68.
150. Schmidt, R. H., B. L. Illingworth, J. C. Deng, and J. A. Cornell. 1979. Multiple regression and
response surface analysis of the effect of calcium chloride and cysteine on heat-induced whey
protein gelation. / . Food Sci. 27:529-532.
151. Hillier, R. M., R. L. J. Lyster, and G. C. Cheeseman. 1980. Gelation of reconstituted whey powder
by heat. J. Sci. FoodAgric. 31:1152-1157.
152. Razanajatovo, L., and C. Alais.1979. Ge"lification des prote*ines lactosdriques en presence de saccharose. 2. Etude biochimique. Le Lait 59:34-45.
153. Razanajatovo, L., C. Alais, and R. Paul. 1978. Gelification des prote*ines Iactos6riques en presence
de saccharose. Influence de certains parametres physicochimiques. Le Lait 58:483-495.
154. Doi, H., S. Ideno, F. H. Kuo, F. Ibuki, and M. Kanamori. 1983. Gelation of the complex between
K-casein and p-lactoglobulin. J. Nutr. Sci. Vitaminology 29:679-689.
155. Doi, H., T. Tokuyama, F. H. Kuo, F. Ibuki, and M. Kanamori. 1983. Heat-induced complex formation between K-casein and a-lactalbumin. Agric. Biol. Chem. 47:2817-2824.
156. Bourne, M. C. 1982. Food Texture and Viscosity: Concept and Measurement. Academic Press,
London.
157. Larmond, E. 1987. Beyond the texture profile. In J. M. V. BIanshard and J. R. Mitchell (eds.),
Food Structure: Its Creation and Evaluation, pp. 449-463. Butterworths, London
158. Szczesniak, A. S. 1963. Classification of textural characteristics. J. Food Sci. 28:385-389.
159. Szczesniak, A. S. 1975. General food texture profile revisited: ten years perspective. J. Food Sci.
6:5-17.

160. Ross-Murphy, S. B. 1987. Small deformation measurements. In J. M. V. Blanshard and J. R.

Mitchell (eds.), Food Structure: Its Creation and Evaluation, pp. 387-400. Buttenvorths, London.
161. Davies, J. T., and E. K. Rideal. 1963. Interfacial Phenomena, pp. 1-52, Academic Press, London.
162. Parker, N. S. 1987. Properties and functions of stabilizing agents in food emulsions. CRC Crit.
Rev. Food ScL Nutr. 25:285-315.
163. Fisher, L. R., and N. S. Parker. 1988. Effect of surfactants on the interactions between emulsion
droplets. In E. Dickinson and G. Stainsby (eds.), Advances in Food Emulsions and Foams,
pp. 45-90. Elsevier Applied Science, London.
164. Stainsby, G. 1985. Foaming and emulsification. In J. R. Mitchell and D. A. Ledward (eds.), Functional properties of Food Macromolecules, pp. 315-353. Elsevier Applied Science, London.
165. Phillips, M. C. 1977. The conformation and properties of proteins at liquid interfaces. Chem. &
Ind. March (5): 170-176.
166. Hesselink, F. Th. 1971. On the theory of the stabilization of dispersions by adsorbed macromolecules. 1. Statistics of the change of some configurational properties of adsorbed macromolecules
on the approach of an impenetrable interface. J. Phys. Chem. 75:65-71.
167. Adamson, A. W. 1990. Physical Chemistry of Surfaces, 5th edit., pp. 203-257. John Wiley &
Sons, New York.
168. Graham, D. E., and M. C. Phillips. 1979. Proteins at liquid interfaces. 2. Adsorption isotherms.
/. Colloid Interface Sci. 76:415-426.
169. Tornberg, E. 1987. Interfacial behavior of food proteins studied by the drop volume method. In
J. L. Brash and T. A. Horbett (eds.), Proteins at Interfaces: Physicochemical and Biochemical
Studies, pp. 647-664. ACS Symp. Ser. 343. American Chemical Society, Washington, D.C.
170. Dickinson, E., B. Murray, and G. Stainsby. 1988. Protein adsorption at air-water interface and oilwater interfaces. In E. Dickinson and G. Stainsby (eds.), Advances in Food Emulsions and Foams,
pp. 123-162. Elsevier Applied Science, London.
171. de Feijter, J. A., and J. Benjamins. 1987. Adsorption kinetics of proteins at the air-water interface.
In E. Dickinson (ed.), Food Emulsions and Foams, pp. 72-85. Royal Society of Chemistry,
London.
172. Cumper, C. W. N., and A. E. Alexander. 1950. The surface chemistry of proteins. Trans. Faraday
Soc. 46:235-253.
173. MacRitchie, F. 1978. Proteins at interfaces. Adv. Protein Chem. 32:283-324.
174. Benjamins, J., J. A. de Feijter, M. T. A. Evans, D. E. Graham, and M. C. Phillips. 1975. Dynamic
and static properties of proteins adsorbed at the air/water interface. Faraday Discuss Chem. Soc.
59:218-229.
175. MacRitchie, F., and A. E. Alexander. 1963. Kinetics of adsorption of proteins at interfaces. 1. The
role of bulk diffusion in adsorption. / . Colloid Sci. 18:453-457.
176. Kim, S. H., and J. E. Kinsella. 1985. Surface activity of food proteins: relationships between surface
pressure development, viscoelasticity of interfacial films and foam stability of bovine serum albumin. / . Food Sci. 30:1526-1530.
177. Castle, J., E. Dickinson, B. S. Murray, and G. Stainsby. 1987. Mixed protein films adsorbed at the
oil-water interface. In J. L. Brash and T. A. Horbett (eds.), Proteins at Interfaces: Physicochemical
and Biochemical Studies, pp. 118-134. ACS Symp. Ser. 343, American Chemical Society, Washington D.C.
178. Graham, D. E., and M. C. Phillips. 1979. Proteins at liquid interfaces. 3. Molecular structures of
adsorbed films. / . Colloid Interface Sci. 76:427-439.

