Food Hydrocolloids 20 (2006) 423431

www.elsevier.com/locate/foodhyd

Keynote Paper

The gap between food gel structure, texture and perception

Denis Renard a,*, Fred van de Velde b,c, Ronald W. Visschers b,c
a

INRA Centre de Recherches de Nantes, Unite de physico-chimie des macromolecules, B.P. 71627, F-44316 Nantes Cedex 3, France
b
Wageningen Centre for Food Sciences, P.O. Box 557, 6700 AN Wageningen, The Netherlands
c
NIZO food research, Product Technology Department, Kernhemseweg 2, P.O. Box 20, 6710 BA Ede, The Netherlands (www.nizo.com)

Abstract
This paper summarizes the current status of research into the structure, texture and perception of food gels based on proteins and
polysaccharides. The first part of this paper deals with mechanisms of biopolymer gelation. In the second part the effects of post-gelation
phenomena are covered, demonstrating that it is of importance for the quality of food to realise that gels are metastable systems that continue to
evolve after the initial gelation process has taken place. Phase separated networks are presented in the context of the huge interest from the
industrial perspective and a short overview of physical mechanisms is given in a third part. In the final part examples from the dairy industry and
flavour perception are presented.
q 2005 Elsevier Ltd. All rights reserved.
Keywords: Food gels; Texture; Perception; Proteins; Polysaccharides

1. General introduction
For companies wishing to produce attractive gelled food
products it is of increasing importance to understand the
relationships between the perception of food gel texture and its
structure. The replacement of different ingredients usually
leads to changes in food structure that are often perceived by
consumers as giving a less attractive texture or mouth feel.
New products in functional foods, low-fat products, vegetarian
products and gelatine replacements were not always successful
as these products had inferior texture and were rejected by the
consumer. The key to prevent these debacles is to control and
adjust the sensoric perception of the product. The prerequisite
to do so is to well understand the relationship between food
structure and its sensory properties.
The product-transformation chain is the base of this
relationship. Nowadays, the product-transformation chain
needs to be considered in a more integrated approach than in
the past. In contrast with the logic of the conventional upstream
approach (do your best with the existing ingredients) the
chain needs re-engineering via a downstream analysis. Downstream analysis starts from the sensations that consumers
expect or desire of food products, down to texture and
* Corresponding author. Tel.: C33 2 40675052; fax: C33 2 40675043.
E-mail address: drenard@nantes.inra.fr (D. Renard).

0268-005X/$ - see front matter q 2005 Elsevier Ltd. All rights reserved.
doi:10.1016/j.foodhyd.2005.10.014

microstructure to end at the ingredient level. This approach

should make it possible to improve the industrial processes and
adapt to consumer requirements regarding the sustainability of
food products, the development of environmentally friendly
processes as well as the safety and diversity of end products.
This paper will give a first step to this integrated approach in
an overview of the relationship between food structure and
sensory perception. The first part of this paper describes the
microstructure of biopolymer gels and the mechanism of
biopolymer gelation with a focus on polysaccharide and
protein gels. Post-gelation phenomena may lead to undesirable
effects like syneresis and are the focus of the second section. A
huge interest for phase-separated networks has given rise to the
third part of this paper concerning biopolymer mixtures. In
addition, to finish, we will delve into the relationship between
gel structure, texture and perception.
2. Biopolymer gelation
Before starting an overview on biopolymer gelation a short
intermezzo on the definition of a gel is needed. The definition
of a gelled material as given by Ferry (1980) is a gel is a
substantially diluted system which exhibits no steady state
flow. This covers a range of substances which exhibit solidlike properties while a vast excess of solvent is present.
Comparable definitions are given by Atkins (1990) and in the
Encyclopedia of Polymer Science and Engineering (Tanaka,
1987). Gels consist either from space filling networks of
interacting particles such as fat crystals in the case of butter or

