Lebensm.-Wiss. u.-Technol.

, 35, 741747 (2002)

k-CarrageenanFProtein Interactions: Eect of Proteins

on Polysaccharide Gelling and Textural Properties
R. I. Baeza*w, D. J. Carpw, O. E. Perezz and A. M. R. Pilosof }

Universidad de Buenos Aires, Departamento de Industrias, Facultad de Ciencias Exactas y Naturales, Ciudad
Universitaria (1428), Buenos Aires (Argentina)
(Received March 4, 2002; accepted August 26, 2002)

Gelation and melting processes of kappa-carrageenan (k-C) in the presence of beta-lactoglobulin (b-lg), native and denatured soy
protein (NSP and DSP) isolates were investigated by dynamic rheological techniques, apparent viscosity measurements and DSC. In
the presence of proteins, large increases in gelation temperatures and storage moduli of the mixed gels compared to single k-C gel
were observed. Dierences between the proteins in the rst steps of the gelation process were revealed by apparent viscosity
measurements. Although little changes in melting temperatures were observed in the presence of proteins by dynamic rheology, the
DSC analysis showed a large increase in these temperatures. Synergistic eects were also observed on textural properties and water
absorption of the gels. The addition of proteins increased gel hardness, cohesiveness, gumminess, springiness and reduced syneresis.
These results might be due to excluded volume eects that increased the eective concentration of the hydrocolloid and electrostatic
interactions between both biopolymers in solution. The dierent behaviours observed with the three proteins would be related to their
water absorption capacity, molecular size, exibility and supercial charge under the experimental conditions described.

r 2002 Published by Elsevier Science Ltd.

Keywords: k-carrageenan; b-lactoglobulin; soy protein; gelation; melting

Introduction
Kappa-carrageenan (k-C) is an anionic sulphated
polysaccharide extracted from red algae, which is widely
used in food industry as a thickening, gelling and
stabilizing agent. It forms thermoreversible gels in the
presence of cations (Samant et al., 1993; Ipsen, 1995;
Drohan et al., 1997; Mleko et al., 1997; Lundin and
Hermansson, 1998; Tziboula and Horne, 1998; Ould
Eleya and Turgeon, 2000). By heating aqueous dispersions of k-C at temperatures above 60 1C, the polysaccharide hydrates and adopts a random coil
conformation. Gelation occurs on cooling at a critical
temperature and it has been attributed to a two-stage
reaction involving a coilhelix transition followed by
aggregation of helices (Morris et al., 1980; Morris,
1998). Further cooling enhances the association of
helices into long sti super-strands (Hermansson,
1995). The gelation process is highly inuenced by
To whom correspondence should be addressed.
E-mail: apilosof@di.fcen.uba.ar.
w
Research Fellow, Consejo Nacional de Investigaciones Cient cas y
Tecnicas de la Republica Argentina.
z
Research Fellow, Agencia Nacional de Promocion Cient ca y
Tecnologica, Argentina.
}
Member of Consejo Nacional de Investigaciones Cient cas y
Tecnicas de la Republica Argentina.

0023-6438/02/$35.00
r 2002 Published by Elsevier Science Ltd.

many factors such as the type and concentration of salts

in solution, cooling and heating rates, concentration of
the hydrocolloid and the presence of other biopolymers.
Modications of these factors greatly aect the gelling
and melting temperatures, and the rheological properties of the gels.
Among the most important applications of k-C is its use
in milk products. Therefore, much work has been done
on the gelation of k-C in the presence of milk proteins,
micellar caseins and real milk systems. k-C gelation was
found to be aected by casein fractions (Lundin and
Hermansson, 1998), micellar caseins (Drohan et al.,
1997) and whey proteins (Ould Eleya and Turgeon,
2000) where beta-lactoglobulin (b-lg) is the major
protein. In a previous work, we have observed that the
addition of sulphated and nonsulphated polysaccharides
to b-lg solutions reduced the critical concentration for
gelation and greatly modied the textural characteristics
of the protein gels (Baeza and Pilosof, 2001).
Soy proteins are used as functional ingredients in dairy
product analogues (Liu, 1997) due to their excellent
ability to impart desirable functionalities. Compared to
their dairy counterparts, soy-based analogues are not
only lower in cost, but also free of cholesterol and lower
in calories and fat. Special formulas based on soy proteins
are produced for people who are allergic to dairy milk.

doi:10.1006/fstl.2002.0938
All articles available online at http://www.idealibrary.com on

741

lwt/vol. 35 (2002) No. 8

The aim of this work was to compare the gelling

properties of k-C in the presence of b-lg and a vegetable
protein (soy protein) under conditions where these
proteins did not gel. The eects of thermal denaturation
of soy protein on the gelling properties of k-C were also
studied.