179. Friberg, S. E., R. F. Goubran, and I. H. Kayali. 1990. Emulsions stability. In K. Larsson and
S. E. Friberg (eds.), Food Emulsions, 2nd edit., pp. 1-40. Marcel Dekker, New York.
180. Cohen Stuart, M. A., J. M. H. M. Scheutjens, and G. J. Fleer. 1984. Displacement of polymers. 1.
Theory. Segmental adsorption from polymer desorption in binary solvent. /. Colloid Interface Sci.
97:515-525.
181. Cohen Stuart, M. A., J. M. H.M. Scheutjens, and G. J. Fleere. 1984. Displacement of polymers.
2. Experiment. Determination of segmental adsorption energy of poly(vinylpyrrolidone) on silica.
/. Colloid Interface Sci. 97:526-535.
182. Cohen Stuart, M. A., J. M. H. M. Scheutjens, and G. J. Fleer. 1984. The role of the solvent in
polymer adsorption; displacement and solvency effects. In E. D. Goddard and B. Vincent (eds.),
Polymer Adsorption and Dispersion Stability, pp. 53-65. ACS Symp. Ser. 240, American Chemical
Society, Washington D.C.
183. MacRitchie, F. 1985. Desorption of proteins from the air/water interface. /. Colloid Interface Sci.
105:119-123.
184. Norde, W., F. MacRitchie, G. Nowicka, and J. Lyklema. 1986. Protein adsorption at solid-liquid
interface: reversibility and conformation aspects. /. Colloid Interface Sci. 112:447-452.
185. Jackson, R. H., and M. J. Pallansch. 1961. Influence of milk proteins on interfacial tension between
butter-oil and various aqueous phases. J. Agric. Food Chem. 9:424-427.
186. Mitchell, J., L. Irons, and G. J. Palmer. 1970. A study of the spread and adsorbed films of milk
proteins. Biochim. Biophys. Ada. 200:138-170.
187. Tomberg, E. 1978. The application of the drop volume technique to measurements of the adsorption
of proteins at interfaces. /. Colloid Interface Sci. 64:391-402.
188. Tomberg, E., and G. Lundh. 1981. A study of the surface enlargement in the drop volume method
and its relation to protein adsorption at A/W and O/W interfaces. / . Colloid Interface Sci.
79:76-84.
189. Britten, M., M. Boulet, and P. Paquin. 1986. Composition and interfacial properties of casein
micelles and their fractions. / . Dairy Sci. 53:573-584.
190. Mohanty, B., D. M. Mulvihill, and P. F. Fox. 1988. Emulsifying and foaming properties of acidic
caseins and sodium casemates. Food Chem. 28:17-30.
191. Mussel withe, P. R. 1966. The surface properties of an oil-water emulsion stabilized by mixtures
of caseins and gelatin. / . Colloid Interface Sci. 21:99-102.
192. Dickinson, E., A. Murray, B. S. Murray, and G. Stainsby. 1987. Properties of adsorbed layers in
emulsions containing a mixture of caseinate and gelatin. In E. Dickinson (ed.), Food Emulsions
and Foams, pp. 86-99. Royal Society of Chemistry, London.
193. Murray, E. K. 1987. Interfacial behavior of proteins mixture at air-water interface. In E. Dickinson
(ed.), Food Emulsions and Foams, pp. 170-187. Royal Society of Chemistry, London.
194. Dalgleish, D. D., and J. Leaver. 1991. The possible conformations of milk proteins adsorbed on
oil/water interfaces. J. Colloid Interface Sci. 141:288-294.
195. Leaver, J. and D. D. Dalgleish. 1990. The topography of bovine p-casein at an oil/water interface
as determined from the kinetics of trypsin-catalysed hydrolysis. Biochim. Biophys. Acta.
1041:217-222.
196. Paquin, P., M. Britten, M.-F. Laliberte", and M. Boulet. 1987. Interfacial properties of milk casein
proteins. In J. L. Brash and T. A. Horbett, (eds.), Physicochemical and Biochemical Studies, pp.
677-686. ACS Symp. Ser. 343, American Chemical Society, Washington D.C.

197. Laliberte", M.-F., M. Britten, and P. Paquin. 1988. Interfacial properties of sodium caseinatemonoglyceride mixture: combined effects of pH and surface areas ratios. Can. Inst. Food Sci.
Technol.J. 21:251-254.
198. Larichev, N. A., A. N. Gurov, and V. B. Tostogugov. 1983. Protein-polysaccharide complexes at
the interphase. 1. Characteristics of decan/water emulsions stabilized by complexes of bovine serum
albumin with dextran sulphate. Colloids Surf. 6:27-34.
199. Graham, D. E., and M. C. Phillips. 1979. Proteins at liquid interfaces. 1. Kinetics of adsorption
and surface denaturation. / . Colloid Interface Sci. 76:403-414.
200. Tornberg, E. 1978. The interfacial behaviour of three food proteins studied by the drop volume
technique. J. Sci. Food Agric. 29:762-776.
201. Ward, A. J. L, and L. H. Regan. 1980. Pendant drop studies of adsorbed films of bovine serum
albumin. / . Colloid Interface Sci. 78:389-394.
202. Games, G. L. 1966. Insoluble Monolayers at Liquid-Gaz Interfaces, pp. 30-128. Interscience, New
York.
203. Bergenstahl, B. A., and P. M. Claesson. 1990. Surfaces Forces. In K. Larsson and S. E. Friberg,
(eds.), Food Emulsions, 2nd edit. pp. 4196. Marcel Dekker, New York.
204. Mahanty, J., and B. W. Ninham. 1976. Dispersions Forces. Academic Press, London.
205. de Gennes, P. G. 1987. Polymers at an interface: a simplified view. Adv. Colloid Interface Sci.
27:189-209.
206. de Boer, J. H. 1936. The influence of van der Waals forces and primary bonds on binding energy,
strength and orientation, with special references to some artificial resins. Trans. Faraday Soc.
32:110-38.
207. Hamaker, H.C. 1937. The London-van der Waals attraction between spherical particles. Physica
4:1058-1072.