424

D. Renard et al. / Food Hydrocolloids 20 (2006) 423431

from cross-linked polymers that form a space-filling network

such as in the case of the white of a boiled egg. The interaction
between polymers or particles can by way of covalent reactions
or by physical interactions between different types of polymers
such as depletion forces and van der waals forces.
The former category (referred to as chemical gels) will not
be discussed in this paper, since most food gels belong to the
second type (referred to as physical gels). Food gels can be
further distinguished on the basis of different criteria. In this
context, we prefer to distinguish protein gels from fine
stranded polysaccharide gels. Examples of the former
category are heat-set protein gels from ovalbumin, whey
proteins and soy proteins (Ikeda & Morris, 2002; Renkema,
Gruppen, & van Vliet, 2002; Weijers, Visschers, & Nicolai,
2002). The latter category includes polysaccharides such as
carrageenan (van de Velde & de Ruiter, 2002), alginate
(Draget, Smidsrd & Skjak-Brk, 2002) and pectin (Ralet,
Bonnin, & Thibault, 2002).
A comparison between these two major classes of
biopolymer gels, protein and polysaccharide, gives rise to the
following items; the critical gelation concentration is generally
five to ten fold higher in the case of proteins while the stress at
failure is three fold lower; protein gels are often turbid except
in the case of gels formed at low ionic strength and gelatine
gels; syneresis and precipitation phenomena are commonly
encountered in protein gels (Renard, Robert, Garnier, Dufour,
& Lefebvre, 2000). The network forming capacity of proteins
is considerably reduced when proteins are denatured during the
purification stage (Renard, Lavenant, Sanchez, Hemar, &
Horne, 2002; Renard, Robert, Faucheron, & Sanchez, 1999;
Sanchez, Pouliot, Renard & Paquin, 1999). The ability to gel is
also reduced in the presence of high sugar concentration
(Bryant & McClements, 2000). Moreover, except for the case
of gelatine gels there are no crystalline phases observed in
protein gels contrary to what is observed in certain
polysaccharide gels. Finally, and probably the most relevant
characteristic for technological applications is that protein
gelation is not easy to control.
Does this mean that proteins are bad candidates to create
structure and texture in food products? Certainly not. Proteins
are an important part of our diet since they have very good
nutritional qualities. They are rich in essential amino acids and
sometimes in organic minerals (calcium and phosphate for
milk proteins). Moreover, proteins also can give color and taste
to foods. Apart from these nutritional qualities, protein gels
may be produced in several ways: increasing temperature,
pressure or exposure to microwaves, acidification or changing
the solvent quality. Several enzymatic treatments can also be
used such as chymosin (rennet) or trans-glutaminase for
instance. All these processes allow the formation of different
microstructures in the protein networks which give rise to
important classes of foods such as cheese, yoghurt and tofu.

their gel forming capacities (Cayot & Lorient, 1997; Doi &
Kitabatake, 1997; Utsumi, Matsumara & Mori, 1997). These
globular protein gels are generally referred to as heat set gels
(Clark & Lee-Tuffnell, 1986), as the gelation is usually induced
by the thermal unfolding of the globular proteins. Such heat-set
mechanisms are generally irreversible and gels formed during
heating retain their gel structure upon cooling and repeatedly
heating. Examples of globular protein gels are depicted in Figs.
1 and 2 for the particular case of b-lactoglobulin (Aymard,
1995). Fig. 1 corresponds to the events occurring during the
early stages of aggregation of the protein in the conditions
where repulsive interactions are predominant. At very low
ionic strength, aggregates formed have a rodlike shape and
contain very few branching points. The stability of these
structures is reached by long range, weak attractive interactions. At low ionic strength these fine-stranded gels may
resemble to some aspects to polysaccharide gels. With
increasing ionic strength both the flexibility of the aggregates
and the number of branching points increase giving rise to
coarser and less translucent gels.
Fig. 2 depicts the protein gels obtained when electrostatic
repulsions are screened. The aggregation occurs in two steps in
these conditions. First small globular aggregates are formed
which subsequently aggregate to form fractal structures.
Fractal means self-similarity at many lengthscales of observation. Interchange of disulfide bonds, leading to intermolecular bonding is probably involved in the formation of the
elementary subunit (Aymard, Gimel, Nicolai, & Durand,
1996). These gels are often called particulate or particle gels.
In the case of fine-stranded gels, the reactivity of the sulphydryl
groups is very small which inhibits the formation of the
elementary subunit. However, in both cases, the step leading to
the formation of fractal aggregates involves mainly an end to
end aggregation, with occasional branching. The amount of

2.1. Globular protein gels

Globular proteins, such as b-lactoglobulin, ovalbumin
and plant storage proteins (soy, pea etc) are well known for

Fig. 1. Mechanism of the formation of a fine-stranded b-lactoglobulin gel (with

permissions adapted from P. Aymard, PhD thesis, Universite du Maine, 1995).

