INTERNATIONAL JOURNAL OF FOOD PROPERTIES, 5(2), 419434 (2002)

RHEOLOGICAL AND PHYSICOCHEMICAL

PROPERTIES OF DERIVATIZED WHEY
PROTEIN CONCENTRATE POWDERS

J. J. Resch and C. R. Daubert*

Department of Food Science, North Carolina State University,

Raleigh, NC 27695-7624

ABSTRACT

The gelling ability of whey proteins provides important textural and

water holding properties in many foods. However, because many pro-
ducts cannot be heated to the temperature needed for thermal gelation
of whey proteins, cold-set gelation of whey proteins could be very
advantageous to the food industry. A derivatization procedure for the
production of a cold gelling whey protein isolate (WPI) consisting of
protein hydration, pH adjustment, thermal gelation, freeze drying, and
milling was applied to three commercial whey protein concentrates
(WPC). The resulting derivatized WPC powders were reconstituted in
water and evaluated through a range of rheological and physical property
studies. The eects of temperature, concentration, and shear on viscosity
as well as water holding capacity and intrinsic viscosity were assessed.
Although the composition of the starting materials inuenced the func-
tionality of the nal derivatized powders, all samples exhibited a dramatic
increase in thickening and water holding ability. All samples were able to
form cold-set weak gel structures suitable for contributing viscosity and
texture to a wide range of food systems.

*Corresponding author. Christopher R. Daubert, North Carolina State University, Depart-

ment of Food Science, NCSU Box 7624, Raleigh, NC 27695-7624 USA. Fax: (919) 515-7124;
E-mail: chris_daubert@ncsu.edu

419

Copyright # 2002 by Marcel Dekker, Inc. www.dekker.com

420 RESCH AND DAUBERT

INTRODUCTION

The unique functional and nutritional properties of whey proteins make

them useful food ingredients for a wide array of applications. The nutritional
quality of whey proteins is high, evidenced by a higher biological value and
a higher essential amino acid score than egg, milk, and soy proteins.[1] The
emulsication, foaming, and gelation properties of whey protein are the basis
of its wide use as a functional ingredient in foods.[2] In particular, the ability
of whey proteins to form gels capable of holding water, lipids, and other
components while providing textural properties is very important to the
consumer acceptability of many foods such as processed meat, dairy, and
bakery products.[3]
Heat-induced whey protein gels have been extensively studied and
reported.[476] However, in many food applications, heating the product to the
high temperatures necessary for heat-induced gelation is undesirable or
impossible. Therefore, the induction of gelation at ambient temperatures,
termed cold-set gelation, greatly extends the possible utility of whey proteins.
Successful cold-set gelation of whey proteins has been described by several
authors.[7710] These cold-set gels were prepared by rst heating whey protein
solutions to achieve unfolding and aggregation, followed by quickly cooling
the solutions to room temperature, and then producing gelation with the
addition of NaCl or CaCl2.
Cold-gelling whey proteins in a dried form have also been documented.
Thomsen[11] described a commercially available modied whey protein con-
centrate powder with potential applications in foods such as surimi, com-
minuted meats, dressings, and bakery products. This whey protein texturizer
is produced by heat treatment during homogenization of a whey protein
concentrate at slightly alkaline pH followed by immediate drying and will gel
upon reconstitution in a salt solution.[12] Although the gelling ability of whey
proteins plays an important function in many foods, this property can also
limit the application in foods where weak or non-gelling characteristics are
needed such as beverages, baby-formula, and salad dressings.[13] Hudson
et al.[14] developed a derivatized whey protein isolate capable of forming cold-
set weak gel structures without the addition of salts or heat. This modica-
tion was accomplished through a process consisting of acid hydrolysis,
thermal gelation, freezing, freeze-drying, and milling.
The performance of thickening and gelling ingredients is often evaluated
with rheological techniques. For viscosifying agents, it is important to not
only examine the level of viscosity achieved, but the dependence of this
viscosity on conditions that may be commonly experienced by the system.
For this reason, thickened systems are often subjected to rotational viscosity
measurements over a range of shear rates, concentrations, and temperatures
and when applicable, rheological models are developed to describe and
predict the ow behavior. Dilute solution viscometry is another valuable tool
DERIVATIZED WHEY PROTEIN CONCENTRATE POWDERS 421

that is employed to probe the molecular properties of the thickening agent.