208. Vincent, B. 1973. The van der Waals attraction between colloidal particles having adsorbed layers.
2. Calculation of interaction curves. / . Colloid Interface Sci. 42:270-285.
209. Payens, T. A. J. 1978. On enzymatic clotting processes. 3. Flocculation rate constants of paracasein
and fibrin. Farad Disc. Chem. Soc. 65:164-174.
210. Israelachvili, J. N., and D. Tabor. 1972. Measurement of van der Waals dispersion forces in the
range 1.5 to 130 nm. Proc. Soc. London, Ser. A 331:19-38. Oxford.
211. Lifshitz, E. M. 1956. The theory of molecular attractive forces between solids. Sov. Phys. JEPT
2:73-83.
212. Dzyaloshinsskii, I. E., E. M. Lifshitz, and L. P. Pitaevskii 1961. The general theory of van der
Waals forces. Adv. Phys. 10:165-209.
213. Verwey, E. J. W., and J. Th. G. Overbeek. 1948. Theory of the Stability of Lyophobic Colloids.
Elsevier, Amsterdam.
214. Derjaguin, B. V., and L. D. Landau. 1941. Theory of the stability of strongly charged lyophobic
sols and of the adhesion of strongly charged particles in solutions of electrolytes. Acta Physicochim.
U.R.S.S. 14:633-662.
215. Dalgleish, D. G. 1989. Protein-stabilized emulsions and their properties. In T. M. Hardman (ed.),
Water and Food Quality, pp. 211-250. Elsevier Applied Science, New York.
216. Overbeek, J. Th. G. 1977. Recent developments in the understanding of colloid stability. / . Colloid
Interface Sci. 58:408-422.
217. Flory, P. 1953. Principles of Polymer Chemistry. Cornell University Press, Ithaca, New York.

218. de Gennes, P. G. 1984. Polymers solution near an interface. 1. Adsorption and depletion layers.
Macromolecules 14:1637-1644.
219. Scheutjens, J. M. H. M., and G. J. Fleer. 1980. Statistical theory of the adsorption of interacting
chain molecules. 2. Trains, loops, and tail distribution. J. Phys. Chem. 84:178-190
220. Scheutjens, J. M. H. M., and G. J. Fleer. 1985. Interaction between two adsorbed polymer layers.
Macromolecules 18:1882-1900.
221. Scheutjens, J. M. H. M., and G. J. Fleer. 1986. Interaction between adsorbed layers of macromolecules. 7. Colloid Interface Sci. 111:504-515.
222. Ninham, B. W., and V. A. Pargesian. 1970. Van der Waals interactions in multilayer systems.
J. Chem. Phys. 53:3398-3402.
223. Le Neveu, D. M., R. P. Rand, V. A. Pargesian, and D. Ginzell. 1977. Measurements and modification of forces between lecithin bilayers. Biophys. J. 18:209-230.
224. Pargesian, V. A., N. Fuller, and R. P. Rand, 1979. Measured work of deformation and repulsion
of lecithin bilayers. Proc. NatL Acad. Sci. USA 6:2750-2754.
225. Lis, L. J., M. McAlister, N. Fuller, R. P. Rand, and V. A. Pargesian. 1982. Interactions between
neutral phopholopid bilayer membranes. Biophys. J. 37:657-666.
226. Pashley, R. 1981. DLVO and hydration forces between mica surfaces in lithium, sodium, potassium,
and cesium electrolyte solutions: a correlation of double-layer and hydration forces with surfaces
cations exchange properties. J. Colloid Interface Sci. 83:531-546.
227. Marra, J. 1986. Direct measurements of attractive van der Waals and adhesion forces between
uncharged lipid bilayers in aqueous solution. / . Colloid Interface Sci. 109:11 -20.
228. Marra, J. and J. N. Israelachvili. 1985. Direct measurements of forces between phosphatidylcholine
and phosphatidylethanolamine bilayers in aqueous electrolyte solution. Biochemistry 24:46084618.
229. Walstra, P. 1983. Formation of emulsions. In P. Becher (ed.), Encyclopedia of Emulsion Technology. I. Basic Theory, pp. 57-127. Marcel Dekker, New York.
230. Napper, D. H. 1983. Polymeric Stabilization of Colloidal Dispersions. Academic Press, London.
231. Feigin, R. L, and D. Napper, 1980. Stabilization of colloids by free polymer. J. Colloid Interface
Sci. 74:567-571.
232. Feigin, R. L, and D. Napper. 1980. Depletion stabilization and depletion flocculation. / . Colloid
Interface Sci. 75:525-541.
233. Fleer, G. J., J. M. H. M. Scheutjens, and B. Vincent. 1984. In E. D. Goddard and B. Vincent (eds.),
Polymer Adsorption and Dispersion Stability, pp. 245-263. ACS Symp. Ser. 240, American Chemical Society, Washington D.C.
234. Walstra, P. 1987. Overview of emulsion and foam stability. In E. Dickinson, (ed.), Food Emulsions
and Foams, pp. 242-257. Royal Society of Chemistry, London.
235. Becher, P. 1961. Emulsions: Theory and Practice. Reinhold Pub. Corp. New York.
236. Dickinson, E. and G. Stainsby. 1988. Emulsion stability. In E. Dickinson, (ed.), Food Emulsions
and Foams, pp. 1 -44. Royal Society of Chemistry, London.
237. Davies, J. T. 1972. Turbulence Phenomena, pp. 273-363. Academic Press, London.
238. Basedow, A. M., and K. H. Ebert. 1977. Ultrasonic degradation of polymers in solution. Adv.
Polymer Sci. 22:83-148.

239. Cook, E. J., and A. P. Lagace, inventors. 1985. Apparatus for forming emulsions. US Patent
4,533,254.
240. Washington, C. 1987. Emulsion production by microfluidizer. Lab. Equip. Dig. 85:69-70.
241. Walstra, P., and H. Oortwijn. 1982. The membranes of recombined fat globules. 3. Mode of formation. Neth. Milk Dairy J. 36:103-113.
242. Dickinson, E. 1987. The structure and stability of emulsions. In J. M. V. Blanshard and J. R.
Mitchell (eds.), Food Structure: Its Creation and Evaluation, pp. 41-57. Butterworths, London.