Materials and Methods

Sample preparation
Native soy protein isolate (NSP) was prepared from
defatted soybean our by extraction at pH 8.0 with
NaOH, precipitation at pH 4.5, neutralization at pH 7.0
and freeze-drying. Denatured soy protein isolate (DSP)
was prepared by heating a 50 g/L aqueous dispersion of
NSP at 100 1C for 30 min and freeze-drying at room
temperature.
Native b-lg samples were supplied by Besnier and Bridel
(France). k-C samples (Sano Bioindustries, Argentina)
were dispersed at a concentration of 10 g/L in 0.005 mol/
L phosphate (KH2PO4/Na2HPO4) buer at pH 7.0 and
then heated at 90 1C for 30 min. NSP and DSP isolates
and b-lg solutions were prepared by dissolving the
proteins in the phosphate buer under low stirring at
room temperature. Both protein and polysaccharide
solutions were prepared at double the desired nal
concentration of the mixed systems. The protein/
polysaccharide mixed systems were prepared by mixing
the solutions of proteins and k-C at 50 1C (to avoid
protein modication) in a 1:1 ratio. Final concentrations
were 20 g/L proteins/5 g/L k-C. To avoid bacterial
growth, 0.2 g/L sodium azide was added to the
solutions.

Rheological determination of gelling and melting

temperatures
Dynamic oscillation measurements were performed
using a Phar Physica controlled stress Rheometer
(MCR 300). Single k-C (5 g/L) or mixed k-C/protein
(5 g/L/20 g/L) solutions initially at 50 1C were poured
onto the bottom plate of a parallel plate measuring
system with a gap setting of 1 mm. The temperature of
the bottom plate was controlled with a Peltier system
(Viscotherm VT2, Phar Physica) and liquid paran was
applied to the exposed surfaces of the sample to prevent
evaporation. During gelling and melting experiments,
the frequency was held constant at 1 Hz and the strain
was kept at 0.01%. The samples were cooled from 50 to
10 1C at a rate of 2.5 1C/min and then held at 10 1C for
15 min, which had sucient time to allow storage
modulus (G0 ) equilibration. After ageing at 5 1C for
5 min, the samples were heated to 50 1C at a rate of
2.5 1C/min. The temperature at which the storage and
loss moduli (G0 and G@, respectively) crossed was taken
as the gel point, and the time and temperature at this
point were evaluated. The melting temperature for each
system was also evaluated at the point where G0 and G@
crossed during heating. The data reported are means of
at least two replicates.

Fig. 1 Experimental device for measuring apparent viscosity

and temperature during k-C gelation.

Viscosity measurements
The experimental set-up with two identical vessels,
shown in Fig. 1, was used to acquire temperature and
torque data simultaneously, under identical heat transfer conditions. Solutions (initially at 50 1C) were cooled
in a bath at 19.670.2 1C. Apparent viscosity as a
function of time was recorded for 1 h with a Brookeld
DV-LVT viscometer. The T-spindle (C) was rotated at
0.3 rpm and a helipath stand (pathway 0.4 cm) was used
(the T-spindle performed a helical pathway) to minimize
the eect of shear on gel formation. Concomitantly, the
temperature was recorded. The rate of aggregation
(vagreg) was estimated from the initial slope of the
apparent viscosity increase over time. Maximum viscosity (mmax) and the time at which this value was reached
were also reported.

DSC measurements
A Mettler TA 4000 DSC was used to obtain thermal
transition temperatures on single k-C and mixed
protein/k-C gels. Twenty milligram gel samples were
heated in aluminium pans (40 mL volume) from 5 1C to
70 1C at 10 1C/min. DSC calibration was performed
using ice and indium fusion thermograms, and an empty
aluminium pan was used as a reference. The recorded
thermograms were analysed using the Mettler TA 72
software to obtain the thermal transition temperatures.
The average of two replicates was reported.