Measurement of dilute solutions with a capillary viscometer can be done to
determine the intrinsic viscosity. Because the intrinsic viscosity is related to
the hydrodynamic volume occupied by the molecule, the molecular weight,
and the radius of gyration, inferences about important molecular char-
acteristics of the food macromolecule can be made.[15] Foods that achieve
functionality by formation of a viscoelastic network are often investigated
with small amplitude oscillatory testing. The response of a sample subjected
to harmonically varying stress or strain is used to construct a mechanical
spectrum that can provide information about the viscous and elastic nature
of the sample behavior over a range of frequencies.[16]
Because extensive processing is required to produce a whey protein
isolate with a protein content greater than 90%, commercial applications
may be cost prohibitive. Therefore, the objectives of this study were to apply
the technique of Hudson et al.[14] to several whey protein concentrates,
creating more economical cold-set thickening agents, and to characterize the
functionality and properties of these ingredients over a wide range of
environmental conditions. Solutions of commercial WPC were manipulated
to produce heat-induced gels, which upon further processing rendered deri-
vatized protein thickeners, the rheological and physical properties of which
are assessed herein.

MATERIALS

Three commercial whey protein concentrate powders were obtained

from Davisco Foods International, Inc. (Le Sueur, MN). The compositions
of the three WPC samples (lot numbers LE 001-7-685, LE 036-9-280, and LE
012-9-665) are compiled in Table 1. Protein contents were determined by
micro-Kjeldahl,[17] mineral composition was determined by inductively cou-
pled plasma atomic emission spectroscopy, and lipid and lactose contents

Table 1. Composition of Commercial Whey Protein Concentrate Samples

Proteina Lactoseb Lipidb Cac Nac Mgc Pc Kc

Sample (%) (%) (%) (%) (%) (%) (%) (%)

WPC86 86.5 2.1 2.9 0.48 0.16 0.00 0.14 0.26

WPC74 74.3 6.8 7.0 0.74 0.16 0.08 0.52 0.55
WPC64 63.6 18.5 5.4 0.75 0.23 0.10 0.57 1.03

a
Determined by micro-Kjeldahl (N66.38).
b
Provided by Davisco Foods International, Inc.
c
Determined by inductively coupled plasma atomic emission spectroscopy.
422 RESCH AND DAUBERT

were provided by the supplier. All chemicals were purchased from Fisher
Scientic Company (Springeld, NJ).

METHODS
Preparation of Protein Dispersions and Gels

Solutions were prepared at 12% w=v protein from each WPC powder in
deionized (DI) water. Each solution was gently stirred for 1 h at room tem-
perature, and pH was adjusted to 3.35 with 6 N HCl or 6 N NaOH. WPC gels
were produced by placing the solutions in aluminum freeze-drier pans
(13.5 cm613.5 cm64.8 cm) and heating in a water bath at 80
C according to
the procedure of Hudson et al.[14] for 3 h.

Derivatized Whey Protein Concentrate (dWPC) Powder Production

After thermal gelation, gels were placed at 5
C for at least 24 h.

Frozen gels were dried in a 10-145-MR-TR Mechanically Refrigerated
Freeze-Mobile freeze dryer with tray drying chamber (Virtis Research
Equipment, Gardiner, NY). The dryer operated at a condenser temperature
of 55
C and a pressure of 15 microns while the shelf temperature was
slowly increased from 30
C to 20
C over a drying period of about 96 h.
Gels were dried until moisture content was below 5% and removed from the
freeze drier pans. Dried gels were crushed by hand, then ground with a ZM-1
Brinkman Centrifugal Grinding Mill equipped with a 24-tooth stainless-steel
rotor (Brinkman Instruments, Inc., Westbury, NY) at 10,000 rpm for 60 sec.
Protein gel powders were stored at room temperature in airtight bags inside a
desiccator until testing.