243. Mulder, H., and P. Walstra. 1974. The Milk fat Globule: Emulsion Science as Applied to Milk
Products and Comparable Food, pp. 101-128, 139-160. C.A.B., Farnham Royal and Pudoc,
Wageningen.
244. Tadros, T. F., and B. Vincent. 1983. Emulsion Stability. In P. Becher (ed.), Encyclopedia of Emulsion Technology. L Basic Theory, pp. 129-285. Marcel Dekker, New York.
245. Dalgleish, D. G., and E. W. Robson. 1985. Centrifugal fractionation of homogenized milks.
J. Dairy Res. 52:539-546.
246. Walstra, P., and H. Oortwijn. 1975. Effect of globule size and concentration on creaming in pasteurized milk. Neth. Milk Dairy J. 29:263-278.
247. Barnea, E., and J. Mizrahi. 1973. A generalized approach to fluid dynamics of paniculate systems.
1. General correlation for fluidization and sedimentation in solid multiparticle system. Chem.
Eng.J. 5:171-189.
248. Ogden, L. V. 1973. The Homogenization-induced Clustering of Fat Globules in Cream and Model
Systems. Ph.D. Diss., Univ. Minnesota, St. Paul.
249. van de Ven, T. G. M., and S. G. Mason. 1976. The microrheology of colloidal dispersions. 4. Pairs
of interacting spheres. J. Colloid Interface Sci. 57:506-517.
250. Spielman, L. A. 1978. Hydrodynamic aspects of flocculation. In K. J. Ives (ed.), The Scientific
Basis of Flocculation, pp. 63-88. Sijthoff and Noordhoff, Alphenaaen den Rijn.
251. van Boekel, M. A. J. S. 1980. Influence of Fat Crystals in the Oil Phase on Stability of Oil-inWater Emulsions. Ph-D Diss., Univ. Wageningen.
252. van Boekel, M. A. J. S., and P. Walstra. 1981. Stability of oil-in-water emulsions with crystals in
the disperse phase. Colloids Surf. 3:109-118.
253. Friberg, S. E., P. O. Jansson, and E. Cederberg. 1976. Surfactant association structure and emulsion
stability. / . Colloid Interface Sci. 55:614-623.
254. Krog, N. J., T. H. Riisom, and K. Larsson. 1985. Applications in the Food Industry. 1. In P. Becher
(ed.), Encyclopedia of Emulsion Technology. 2. Applications, pp. 321-365. Marcel Dekker, New
York.
255. Darling, D. F., and R. J. Birkett. 1987. Food colloids in practice. In E. Dickinson (ed.), Food
Emulsions and Foams, pp. 1 -29. Royal Society of Chemistry, London.
256. Hailing, P. J. 1981. Protein-stabilized foams and emulsions. Crit. Rev. Food Sci. Nutr. 13:155-203.
257. Nielsen, L. E., A. Wall, and G. Adams. 1958. Coalescence of liquid drops at oil-water interfaces.
/ . Colloid Sci. 13:441-458.
258. Biswas, B. and D. A. Haydon. 1962. The coalescence of droplets stabilized by viscoelastic adsorbed
films. Kolloid-Z Z Polym. 185:31-38.
259. Aoki, H., M. Murata, and K. Hiramatsu, K. 1974. Urea denaturation of bovine serum albumin at
pH 9. Anal. Biochem. 59:146-157.

260. Pearce, K. N., and J. E. Kinsella. 1978. Emulsifying properties of proteins: evaluation of a turbidimetric technique. /. Agric. Food Chem. 26:716-723.
261. Waniska, R. D., J. K. Shetty, and J. E. Kinsella. 1981. Protein stabilized emulsions: effects of
modifications on the emulsifying activity of bovine serum albumin. J. Agric. Food Chem.
29:826-831.
262. Shimizu, M., T. Takahashi, S. Kaminogawa, and K. Yamauchi. 1983. Adsorption onto an oil surface
and emulsifying properties of bovine as 1-casein in relation to its molecular structure. J. Agric.
Food Chem. 31:1214-1218.
263. Mita, T., E. Iguchi, K. Yamada, S. Matsumoto, and D. Yonezawa. 1974. Dispersion state of proteinstabilized emulsions. 2. Effect of sodium chloride on stability of oil-in-water emulsions. / . Texture
Studies 5:89-96.
264. McWaiters, K. H., and M. R. Holmes. 1979. Influence of pH and salt concentration on nitrogen
solubility and emulsification properties of soy flours. / . Food Sci. 44:770-773.
265. Swift, C. E., C. Lockett, and A. J. Fryar. 1961. Comminuted meat emulsions: the capacity of meats
for emulsifying fat. Food Technol. 15:468-473.
266. Vuillemard, J.-C, S. Gauthier, J.-P. Richard, and P. Paquin. 1990. Development of a method for
the measurement of the maximum value of emulsifying capacity of milk proteins. Milchwissenschaft 45:572-575.
267. Reimerdes, E. H., P. Lorenzen, D. Precht, and H. A. Mehrens. 1986. The determination of the size
distribution of oil/water emulsions with regard to its stability. Lebensm. Wiss. u. Technol. 19
(l):82-86.
268. Buccheim, W., and P. Djemek. 1990. Milk and dairy-type emulsions. In K. Larsson and S. E.
Friberg (eds.), Food Emulsions, 2nd edit., pp. 203-246. Marcel Dekker, New York.
269. Klemaszewski, J. L., Z. Haque, and J. E. Kinsella. 1989. An electrode imaging system for determining droplet size and dynamic breakdown of protein stabilized emulsions. J. Food Sci. 54:440445.
270. Walstra, P., and H. Oortwijn. 1969. Estimating globule-size distribution of oil-in-water emulsions
by Coulter counter. / . Colloid Interface Sci. 29:424-431.
271. Walstra, P., H. Oortwijn, J. J. de Graaf. 1969. Studies on milk fat dispersion. 1. Methods for
determining globule-size distribution. Neth. Milk Dairy J. 23:12-36.
272. Walstra, P. 1968. Estimating globule-size distribution of oil-in-water emulsions by spectroturbidimetry. / . Colloid Interface Sci. 27:493-500.