Longitudinal compression measurements

Hot (50 1C) single k-C and mixed protein/k-C solutions
were poured into cylindrical containers, cooled to 5 1C
and stored overnight at 5 1C. Texture prole analysis
(TPA) was performed on the cylindrical gel specimens
(19 mm diameter  15 mm high) using a Stable Micro
Systems TA-XT2i Texture Analyser. The gels were
compressed with a cylindrical probe (3.6 mm diameter)
to 40% of their original height at a rate of 0.5 mm/s. The
average of two replicates was reported.

Results and Discussion

Table 1 shows the parameters determined for the
gelation process of single k-C and k-C+protein mixed

742

lwt/vol. 35 (2002) No. 8

Table 1 Gelation properties of single k-C (5 g/L) and k-C+protein (5 g/L/20 g/L) systems obtained by dynamic
oscillatory measurements
System
k-C
k-C+b-lg
k-C+NSP
k-C+DSP

tgel
(min)

Tgel
( 1C)

G0 max
(Pa)

19.670.2
14.670.2
16.470.1
14.370.3

11.170.4
20.970.4
17.270.1
21.670.5

45.572.8
154.677.7
129.3710.9
234.2729.2

k-C=kappa-carrageenan; b-lg=beta-lactoglobulin; NSP=native soy protein; DSP=denatured soy protein.

50

G' (Pa)

40
30

-C
-C + -LG

20

-C + NSP
-C + DSP

10
0
10

20

30

40

T (C)

Fig. 2 Temperature dependence of storage modulus for

single k-C (5 g/L) and k-C+protein (5 g/L/20 g/L) mixtures
during cooling process. Cooling rate 2.5 1C/min.

solutions by dynamic oscillatory measurements. The

gelling temperature (Tgel) for the dierent systems
decreased in the order k-C+DSPDk-C+b-lg4kC+NSP4k-C, and the gelling times varied inversely.
The cooling curves obtained by dynamic viscoelasticity
measurements are shown in Fig. 2. The storage modulus
started to increase at temperatures above 20 1C for all
the protein-containing systems although the gelation
temperatures reported in Table 1 are a little lower
because they correspond to the G@G0 cross-over point.
The storage modulus increased gradually with decrease
in temperature, showing dierences between dierent
systems. The mixtures of k-C with b-lg and DSP showed
similar G0 evolution with cooling down to 10 1C.
However, after 15 min at 10 1C, the systems with b-lg
and NSP reached similar G0 values, and the mixed gel
with DSP showed higher values of the storage modulus
(Table 1).
The sol-to-gel transition for k-C has been widely
studied. In most works, the gelation process has been
studied at concentrations higher than 5 g/L, which
resulted in higher values of gelling temperature and
storage modulus than those reported in Table 1. As the
objective of the present work was to study the inuence
of protein addition on the dynamics of k-C gelation, we
chose a low k-C concentration in order to maximize the
response.
Previous observations on k-Cprotein systems showed
synergistic eects between the two biopolymers on
gelation properties at pH above the isoelectric point of
proteins (Kampf and Nussinovitch, 1997; Mleko et al.,

1997; Neiser et al., 2000; Ould Eleya and Turgeon, 2000;

Schorsch et al., 2000). The main cause of these
synergistic eects seems to be thermodynamic incompatibility between the dierent biopolymers in solution.
At low pH values, sulphated polysaccharides and
proteins seem to be completely compatible. When pH
is increased above the isoelectric point of the protein, the
net charge of the protein becomes negative. As a result,
electrostatic repulsive forces between protein molecules
and sulphated polysaccharides increase, promoting
excluded volume eects. This leads to a mutual
concentration of both biopolymers in separated microphases and favour the gelation of the hydrocolloid. For
incompatible biopolymers in mixed solutions, the rate of
gelation is higher and the critical concentration for
gelation is lower than that for each individually
(Tolstoguzov, 1995). Lynch and Mulvihill (1994)
observed such excluded volume eects on Ca2+-free
i-carrageenan gels in the presence of caseins, resulting in
a local concentration of the hydrocolloid. Those eects
probably account for the ability of caseins to modify the
rheology of Ca2+-free i-carrageenan gels.
In this work, all the mixed systems were prepared at
neutral pH, which is above the isoelectric point of the
two proteins used (pH 5.2 for b-lg and pH 4.6 for soy
protein). Under these experimental conditions, thermodynamic incompatibility is favoured and the eect of
concentration would be the main explanation for the
increased Tgel and the high value of the storage modulus
for the mixed k-Cprotein systems. The dierent eects
observed when b-lg or soy protein were added may be
related to the dierences in their molecular exibility,
size and shape as excluded volume eects are inuenced
by these factors (Tolstoguzov, 1995).
As observed in Fig. 2, the rheological characteristics
monitored by dynamic measurements did not reveal any
dierences between the protein-containing gels at
temperatures above the gel point. In a previous work,
Stading and Hermansson (1990) dened the gel point as
the event that occurs when an innite network is formed
in a sample. Prior to the formation of the threedimensional network, several mechanisms involving
coil-to-helix transition of k-C molecules and helix
aggregation take place in the solution. In order to
obtain additional information on the solgel transition
of k-C in the presence of proteins, the experimental
device shown in Fig. 1 was used. The dynamics of
k-C+protein mixed systems at temperatures above the
gel point was determined from the continuous evolution
of apparent viscosity and temperature over time. Mixed