Rheological Analyses

The protein powders were reconstituted in DI water for rheological

testing. Shear rate ramps, temperature ramps, and frequency sweeps were
conducted on a StressTech Controlled Stress Rheometer (ReoLogica
Instruments AB, Lund, Sweden) using a concentric cylinder geometry
(CC25). All rheological measurements were performed in triplicate.

Shear Rate Ramps

The derivatized protein samples were reconstituted at 8% w=w protein

in DI water and allowed to hydrate for 24 h. All samples were exposed to a
30 sec pre-shear at 15 s1. Apparent viscosity and shear rates were recorded
as shear stresses were ramped from 0.05 to 25 Pa. Fresh samples were sheared
at temperatures of 25, 50 and 75
C.
DERIVATIZED WHEY PROTEIN CONCENTRATE POWDERS 423

Flow behavior was described by the cross model

Z0  Z1
Z Z1 1
1 C_gm

where Z apparent viscosity, Z0 zero shear viscosity, Z 1 innite shear

viscosity, C a time constant related to the relaxation time of the polymer in
solution, g_ shear rate, and m a dimensionless exponent. In food disper-
sions, the magnitude of Z 1 is usually very low and dicult to determine
experimentally, and is therefore often neglected (15). Accordingly, Z 1 was
assumed to be zero for the purposes of the shear rate ramps conducted at
concentrations of 8% protein.
To investigate the protein concentration eects, the dWPC86 sample
was also prepared at concentrations of 5.5, 6.0, 6.5, 7.0 and 7.5% w=w
protein. These samples were allowed to hydrate for 24 h, subjected to the
same shear rate ramps at 25
C, and described by the same Cross model
methodology. For the solutions with concentrations greater than 7.0%,
there was no evidence of an innite viscosity plateau, so Z 1 was again
assumed to be zero for the purposes of modeling data over the experimental
shear rate range. The solutions with concentrations less than or equal to
6.5% exhibited innite viscosity plateaus, therefore Z 1 was incorporated
into the model.

Temperature Ramps

Solutions of 8.6% w=w protein were sheared at a constant shear rate of

50 s  1 while temperatures were ramped from 10 to 90
C and back to 10
C
for 2400 s while apparent viscosity was noted. A solvent trap was used, and a
thin layer of mineral oil was applied to the surface of the sample to prevent
moisture loss during the experiment.

Frequency Sweeps

The derivatized samples were prepared in DI water to contain 10% w=w

protein and allowed to hydrate for 24 h. Storage and loss moduli (G0 and G00 )
were recorded while stress amplitude was held at 0.7 Pa and frequency was
increased from 0.01 to 40.0 Hz at 25
C. All frequency sweeps were performed
within the identied linear viscoelastic region for each material tested. The
frequency dependence of G0 and G00 was modeled with the power law para-
meters, a, b, c, and d, as described by Eqs. (2) and (3).

G0 aob 2

G00 cod 3
424 RESCH AND DAUBERT

Intrinsic Viscosity

Intrinsic viscosity was measured using Cannon-Fenske capillary visc-

ometers (Cannon Instrument Co., State College, PA) immersed in a constant-
temperature bath at 25  0.1
C. In accordance with the recommended
viscosity ranges for each instrument, the derivatized protein samples were
measured with a size 50 viscometer, and the commercial WPC samples were
assessed with a size 25 viscometer. Stock solutions for each sample were
prepared with DI water to contain 5 mg protein=mL. The stock solutions
were diluted with DI water to produce a series of ve concentrations between
0.5 and 5.0 mg protein=mL. The specic viscosity was calculated by

Zsp t  to =to 4

where Zsp specic viscosity, t eux time of protein solution, and

to eux time of the solvent, water. Based on the Huggins equation

Zsp =c Z kZ2 c 5

where c the protein concentration, the intrinsic viscosity, [Z], was deter-
mined from the extrapolation of Zsp=c vs. c.