273. Robin, O., and P. Paquin. 1991. Evaluation of the particle size distribution of fat globules in a milk
model emulsion by photon correlation spectroscopy. J. Dairy Sci. 74:2440-2447.
274. Inklaar, P. A., and J. Fortuin. 1969. Determining the emulsifying and emulsion stabilizing capacity
of protein meat additives. Food Technol. 23 (l):103-107.
275. Acton, J. C , and R. L. Saffle. 1970. Stability of oil-in-water emulsions. 1. Effects of surface tension,
level of oil, viscosity and type of meat protein. / . Food Sci. 35:852-855.
276. Yasumatsu, K., J. Toda, T. Wada, M. Misaki, and K. Iskii. 1972. Studies on the functional properties
of food grade soybean products. 3. Properties of heat coagulated gels from soybean products. Agric.
Biol. Chem. 36:537-543.
277. Tomberg, E., and A.-M. Hermansson. 1977. Functional characterization of protein stabilized emulsions: effect of processing. / . Food Sci. 42:468-472.
278. Cannella, M., G. Castriotta, A. Bernadi, and R. Boni. 1985. Functional properties of individual
sunflower albumin and globulin. Lebensm. Wiss. -u. Technol. 18:288-292.

279. Noguchi, S., and Y. Maeda. 1973. Dielectric properties of water-liquid paraffin emulsion systems
at the microwave frequency of 9.4 GHz. Agric. Biol. Chem. 37:1531-1535.
280. Kato, A., T. Fujishige, M. Matsudomi, and K. Kobayashi. 1985. Determination of emulsifying
properties of some proteins by conductivity measurements. / . Food Sci. 50:56-62.
281. Wang, J. C , and J. E. Kinsella. 1976. Functional properties of novel proteins: alfalfa leaf protein.
J. Food Sci. 41:286-292.
282. Goldsmith, P. 1988. Determination of Emulsion Stability by an Accelerated Sedimentation Conductivity Method. M. Sc. Diss., Laval University, Ste-Foy.
283. Latreille, B., and P. Paquin. 1990. A method of conductimetry to evaluate the emulsion stability
of long shelf life products. / . Food Sci. 55:1670-1672.
284. Void, R. D., and R. C. Groot. 1962. An ultracentrifugal method for the quantitative determination
of emulsion stability. J. Phys. Chem. 66:1969-1975.
285. Void, R. D., and R. C. Groot. 1964. Effect of electrolytes on the ultracentrifugal stability of emulsions./. Colloid Sci. 19:384-398.
286. Howes, A. M., A. R. Mackie, and M. M. Robbins. 1986. Technique to measure emulsion creaming
by velocity of ultrasound. / . Dispersion Sci. Technol. 7:231-243.
287. Britten, M., H. J. Giroux, and L. Lavoie. 1991. Phase separation in dairy products monitored by
optical densitometry. Milchwissenschaft 46:300-303.
288. Akers, R. J. (ed.). 1976. Foams. Academic Press, London.
289. Prins, A. 1988. Principles of foam stability. In E. Dickinson and G. Stainsby (eds.), Advances in
Food Emulsions and Foams, pp. 91-122. Elsevier Applied Science, London.
290. Anderson, M. B. E. Brooker, and N. C. Needs. 1987. The role of proteins in the stabilization/
destabilization of dairy foams. In E. Dickinson (ed.), Food Emulsions and Foams, pp. 100-109.
Royal Society of Chemistry, London.
291. Phillips, L. C , Z. Haque, and J. E. Kinsella. 1987. A method for the measurement of foam formation
and stability. / . Food Sci. 52:1074-1077.
292. Kato, A., A. Takahashi, N. Matsudomi, and K. Kobayashi. 1983. Determination of foaming properties by conductivity measurements. /. Food Sci. 48:62-65.
293. Graham, D. E. and M. C. Phillips. 1976. The conformation of proteins at the air interface and their
role in stabilizing foams. In R. J. Akers (ed.), Foams, pp. 237-255. Academic Press, London.
294. Townsend, A., and S. Nakai. 1983. Relationships between hydrophobicity and foaming characteristics of food proteins. J. Food Sci. 48:588-594.
295. Damodaran, S., and J. E. Kinsella. 1981. Interaction of carbonyls with soy protein: thermodynamic
effects. / . Agric. Food Chem. 29:1249-1253.
296. Malcolmson, L. C , M. R. McDaniel, and E. Hoehn. 1987. Flavor protein interactions in a formulated soup containing flavored soy protein. Can. Inst. Food Sci. Technol. J. 20:229-235.
297. O'Neill, T., and J. E. Kinsella. 1987. Binding of carbonyl flavors to /3-lactoglobulin: effects of
conformational and chemical modification. / . Agric. Food Chem. 35:770-774.
298. Damodaran, S., and J. E. Kinsella, 1980. Flavor protein interactions. Binding of carbonyls to bovine
serum albumin: thermodynamic and conformation effects. /. Agric. Food Chem. 28:567-571.
299. Solms, J., F. Osma-Ismael, and M. Beyeler. 1970. The interaction of volatiles with food components. Can. Inst. Food Sci. Technol. 6:10A-15A.
300. Peters, T. Jr. 1985. Serum albumin. Adv. Prot. Chem. 37:161-245.

301. Lubas, B., M. Soltysik-Raset, and I. Hesniewska. 1979. Proton nuclear magnetic resonance study
of the association of nonvalent and divalent alcohols with bovine serum albumin. Biochemistry
18:4943-4951.
302. Damodaran, S., and J. E. Kinsella. 1980. Stabilization of proteins by solvents. Effect of pH and
anions on the positive cooperative of 2-nonanone binding to bovine serum albumin. / . Biol. Chem.
255:8503-8508.
303. O'Neill, T., and J. E. Kinsella. 1988. Effect of heat treatment and modification of conformation
and flavor binding by /3-lactoglobulin. / . Food Sci. 53:906-909.
304. Wilson, L. A. 1986. Kinetics of flavor changes in foods. In M. R. Okos (ed.), Physical and Chemical
Properties of Food, pp. 382-407. American Society of Agricultural Engineers, St-Joseph.