743

lwt/vol. 35 (2002) No. 8

DSP

2000
1500

NSP

1000
500

-lg
-C

0
0

10

20

Apparent viscosity (cps)

(a)

30
40
Time (min)

50

60

50-20 C

2000
DSP
-lg
1000
NSP
500

100
80

750

app

60

500

-C

40

G'
250

0
0

(b)

19.5 C

1000

1500

app (cp)

Apparent viscosity (cps)

2500

protein isolates on 5 g/L k-C gels (Mleko et al., 1997).

Imeson et al. (1977) also found a higher modication of
polysaccharide gelation in the presence of denatured
proteins. Protein denaturation enhanced the synergistic
eect of the gelation behaviour of k-C and this could be
related not only to an increase in thermodynamic
incompatibility due to the excluded volume eect, but
also due to an increase in electrostatic complex
formation because more charged groups on the surfaces
of the biopolymers became exposed. In conditions
of thermodynamic incompatibility, Grinberg and
Tolstoguzov (1997) observed the formation of soluble
protein-sulphated polysaccharides complexes at pH
values above the protein pI. This was attributed to the
formation of ionic pairs between ionized sulphate
groups of the polysaccharide and e-amino groups of
the protein.
An interesting observation was that the time at which
the maximum viscosity value was reached was approximately equal to the time to become gel as obtained by
dynamic measurements (Table 1). After this point, a
change in the viscosity curves was observed probably
due to the breakdown of transient structures formed at
the gel point. Fig. 4 shows the evolution of the apparent
viscosity and storage modulus obtained by the two
experimental methods for k-C+NSP system.
Addition of proteins to k-C gels had little eect on
melting temperatures of k-C gels as determined by
rheological measurements (Tm1 in Table 3). In the
presence of proteins, the melting temperature of the
mixed solutions was 13.4 1C higher than that of k-C
gels that melted at 32 1C. A hysteresis eect in the
rheological measurements between the heating and
cooling curves was observed (DT in Table 3). These

10

15

20

t gel

20

Time (min)

0
0

Fig. 3 Apparent viscosity of single k-C (5 g/L) and mixed kC+protein solutions (5 g/L/20 g/L) during gel formation as a
function of time (a) and initial viscosity increase (b) for gelling
rate determination. (B) k-C, (&) k-C+b-lg, (~) k-C+NSP,
(~) k-C+DSP

G' (Pa)

k-C+proteins solutions, initially at 50 1C, were cooled

down to 19.5 1C (the average sol-to-gel transition
temperature for all the mixtures determined by rheological measurements). Typical proles for the development of viscosity during cooling of k-C/protein mixtures
are shown in Fig. 3. For all the samples, there was an
initial period during which viscosity was very low. Then,
a sharp rise in viscosity was observed and continued to
increase up to a maximum.
Table 2 shows the parameters obtained from the
viscosity curves for the mixed systems. The aggregation
rate was determined from the initial slope of the
apparent viscosity over time (Fig. 3b). The systems with
b-lg or NSP had similar aggregation rates and maximum
viscosities, mmax (Table 2). In the presence of DSP, these
values greatly increased similar to the behaviour
exhibited by the storage modulus (Table 1). The higher
synergistic eects observed in k-C/DSP systems might
be associated with higher incompatibility due to thermal
denaturation of the protein. Higher synergistic eects
were also observed with thermally denatured whey

10

20

30

40

50

Time (min)

Fig. 4 Apparent viscosity and storage modulus plots for

k-C+NSP system during gel formation as a function of
time

Table 2 Aggregation rate (vaggreg), maximum viscosities (mmax) and gelation time obtained from apparent viscosity
measurements on k-C+protein (5 g/L/20 g/L) mixed systems
System
k-C+b-lg
k-CNSP
k-CDSP

vaggreg
(cps/min)

mmax
(cps)

t0 gel
(min)

8274
8772
19676

1057710
1123710
2286715

15.570.5
1671
1670.3

k-C=kappa-carrageenan; b-lg=beta-lactoglobulin; NSP=native soy protein; DSP=denatured soy protein.