Water Holding Capacity

The water holding capacity was determined by a modication of the

centrifugation procedure of Fleming et al.[18] in which 7% w=w protein
solutions were prepared in DI water and centrifuged at 2500 rpm for 15 min.
Upon removal from the centrifuge, the supernatant was carefully decanted
and the water held per gram of protein was calculated by weight dierence.

Electrophoresis

The approximate contents of the individual whey proteins in each

commercial WPC sample were analyzed by sodium dodecyl sulfate-poly-
acrylamide gel electrophoresis (SDS-PAGE) with a Novex Midget electro-
phoresis unit (Novex, Novel Experiment Technology, San Diego, CA). A
Tris-Tricine gel with dithiothreitol (DTT) serving as the denaturant was
utilized. A 0.1% protein solution was prepared for each sample by 1:1
dilution of a 0.2% protein solution with sample buer. A 25 mL aliquot of
the 0.1% protein sample was injected into each well of the 10720% gradient
polyacrylamide gel (Novex, Novel Experiment Technology, San Diego, CA).
The gel was stained with a colloidal Coomassie solution (Pierce Chemical
Company, Rockford, IL), and the protein bands were quantied with a
DERIVATIZED WHEY PROTEIN CONCENTRATE POWDERS 425

Molecular Dynamics personal densitometer (Molecular Dynamics, Sunny-

vale, CA).

RESULTS AND DISCUSSION

Rheological Analyses
Shear Rate Ramps

Shear rate ramps were performed at 25, 50, and 75
C to investigate the
shear and temperature eects on the apparent viscosity of the three deriva-
tized whey protein concentrate (dWPC) powders. Table 2 summarizes the
Cross model parameters as well as the apparent viscosities at shear rates of 10
and 50 s1 (Z10 and Z50) for each of the shear rate ramps. The dWPC86
sample produced the greatest viscosity at each temperature. At the three
temperatures evaluated, the dWPC74 and dWPC64 samples exhibited similar
viscosities that were signicantly lower than the dWPC86 sample. All sam-
ples showed a decrease in viscosity from 25 to 50
C due to the increased
thermal energy of the system. A viscosity increase was observed in each
sample from 50 to 75
C, with the dWPC64 sample exhibiting the greatest
viscosity change. This increase in viscosity can be attributed to additional
protein unfolding and the formation of physical crosslinks. Hudson et al.[14]
demonstrated that an increased concentration of salts had a stabilizing eect
on the protein, resulting in a greater percentage of native protein remaining
after a thermal treatment at pH values near 3.35. Harwalkar and Kalab[19]
also reported a protective eect from denaturation when ionic strength was
increased from 0 to 0.1. The protein solutions used in this research were
within the ionic strength range of 0 to 0.1. Therefore, the dWPC64 sample,

Table 2. Cross Model Parameters of 8% (w=w Protein) Derivatized Whey Protein Con-
centrate Solutions at 25, 50, and 75
C

Temperature Z0a Ca ma Z10 Z50 g_

Sample (
C) (Pa s) (sm) () (Pa s) (Pa s) (s1)

dWPC86 25 0.891  0.050 0.024  0.006 1.087  0.064 0.692 0.334 27200
50 0.662  0.072 0.015  0.002 1.069  0.018 0.564 0.336 27200
75 0.874  0.184 0.219  0.088 0.752  0.122 0.399 0.180 27200
dWPC74 25 0.255  0.112 0.102  0.051 0.804  0.095 0.162 0.081 27200
50 0.149  0.037 0.051  0.008 0.863  0.031 0.108 0.060 27200
75 0.360  0.029 0.087  0.040 0.855  0.059 0.225 0.109 27200
dWPC64 25 0.236  0.020 0.030  0.018 0.947  0.032 0.186 0.107 27200
50 0.199  0.024 0.008  0.002 1.068  0.030 0.182 0.129 27200
75 0.534  0.146 0.050  0.017 0.934  0.048 0.372 0.183 27200