305. Harper, W. J. 1976. Processing-induced changes. In W. J. Harper and C. W. Hall (eds.), Dairy
Technology and Engineering, pp. 539-596. AVI Publishing Co., Westport.
306. Morr, C. V. 1982. Functional properties of milk proteins and their uses and as food ingredients. In
P. Fox (ed.), Developments in Dairy Chemistry. I. Proteins, pp. 375-399. Applied Science Publishers, London.
307. Marshall, K. R., and W. J. Harper. 1988. Whey protein concentrates. IDF Bulletin 233:21-32.
308. Harper, W. J. 1992. Functional properties of whey protein concentrates and their relationship to
ultrafiltration. IDF Special Issue 9201:77-108.
309. Schmidt, R. H., V. S. Packard, and H. A. Morris. 1984. Effect of processing on whey protein
functionality. /. Dairy Sci. 67:2723-2733.
310. Kilara, A. and T. Y. Sharkasi. 1986. The effect of temperature on foot proteins and its implications
on functional properties. CRC Crit. Rev. Food Sci. Nutr. 23:323-395.
311. Kinsella, J. E., and D. M. Whitehead. 1989. Proteins in whey: chemical, physical and functional
properties. Adv. Food Nutr. Res. 33:343-438.
312. Singh, H. and P. F. Fox. 1989. Heat-induced changes in casein. IDF Bulletin 238:24-30.
313. Fox, P. F. 1982. Heat-induced coagulation of milk. In P. F. Fox (ed.), Developments in Dairy
Chemistry. I. Proteins, p. 189-228. Applied Science Publishers, London.
314. Dalgleish, D. 1989. Changes (physical and chemical) in milk salts (including interactions with milk
proteins). IDF Bulletin 238:31-34.
315. Rose, D. 1969. A proposed model of micelle structure in bovine milk. Dairy Sci. Abstr.
31:171-175.
316. Fox, P. F., and J. Guiney. 1973. Casein micelle structure. Succeptibility of various casein systems
to proteolysis. /. Dairy Res. 40:229-234.
317. Howat, G. R., and N. C. Wright. 1934. The heat coagulation of caseinogenen. 1. The role of
phosphorus cleavage. Biochem. J. 28:1336-1345.
318. Belec, J., and R. Jenness. 1962. Dephosphorylation of casein by heat-treatment. 1. In caseinate
solution. / . Dairy Sci. 45:12-19.
319. Hindle, E. J., and J. V. Wheelock. 1970. The release of peptides and glycopeptides by action of
heat on cow's milk. / . Dairy Res. 37:397-405.
320. Alais, C, N. Kiger, and P. Jolles. 1967. Action of heat on cow K-casein. Heat caseinoglycopeptides.
J. Dairy Sci. 50:1738-1743.
321. White, J. C. D., and D. T. Davies. 1966. The stability of milk proteins to heat. 3. Objective
measurement of heat stability of milk. / . Dairy Res. 33:93-102.

322. Josephson, R. V., E. L. Thomas, C. V. Morr, and S. T. Coulter. 1967. Relation of heat-induced
changes in protein-salt constituents to astringency in milk systems. /. Dairy Sci. 50:1376-1383.
323. Wilson, H. K., and E. O. Herreid. 1961. Photomicrographs of milk protein particles. /. Dairy Sci.
44:552-553.
324. Carroll, R. J., M. P. Thompson, and P. Melnychyn. 1971. Gelation of concentrated skimmilk.
Electron microscopy study. / . Dairy Sci. 54:1245-1252.
325. Riiegg, M. and B. Blanc. 1978. Influence of pasteurization and UHT processing upon the size
distribution of casein micelles in milk. Milchwissenschaft 33:364-366.
326. Creamer, L. K., G. P. Berry, and A. R. Matheson. 1978. The effect of pH on protein aggregation
in heated skim milk. N. Z. / . Dairy Sci. Technol. 13:9-15.
327. Fox, P. F., M. K. Harper, V. H. Holsinger, and M. J. Pallansch. 1967. Effects of high-heat treatment
on stability of calcium caseinate aggregates in milk. J. Dairy Sci. 50:443-450.
328. Morr, C. V. 1973. Protein aggregation in conventional and ultra high temperature heated skimmilk.
/ . Dairy Sci. 52:1174-1180.
329. Morr, C. V. 1975. Chemistry of milk proteins in food processing. J. Dairy Sci. 58:977-984.
330. Fox, P. F., and P. A. Morrissey. 1977. Reviews of the progress of dairy science: the heat stability
of milk. J. Dairy Res. 44:627-646.
331. Brown, R. J. 1988. Milk coagulation and protein denaturation. In N. P. Wong, R. Jenness,
M. Keeney, and E. H. Marth (eds.), Fundamentals of Dairy Chemistry, 3rd edit., pp. 583-608.
Van Nostrand Reinhold Co., New York.
332. Rose, D. 1961. Variations in the heat stability and composition of milk from individual cows during
lactation. J. Dairy Sci. 44:430-441.
333. Rose, D. 1961. Factors affecting the pH sensitivity of the heat stability of milk from individual
cows. J. Dairy Sci. 44:1405-1413.
334. Tessier, H. and D. Rose. 1964. Influence of /c-casein and /3-lactoglobulin on the heat stability of
skimmilk. / . Dairy ScL 47:1047-1051.
335. de Wit, J. N. and G. Klarenbeek. 1981. A differential scanning calorimetry study of the thermal
behavior of bovine /3-lactoglobulin at temperatures up to 16O0C. /. Dairy Res. 48:293-302.
336. Harwalkar, V. R. 1980. Measurement of thermal denaturation of /3-lactoglobulin at pH 2.5. J. Dairy
Sci. 63:1043-1051.
337. Harwalkar, V. R. 1980. Kinetics of thermal denaturation of /3-lactoglobulin at pH 2.5. J. Dairy Sci.
63:1052-1057.
338. Bemal, V., and P. Jelen. 1985. Effect of calcium binding on thermal denaturation of bovine
a-lactalbumin. J. Dairy Sci. 67:2452-2454.