744

lwt/vol. 35 (2002) No. 8

Table 3 Melting temperatures obtained by dynamic oscillatory measurements (Tm1) and DSC (Tm2) and thermal
hysteresis (DT) for k-C and k-C+protein systems
DT (Tm1Tgel)

Tm (1C)
System
k-C
k-C+b-lg
k-C+NSP
k-C+DSP

Tm1
3270.5
35.470.9
3370.4
34.570.7

Tm2 (DSC)

(1C)

o35
35.571
4071
4371

20.9
14.5
15.8
12.9

k-C=kappa-carrageenan; b-lg=beta-lactoglobulin; NSP=native soy protein; DSP=denatured soy protein.

Hardness

Texture properties

60

Adhesiveness
Gumminess

45
30
15
0

-C

+ -lg -C + NSP -C + DSP

-C

Springiness
Cohesiveness

1.0

Resilience

Texture properties

temperatures are in agreement with those reported by

Lundin and Hermansson (1998) for mixtures of Na-k-C
and casein. In the presence of caseins, an increase in
gelling and melting temperatures was observed. However, depending on the type of protein added and the
concentration of the hydrocolloid, the magnitude of the
hysteresis increased or decreased compared to that
observed for the system with k-C alone.
The hysteresis between setting and melting temperatures
for k-C gels is attributed to aggregation of carrageenan
helices that strengthens the gel network. The experimental evidence suggests that at Tgel, carrageenan
helices start to form and these helices aggregate during
ageing at low temperature so that melting of the gel
would occur at higher temperature than Tgel (Morris,
1998). The data reported in Table 3 show that in the
presence of proteins, the magnitude of thermal hysteresis decreased due to the large increase in Tgel compared
to the small increase in Tm1 observed for the mixed
systems. Similar eects were observed in the presence
of galactommanans, a- and k-casein and b-lg (Fernandes
et al., 1995; Lundin and Hermansson, 1998; Ould Eleya
and Turgeon, 2000).
DSC study showed a single endothermic transition on
heating k-C gels associated with gel melting and
dissociation of aggregates. Higher temperatures for the
gel melting process were obtained for the proteink-C
mixed systems (Table 3). For the soy protein-containing
systems, the melting temperature obtained by DSC was
much higher than that observed at the G0 G@ crossover.
The melting temperatures Tm1, obtained by dynamic
oscillatory measurements for the carrageenansoy protein systems, coincided fairly well with the onset point of
DSC endotherms. Thus, the DSC peak temperatures
represent the additional energy needed to complete
breakage of the aggregated ordered structure induced by
soy proteins. Similar behaviour occurred in konjac
glucomannank-C mixed systems. When the gel melted
completely and the system behaved rheologically as a
sol, a small amount of aggregated ordered structure still
remained as shown by DSC peak temperatures
(Kohyama et al., 1996).
In the mixed k-C+protein systems, the excluded volume
eects would be responsible for the formation of
stronger junction zones between k-C molecules that
melt at higher temperatures. Several authors have
reported transition temperatures for k-C from DSC
measurements indicating an important increase in
melting temperatures with k-C concentration (Nishinari

0.9
0.8
0.7
0.6
0.5

-C

+ NSP -C + DSP
-C + -lg -C

Fig. 5 Texture characteristics of k-C (5 g/L) and k-C+protein (5 g/L/20 g/L) mixed gels

et al., 1996; Kohyama et al., 1996; Tanaka et al., 1996).