a
Mean  standard deviation.
426 RESCH AND DAUBERT

which was derived from the WPC sample containing the highest level of salts
(Table 1), likely had a greater amount of undenatured protein available to
unfold and produce the greatest increase in solution viscosity during tem-
perature studies.
The dWPC86 sample was prepared at a range of concentrations and
subjected to shear rate ramps to examine the concentration eects. Solutions
of less than 5% protein were very thin and would oer little viscosifying
power. Solutions with concentrations from 5.5 to 8.0% exhibited steadily
increasing thickening ability (Table 3). These solutions manifested typical
rheological characteristics of a thickened uid: a zero shear viscosity plateau
at low shear rates, a shear-thinning regime, and an innite shear plateau at
high shear rates for the thinner solutions (Fig. 1).

Temperature Ramps

Subjecting the dWPC86 sample to a temperature ramp under a shear

rate of 50 s  1 produced little variation in apparent viscosity (Fig. 2). As the
temperature was increased from 10 to 60
C, the viscosity gradually decreased
from 1.35 to 0.52 Pa s. From 60 to 90
C, there was a subsequent 0.10 Pa s
increase in viscosity, possibly attributed to additional denaturation of native
or renatured proteins.[14] This protein unfolding and increased hydrophobic
interactions were responsible for the higher viscosity during the 90 to 10
C
temperature ramp. The dWPC74 and dWPC64 samples also displayed a
similar temperature dependency over this range.

Frequency Sweeps

Small amplitude oscillatory rheology was used to determine the

mechanical spectrum of each dWPC powder. The power law parameters

Table 3. Cross Model Parameters for dWPC86 Solutions with Concentrations Between 5.5
and 8.0% (w=w Protein) at 25
C

Concentration Z0a Ca ma Z1 Z10 Z50 g_

(% Protein) (Pa s) (sm)  (Pa s) (Pa s) (Pa s) (s  1)

8.0 0.891  0.050 0.024  0.006 1.087  0.064 0 0.692 0.334 27200
7.5 0.359  0.135 0.144  0.079 0.795  0.070 0 0.194 0.091 27200
7.0 0.188  0.029 0.258  0.067 0.671  0.045 0 0.086 0.065 27200
6.5 0.077  0.047 0.003  0.004 1.500  0.310 0.021 0.072 0.055 27200
6.0 0.053  0.005 0.000  0.000 1.749  0.126 0.017 0.052 0.048 27200
5.5 0.024  0.002 0.000  0.000 1.623  0.080 0.010 0.024 0.022 27200

Mean  standard deviation.

a
DERIVATIZED WHEY PROTEIN CONCENTRATE POWDERS 427

Figure 1. Shear rate ramps for dWPC86 solutions with concentrations between 5.5 and 8.0%
(w=w protein) at 25
C.

relating the storage modulus (G0 ) and loss modulus (G00 ) to frequency for
each sample are presented in Table 4. The power law coecients, a and c,
represent the magnitude of G0 and G00 respectively at a given frequency. The
dWPC86 sample had the greatest values of a and c, while the dWPC74 and

Figure 2. Apparent viscosity of a 8.6% (w=w protein) dWPC86 solution as temperature is

ramped from 10 to 90
C and back to 10
C at a constant shear rate of 50 s1.
428 RESCH AND DAUBERT

Table 4. Viscoelastic Power Law Constants for 10% (w=w Protein) dWPC Solutions at 25
C

aa ba ca da o
Sample (Pa Hzb) () (Pa Hzd) () (Hz)

dWPC86 1159.6  149.4 0.085  0.001 361.6  74.5 0.265  0.018 0.01720
dWPC74 692.8  169.8 0.108  0.003 216.0  63.9 0.237  0.014 0.01720
dWPC64 605.5  46.9 0.127  0.003 200.8  19.3 0.235  0.008 0.01720

Mean  standard deviation.