339. Pearce, R. J. 1983. Thermal separation of /3-lactoglobulin and a-lactalbumin in bovine Cheddar
cheese whey. Aust. J. Dairy Technol. 38:144-149.
340. Pearce, R. J. 1987. Fractionation of whey proteins. IDF Bulletin 212:150-153.
341. Pierre, A. and J. Fauquant. 1986. Industrial process for production of purified proteins from whey.
Le Lait 66:405-419.
342. Nakai, S. and E. LiChan. 1985. Structure modification and functionality of whey proteins: quantitative structure-activity relationship approach. / . Dairy Sci. 68:2763-2772.
343. de Wit, J. N. 1990. Thermal stability and functionality of whey proteins. J. Dairy Sci. 73:36023612.

344. Mulvihill, D. M., and M. Donovan. 1987. Whey proteins and their thermal denaturation: a review.
Irish J. Food Sci. Technol 11:43-75.
345. Morr, C. V. 1987. Effect of HTST pasteurization of milk, cheese whey, and cheese whey UF
retentate upon the composition, physicochemical, and functional properties of whey protein concentrates. / . Food Sci. 52:312-317.
346. Mangino, M. E., L. M. Huffmann, and G. O. Regester. 1988. Changes in hydrophobicity and
functionality of whey during processing of whey protein concentrates. /. Food Sci. 53:16841686,
1693.
347. Novak, A. 1992. Milk protein concentrate. IDF Special Issue 9201:51-66.
348. Jelen, P. 1992. Pressure-driven membrane processes: principles and definitions. IDF Special Issue
9201.7-14.
349. Cheryan, M. 1986. Ultrafiltration Handbook. Technomics Publishers Co., Lancaster.
350. Rousseau, R. W. (ed.). 1987. Handbook of Separation Process Technology. John Wiley & Sons,
New York.
351. Schweitzer, P. A. (ed.). 1988. Handbook of Separation Techniques for Chemical Engineers, 2nd
edit. McGraw-Hill, New York.
352. Porter, M. C. (ed.). 1990. Handbook of Industrial Membrane Technology. Noyes Publishers, Park
Ridge.
353. Olesen, N., and F. Jensen. 1989. Microfiltration: the influence of operating parameters on the
process. Milchwissenschaft 44:476-479.
354. Pedersen, P. J. 1992. Microfiltration for the reduction of bacteria in milk and brine. IDF Special
Issue 9201:33-50.
355. Pearce, R. J., S. C. Marshall, and J. A. Dunkerley. 1992. Reduction of lipids in whey protein
concentrates by microfiltration: effect on functional properties. IDF Special Issue 9201:118-129.
356. Mohr, C. M., D. E. Engelgau, S. A. Leeper, and B. L. Charboneau. 1989. Membrane Applications
and Research in Food Processing. Noyes Data Corporation, Park Ridge.
357. de Boer, R., J. and Hiddink. 1980. Membrane processes in the dairy industry. Desalination
35:169-192.
358. Kosikowski, F. V. 1986. Membrane separation in food processing. In W. C. McGregor (ed.),
Membrane Separations in Biotechnology, pp. 201-254. Marcel Dekker, New York.
359. Gregory, A. G. Desalination of sweet-type whey salt drippings for whey solids recovery. IDF
Bulletin 212:38-49.
360. Roy, D., J. Francoeur, L. Blanchette, and D. Minier. 1990. Demineralization d'un lactose*rum
de'prote'ine' par ultra-osmose. Brief Comm. & Abstr. Posters. Proc. XXII International Dairy Congress, p. 485, Montreal.
361. Jelen, P. 1978. Physico-chemical properties of milk and whey in membrane processing. / . Dairy
Sci. 62:1343-1351.
362. Kelly, P. M., B. S. Horton, and H. Burling. 1992. Partial demineralization of whey by nanofiltration.
IDF Special Issue 9201:130-140.
363. Puham, Z. 1992. Standardization of milk protein content by membrane processes for product manufacture. IDF Special Issue 9201:23-32.
364. Maubois, J.-L., and G. Mocquot. 1971. Preparation du fromage a partir de pre*-fromage liquide
obtenu par ultracentrifugation du lait. Le Lait 51:495-534.

365. Mahaut, M., J.-L. Maubois, A. Zink, R. Pannetier, and R. Veyre. 1982. Elements de fabrication de
fromage frais par ultrafiltration sur membrane de coagulum de lait. Technique Laitiire 961:9-13.
366. Emstrom, C. A., and S. K. Anis. 1986. Properties of products from ultrafiltered whole milk. Proc.
IDF Seminar, pp. 21-30. Atlanta.
367. Lelievre, J. and R. C. Lawrence. 1988. Manufacture of cheese from milk concentrated by ultrafiltration. J. Dairy Res. 55:465-478.
368. Lawrence, R. C. 1989. The use of ultrafiltration technology in cheesemaking. IDF Bulletin
240:1-15.
369. Pedersen, P. J. and N. Ottosen. 1992. Manufacture of fresh cheese by ultrafiltration. IDF Special
Issue 9201:67-76.
370. de Boer, R., and J. P. J. M. Koenraads. 1992. Incorporation of liquid ultrafiltrationwhey retentates
in dairy desserts and yogurts. IDF Special Issue 9201:109-117.
371. Green, M. L., K. J. Scott, M. Anderson, M. C. A. Griffin, and F. A. Glover. 1984. Chemical
characterization of milk concentrated by ultrafiltration. / . Dairy Res. 51:267-278.
372. Srilaorkul, S., L. Ozimek, B. Ooraikul, D. Hadziyev, F. Wolfe. 1991. Effect of ultrafiltration of
skim milk on casein micelle size distribution in retentate. / . Dairy Sci. 74:50-57.
373. Schmidt, D. G. 1980. Colloidal aspect of casein. Neth. Milk Dairy J. 34:42-64.
374. Hallstrom, M., and P. Djemek. 1988. Rheological properties of ultrafiltered skim milk. 1. Effects
of pH, temperature and heat pretreatment. Milchwissenschaft 43:31-34.