The ability of the soy protein to promote an increase in
Tm2 would be due to the great water absorption capacity
of this protein compared with b-lg (Cheftel et al., 1989).
This would promote an increase in the eective
concentration of the polysaccharide, limiting the water
available and favouring inter- and intra-helix interactions in the polysaccharide solution. Additionally, the
breakdown of electrostatic complexes formed between
both biopolymers would shift the melting temperatures
to higher values.
The addition of proteins had a large eect on the texture
and visual characteristics of the gels. The mixed gels
showed increased gel turbidity and decreased syneresis
(data not shown). As shown in Fig. 5, the addition of
protein increased gel hardness, gumminess and cohesiveness of 5 g/L k-C gels. Springiness was increased
only in the presence of soy protein, and denaturation
further enhanced the texture parameters.

745

lwt/vol. 35 (2002) No. 8

Synergistic eects have been previously observed between carrageenan and proteins which resulted in much
stronger gels compared to carrageenan alone. Tziboula
and Horne (1998) suggested that in mixed carrageenan
serum proteins, the polysaccharide would interact with
the serum proteins and this interaction would have a
synergistic eect on gel strength. Mleko et al. (1997)
observed higher values of shear stress at fracture for
k-C gels in the presence of whey protein and similar
eects were found by Ipsen (1995) for mixed gels of
k-C with soy or pea protein.
The increased gel strength in the presence of proteins
might be caused by an increased hydrocolloid concentration because of the excluded volume eects. These
results agree with the increased aggregation rate and the
higher gelling and melting temperatures for the mixed
gels. Additionally, electrostatic cross-links between
proteins and k-C might cause a reinforcement of the
network structure.

Conclusions
The data reported in this work demonstrate the eects
of native or denatured proteins on the gelation and
melting of kappa-carrageenan (k-C) solutions and gels.
These eects might be due to thermodynamic incompatibility between k-C and globular proteins that enhanced
the gelling properties of the polysaccharide. The
increased aggregation rate observed during the cooling
process and the shift of peak temperatures under heating
conditions would be due to dierences between the
proteins, related to volume exclusion eects and
electrostatic interactions with k-C molecules.
The use of dynamic oscillatory methodology has proven
to be an excellent tool for characterizing gelation and
melting processes of dierent gel systems. In this work,
the application of complementary methods such as
apparent viscosity measurements and dierential scanning calorimetry gave additional information about the
phenomenon occurring during gelation, involving formation and dissociation of aggregates.
The increased gelation and melting temperatures and the
great improvement in gelation rate and characteristics of
k-C gels in the presence of proteins could be successfully
applied in food technology. The vegetable protein
showed behaviour similar to the animal protein, so the
former could be used as a replacement for the latter in
special foods. Synergistic eects increased with denaturation of soy protein, and this could be applied in the
design of new food formulations.

Acknowledgements
The authors acknowledge the nancial support from
Universidad de Buenos Aires, Consejo Nacional
de Investigaciones Cient cas y Tecnicas y Agencia
Nacional de Promocion Cient ca y Tecnologica de la
Republica Argentina.