a

dWPC64 samples had lower, but similar magnitudes for their moduli. In all
three samples, the magnitude of a was much greater than c. The existence of
such a pronounced region where the storage modulus is considerably greater
than the loss modulus, as represented graphically in Fig. 3, indicates gel
behavior.[20] The power law exponents b and d represent the slope of the
relationships between the moduli and frequency. An exponent value of zero
would indicate the modulus is not changing with frequency, a characteristic
of a fully cured gel. The dWPC86 sample exhibited the lowest values of b and
d, while the dWPC74 and dWPC64 samples had similar, higher slope values.
The dependence of G0 and G00 on frequency illustrates that the derivatized
WPC samples form weak gels under these conditions.

Figure 3. Storage and loss moduli for 10% (w=w protein) derivatized whey protein con-
centrate samples during a frequency seep from 0.01 to 20 Hz at 25
C.
DERIVATIZED WHEY PROTEIN CONCENTRATE POWDERS 429

Intrinsic Viscosity

Intrinsic viscosity, [Z], is a characteristic property of a polymer in a

specic solvent that measures the hydrodynamic volume occupied by a
polymer molecule. The largest intrinsic viscosity was produced by dWPC86
(Table 5), suggesting the derivatization process produced particles capable of
occupying the greatest hydrodynamic volume once hydrated in solution. The
dWPC74 and dWPC64 samples displayed intrinsic viscosities of 56.4 and
49.5 mL=g. This response is indicative of smaller and=or more spherical
particles than those of dWPC86. The intrinsic viscosities of the derivatized
samples were much greater than those of the commercial WPC samples from
which they were derived. The commercial WPC samples had very low
intrinsic viscosities ranging from 678 mL=g. These values agree with the
ndings of Vardhanabhuti and Foegeding[21] who reported a value of
5.0 mL=g for a native whey protein isolate sample. The plots of Zsp=c vs. c for
each dWPC powder had negative slopes (Fig. 4). A possible explanation is
that the dWPC powders behaved as polyelectrolytes. Dilution decreases the
ionic strength and leads to an increase in the repulsive forces, resulting in the
expansion of the molecule and an increase in the reduced viscosity (Zsp=c).[21]

Water Holding Capacity

The derivatized protein powders possessed a much greater capacity to

hold water than the commercial WPCs (Table 5). With the underivatized
commercial WPC samples, nearly all of the powder remained in solution
after centrifugation. Because there was no pellet created by centrifugation
capable of retaining water, the water holding capacity was deemed to be zero.
Conversely, upon centrifugation of the derivatized protein solutions, the
derivatized powders were observed to hold greater than seven times their
weight in water.

Table 5. Intrinsic Viscosity and Water Holding Capacity of Commercial and Derivatized
Whey Protein Concentrate Powders at 25
C

Intrinsic Viscositya Water Holding Capacitya

Sample (mL=g) (g water held=g protein)

WPC86 8.0  0.5 0

WPC74 7.5  0.9 0
WPC64 6.7  2.1 0
dWPC86 75.4  2.5 8.39  0.05
dWPC74 55.8  1.7 7.62  0.18
dWPC64 48.0  2.1 7.79  0.07

a
Mean  standard deviation.
430 RESCH AND DAUBERT

Figure 4. Intrinsic viscosity plots of reduced viscosity vs. protein concentration for dWPC
samples at 25
C.