375. Mistry, V. V. 1989. Thermal inactivation characteristics of alkaline phosphatase in ultrafiltered
milk. /. Dairy ScL 72:1112-1117.
376. Renner, E. and M. H. Abd El-Salam. 1991. Application of Ultrafiltration in the Dairy Industry.
Elsevier Applied Science, London.
377. Korolczuk, J., J.-L. Maubois, and J. Fauquant. 1986. In Milk, The Vital Force, pp. 123-153. XXII
Int. Dairy Congress, The Hague.
378. Mortensen, B. K. 1985. Recent developments in the utilization of milk proteins in dairy products.
Milk Proteins 1984. In Int. Congress Milk Proteins, pp. 109-119. Luxembourg.
379. de Wit, J. N., G. Klarenbeek, and E. Hontelez-Backx. 1983. Evaluation of functional properties of
whey protein concentrates and whey protein isolates. 1. Isolation and characterization. Neth. Milk
Dairy J. 37:37-49.
380. de Wit, J. N., G. Klarenbeek, and M. Adamse. 1986. Evaluation of functional properties of whey
protein concentrates and whey protein isolates. 2. Effects of processing, history, and composition.
Neth. Milk Dairy J. 40:41-56.
381. de Wit, J. N., E. Hontelez-Backx, and M. Adamse. 1988. Evaluation of functional properties of
whey protein concentrates and whey protein isolates. 3. Functional properties in aqueous solution.
Neth. Milk Dairy J. 42:155-172.
382. Hugunin, A. G. 1987. Applications of UF whey proteins: developing new markets. IDF Bulletin
212:134-144.
383. Morr, C. V. 1992. Improving the texture and functionality of whey protein concentrate. Food
Technol. 46(1):110-113.
384. Morr, C. V., and E. A. Foegeding. 1990. Composition and functionality of commercial whey and
milk protein concentrates and isolated: a status report. Food Technol. 44(4): 100-112.
385. de Wit, J. N., G. Klarenbeek, and R. de Boer. 1978. A simple method for the clarification of whey.
Int. Dairy Congress; E. 919-920.

386. Merin, V., S. Gordin, and G. B. Tanny. 1983. Microfiltration of sweet cheese whey. N. Z. /. Dairy
Sci. Technol. 18:153-160.
387. Piot, M., J. C. Vachot, M. Veaux, J.-L. Maubois, and G. E. Brinkman. 1987. Ecre"mage et e*puration
bacte"rienne du lait entier cru par microfiltration sur membrane en flux tangentiel. Technique Laitiere
& Marketing 1016:42-26.
388. Maubois, J.-L., G. Brule", and P. Gourdon. 1981. Ultrafiltration of whey: optimization of technology
and utilization of permeate. Technique Laitiere 952:29-33.
389. Fauquant, J., A. Pierre, and G. Brule. 1985. Clarification of acid casein whey. Technique Laitiere
& Marketing 1003:37-39.
390. Harris, J. L., M. A. Pecar, and R. J. Pearce. 1989. Effect of the processing equipment on protein
functionality in the concentration of cheese whey by ultrafiltration. Aust. J. Dairy Technol. 78-81.
391. Whitaker, J. R. 1977. Enzymatic modification of proteins applicable to foods. In R. E. Feeney, and
J. R. Whitaker (eds.), Food proteins: Improvement Through Chemical and Enzymatic Modification,
pp. 95-155. Adv. Chem. Ser. 160. ACS, Washington, D.C.
392. Woo, S. L. and T. Richardson. 1983. Functional properties of phosphorylated /3-lactoglobulin.
J. Dairy Sci. 66:984-988.
393. Morr, C. V. 1984. Production and use of milk proteins in food. Food Technol. 38:39-48.
394. Kester, J. J. and T. Richardson. 1984. Modification of whey proteins to improve functionality.
/. Dairy Sci. 67:2757-2774.
395. Arai, S., and M. Watanabe. 1988. Emulsifying and foaming properties of enzymatically modified
proteins. In E. Dickinson and G. Stainsby (eds.), Advances in Food Emulsions and Foams, pp.
163-188. Elsevier Applied Science, London.
396. Turgeon, S. 1991. Amelioration des Proprietes Interfaciales et Emulsifiantes dun Concentre de
Lactoserum par Traitement Enzymatique etlou Thermique. Ph.D. Diss., Universit6 Laval.
397. Kinsella, J. E. and D. M. Whitehead. 1988. Emulsifying and foaming properties of chemically
modified proteins. In E. Dickinson and G. Stainsby (eds.), Advances in Food Emulsions and Foams,
pp. 189-220. Elsevier Applied Science, London.
398. Meisel, H. and H. Frister. 1989. Chemical characterization of biocative peptides from in vivo digests
of casein. J. Dairy Res. 56:343-349.
399. Fiat, A.-M., S. Levy-Toledano, J. P. Caen, and P. Jolles. 1989. Biologically active peptides of
casein and lactotransferrin implicated in platelet function. / . Dairy Res. 56:351-355.
400. Migliore-Samour, D., F. Floc'h, and P. Jolles. 1989. Biologically active casein implicated in immunomodulation. /. Dairy Res. 56:357-362.
401. Chiba, H., F. Tani, and M. Yoshikawa. 1989. Opioid antagonist peptides derived from /c-casein.
/ . Dairy Res. 56:363-366.
402. Nabet, P., F. Belleville-Nabet, and G. Linden. 1991. Les peptides a activite" physiologiques. 1.
Facteurs de croissance dans Ie lait et Ie lactoserum. Le Lait 71:225-239.
403. Coste, M., and D. Tome". 1991. Les peptides a activite* physiologiques. 2. Activite morphinomime"trique et immunostimulante. Le Lait 71:241-247.
404. Maubois, J.-L. 1988. Nouvelles utilisations des ingredients laitiers. In Nouvelles utilisations du
lait. Colloque STELA, pp. 149-184. Quebec.
405. Sanderson, W. B. 1988. Utilisations des ingredients laitiers dans les charcuteries. In Nouvelles
utilisations du lait. Colloque STELA, pp. 1-12. Quebec.