References
BAEZA, R. AND PILOSOF, A. M. Mixed biopolymer gel systems
of b-lactoglobulin and non-gelling gums. In: DICKINSON, E.
AND MILLER, R. (Eds), Food ColloidsFFundamentals of
Formulation. Cambridge, U.K.: The Royal Society of
Chemistry, pp. 392403 (2001)
CHEFTEL, J. C., CUQ, J. L. AND LORIENT, D. Propiedades
funcionales. In: CHEFTEL, J., CUQ, J. AND LORIENT, D. (Eds),
Protenas Alimentarias. Zaragoza, Spain: Acribia Editorial
S. A., pp. 49105 (1989)
DROHAN, D. D., TZIBOULA, A., MCNULTY, D. AND HORNE, D. S.
Milk proteinscarrageenan interactions. Food Hydrocolloids, 11(1), 101107 (1997)
FERNANDES, P. B., GONCALVES, M. P. AND DOUBLIER, J.-L.
Thermal behaviour of kappa-carrageenan + galactomannan
mixed systems. In: DICKINSON, E. AND LORIENT, D. (Eds),
Food Colloids and Macromolecules. Cambridge, U.K.: The
Royal Society of Chemistry, pp. 321327 (1995)
GRINBERG, V. AND TOLSTOGUZOV, V. B. Thermodynamic
incompatibility of proteins and polysaccharides in
solutions. Food Hydrocolloids, 11(2), 145158 (1997)
HERMANSSON, A. M. The importance of biopolymers in
structure engineering. In: DICKINSON, E. AND LORIENT, D.
(Eds), Food Colloids and Macromolecules. Cambridge, U.K:
The Royal Society of Chemistry, pp. 321327 (1995)
IMESON, A .P., LEDWARD, D. A. AND MITCHELL, J. R. On the
nature of the interaction between some anionic
polysaccharides and proteins. Journal of the Science of
Food and Agriculture, 28, 661668 (1977)
IPSEN, R. Mixed gels made from protein and kappacarrageenan. Carbohydrate Polymers, 28, 337339 (1995)
KAMPF, N. AND NUSSINOVITCH, A. Rheological characterization
of k-carrageenan soy milk gels. Food Hydrocolloids, 11(3),
261269 (1997)
KOHYAMA, K., SANO, Y. AND NISHINARI, K. A mixed system
composed of dierent molecular weights konjac
glucomannan and k-carrageenan. II. Molecular weight
dependence of viscoelasticity and thermal properties. Food
Hydrocolloids, 10(2), 229238 (1996)
LIU, K. Soybeans: Chemistry, Technology and Utilization. New
York, U.S.A.: Chapman & Hall, International Thomson
Publishing (1997)
LUNDIN, L. AND HERMANSSON, A. M. Multivariate analysis of
the inuences of locust beam gum, as-casein, k-casein on
viscoelastic properties of Na-k-carrageenan gels. Food
Hydrocolloids, 12, 175187 (1998)
LYNCH, M. AND MULVIHILL, D. M. The inuence of caseins
on the rheology of i-carrageenan gel. Food Hydrocolloids,
8(34), 317329 (1994)
MLEKO, S., LI-CHAN, E. C. Y. AND PIKUS, S. Interactions of
k-carrageenan with whey proteins in gels formed at dierent
pH. Food Research International, 30(6), 427433 (1997)
MORRIS, E. R., REES, D. A. AND ROBINSON, G. Cation-specic
aggregation of carrageenan helices. Domain model of
polymer gel structure. Journal of Molecular Biology, 138,
349362 (1980)
MORRIS, V. J. Gelation of polysaccharides. In: HILL, S. E.,
LEDWARD, D. A. AND MITCHELL, J. R. (Eds), Functional
Properties of Food Macromolecules. Elsevier Applied
Science, UK, pp. 143226 (1998)
NEISER, S., DRAGET, K. I. AND SMIDSROD, O. Gel formation in
heat-treated bovine serum albumink-carrageenan systems.
Food Hydrocolloids, 14, 95110 (2000)
NISHINARI, K., WATASE, M., RINAUDO, M. AND MILAS, M.
Characterization and properties of gellank-carrageenan
mixed gels. Food Hydrocolloids, 10(3), 277283 (1996)
OULD ELEYA, M. M. AND TURGEON, S. L. Rheology of kcarrageenan and b-lactoglobulin mixed gels. Food
Hydrocolloids, 14, 2940 (2000)
SAMANT, S. K., SINGHAL, R. S., KULKARNI, P. R. AND REGE,
D.V. Proteinpolysaccharide interactions: a new approach

746

lwt/vol. 35 (2002) No. 8

in food formulations. International Journal of Food Science

and Technology, 28(6), 547562 (1993)
SCHORSCH, C., JONES, M. G. AND NORTON, I. T. Phase
behaviour of pure micellar casein/k-carrageenan systems in
milk salt ultraltrate. Food Hydrocolloids, 14, 347358
(2000)
STADING, M. AND HERMANSSON, A. M. Viscoelastic behaviour
of b-lg gel structures. Food Hydrocolloids, 4(2), 121135
(1990)
TANAKA, R., HATAKEYAMA, T., HATAKEYAMA, H. AND PHILLIPS,
G. O. Dierential scanning calorimetric studies of

Phillippiness
natural
grade
k-carrageenan.
Food
Hydrocolloids, 10(4), 441444 (1996)
TOLSTOGUZOV, V. B Some physico-chemical aspects of protein
processing in foods. Multicomponent gels. Food Hydrocolloids, 9(4), 317332 (1995)
TZIBOULA, A. AND HORNE, D. S. Inuence of milk proteins on
the gel transition temperature and mechanical properties of
weak k-carrageenan gels. In: WILLIAMS, P. A. AND PHILLIPS,
G. O. (Eds), Gums and Stabilisers for the Food Industry.
Cambridge, U.K.: The Royal society of Chemistry, pp.
202211 (1998)

747