Electrophoresis

In the aforementioned experiments, the dWPC86 sample consistently

demonstrated superior thickening and water holding abilities, while the
dWPC74 and dWPC64 samples exhibited levels of functionality that were
similar to one another, but lower than that of the dWPC86 sample. To
attempt to explain these dierences in performance, the compositions of the
commercial WPC samples were examined by electrophoresis and mineral
content analysis. Because the protein component in each sample is ultimately
responsible for the thickening functionality, SDS-PAGE was employed to
determine if dierences existed in the amounts of the specic whey proteins in
each commercial WPC. Variations in the original whey composition and the
whey protein concentrate production conditions could result in WPCs with
dierent protein constituents and functionalities. However, Fig. 5 clearly
shows that the three commercial WPCs had very similar protein proles.
Quantication of the protein bands by densitometry revealed no signicant
dierences in the quantities of individual proteins.
The WPC compositions do oer possible explanations for the results of
the dWPC functionality tests. Table 1 shows that the WPC86 sample con-
tained the lowest quantities of the major minerals, especially calcium, while
the WPC74 and WPC64 samples had similar mineral contents. The level of
salts inuences the type of gel structure formed during the 3 h gelation period
at 80
C. At low salt concentrations the electrostatic repulsions between
proteins are only partially shielded and a translucent ne-stranded lament
DERIVATIZED WHEY PROTEIN CONCENTRATE POWDERS 431

Figure 5. SDS-PAGE gel of commercial whey concentrate powders. Lane 1 is a molecular

weight marker, lanes 24 are WPC86, lanes 57 are WPC74, and lanes 810 are WPC64.

gel is formed. As the salt concentration is increased, the electrostatic repul-

sions are completely shielded and attractive forces dominate, resulting in
protein aggregation and the formation of a particulate gel.[22] Hudson et al.[14]
reported that in the production of derivatized WPI powders, solutions with
higher salt concentrations permitted aggregation and formation of more
particulate-type ne-stranded gel structures. Upon freeze-drying and mil-
ling, the particulate gel structures were less eective in producing cold-set
thickening functionality than the ne stranded gel structures. Based on these
previous ndings, the lower level of salts in the WPC86 sample may have
limited protein aggregation more than in the WPC74 and WPC64 samples,
creating a more ne-stranded gel which upon further processing rendered
a more functional thickener. Furthermore, the similarity in the mineral
contents of the WPC74 and WPC64 samples may have been responsible for
the similarities in the rheological and physical properties displayed by the
dWPC74 and dWPC64 samples.
The lactose and lipid contents of each WPC sample listed in Table 1
may also provide rationale for the results of the dWPC characterization. The
WPC86 sample had signicantly lower contents of both lactose and lipid. The
increased sugar content in the WPC74 and WPC64 protected the proteins
from denaturation during the heating and tended to produce a more parti-
culate-type gel structure. The higher lipid content may have also inuenced
432 RESCH AND DAUBERT

the gel structure, as interactions between lipids and whey proteins, particu-
larly b-lactoglobulin, are well established.[23] However, additional research is
needed to further delineate the precise role played by minerals, lipids, and
lactose in the performance of derivatized whey protein concentrate powders.

CONCLUSIONS

A procedure for production of cold-set gelling derivatized whey protein

isolate was successfully applied to three commercial whey protein con-
centrates. The derivatization procedure greatly increased the ability of the
powders to impart viscosity and hold water. Weak gel structures were
formed by all three derivatized powders at ambient temperatures without
addition of salts. The performance dierences among the derivatized pow-
ders were explained by the inuence of the mineral content on the thermal
gelation whey proteins during the production of the derivatized powders.
The cold-set gelation capability gives rise to a wide range of applications
such as sports drinks, dairy beverages, sauces, llings, and infant and enteral
formulations.

ABBREVIATIONS

WPI, whey protein isolate; WPC, whey protein concentrate; WPC86,

whey protein concentrate 86% protein; dWPC, derivatized whey protein
concentrate; DI, deionized; SDS-PAGE, sodium dodecyl sulfate-poly-
acrylamide gel electrophoresis

AKNOWLEDGMENTS

The authors would like to thank Tim Seaboch for his freeze drying
assistance, Davisco Foods International, Inc. for providing the whey protein
concentrate samples, and the Southeast Dairy Foods Research Center for
supporting this study.
Paper No. FSR01-12 of the Journal Series of the North Carolina
Agricultural Research Service, Raleigh, NC 27695-7643. The use of trade
names does not imply endorsement by the North Carolina Agricultural
Research Service of products named, nor criticisms of similar ones not
mentioned.

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Received May 13, 2001

Revised September 6, 2001
Accepted September 25, 2001
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