D. Renard et al. / Food Hydrocolloids 20 (2006) 423431

Fig. 2. Mechanism of the formation of a b-lactoglobulin particle gel (with

permission adapted from P. Aymard, PhD thesis, Universite du Maine, 1995).

branching and the persistence length of the aggregates are

determined by the concentration of added salt, which screens
the repulsive electrostatic interactions (Aymard, Nicolai,
Durand, & Clark, 1999).
2.2. Polysaccharide gels
In contrast to globular protein gels, most polysaccharide
gels are reversible cold setting gels. Gel formation proceeds via
a disorder-to-order transition induced by cooling (Morris,
1998). This process is reversible and gel melting is therefore
possible by re-heating. The way in which crosslinks between
individual chains are formed is different from polysaccharide
to polysaccharide. Grant and co-workers (Grant, Morris, Rees,
Smith, & Thom, 1973) proposed the egg-box model for
gelation of alginate or pectin (Fig. 3). Affinity of some parts of
the chain for calcium gives rise to junction zones formation,
thus promoting intermolecular associations. Alginates consists
of (1/4) linked b-D-mannuronic acid and a-L-guluronic acid
residues of widely varying composition and sequence, in which

Fig. 3. Different junction zones of the egg-box model. a) Multichain junction

zones. b) Dimeric junction zones (with permission reproduced from (a) Grant
G.T. et al., FEBS Letters (1973), 32, 195198 and (b) Morris E.R. et al.,
International Journal of Biological Macromolecules (1980), 2, 327330).

425

the calcium binding sites are formed by homopolymeric

regions of guluronic acid residues (Draget et al., 2002). In
pectin, particularly in the case of low-methoxy pectin, the Cabinding sites are formed by the so-called smooth regions of
homogalacturonic acid regions (Ralet et al., 2002). Besides
these smooth regions, pectic polysaccharides consist of
hairy rhamnogalacturonan regions to which complex neutral
sugars side chains are attached. Initially the egg boxes were
considered to be multimolecular aggregates (Fig. 3). More
recent studies (Morris, Gidley, Murray, Powell, & Rees, 1980)
support a simpler dimerisation model for the junction zones
(Fig. 3b).
A second example concerns the gelation of carrageenans, a
group of sulfated galactans extracted from certain species of
red seaweeds (van de Velde & de Ruiter, 2002). In general
terms, k-carrageenan gels are hard, strong and brittle gels that
are freeze/thaw instable, whereas i-carrageenan forms soft and
weak gels that are freeze/thaw stable. The first step in the
gelation of carrageenan is the transition from a disordered
(random coil) to the ordered (helical) state (Viebke, Piculell &
Nilsson, 1994). The helical conformation is promoted by the
addition of salts or by lowering the temperature. Monovalent
cations (KC, RbC, CsC and NHC
4 ) promote the aggregation of
k-carrageenan double helices to form so-called aggregated
domains (Fig. 4) (Morris, 1998). Gel formation in i-carrageenan gels is assumed to take place at the helical level by
branching and association through incomplete formation of
double helices (Viebke et al., 1994). The number of branching
points plays an important role in the gel strength of
i-carrageenan gels (van de Velde et al., 2002).
2.3. Gelatine gels
In some respects, gelatine behaves more like a polysaccharide gel than a globular protein gels, as it is a cold-setting
thermoreversible gelation process. In comparison with carrageenan and other gel forming polysaccharides, such as gellan
gum and agarose, gelatine exhibit a coil-to-helix or disorderedto-ordered transition upon cooling. Fig. 5 illustrates the
mechanism of the formation of a gelatine gel. Gelation is
governed by the partial reformation of triple helices found in
collagen during cooling. In a first step, a polypeptidic chain
takes an orientation to induce a reactive site then, condensation
of two others chains near the reactive site occurs giving rise to

Fig. 4. Domain model for the gelation of k-carrageenan (with permission

adapted from Morris V.J. Gelation of polysaccharides. In: Functional properties
of food macromolecules (pp. 143226), Hill S.E., Ledward D.A. & Mitchell
J.R. (1998) Aspen, Gaithersburg (USA)).

426

D. Renard et al. / Food Hydrocolloids 20 (2006) 423431

Fig. 5. Model describing the cooperative character of gelatine gelation (with

permission reproduced from V. Normand, PhD Thesis, Universite Henri
Poincare Nancy I (1995)). Small coiled structures can induce further formation
of coils on different strands.

triple helix formation (Godard, Biebuyck, Barriat, Naveau, &

Mercier, 1980; Normand, 1995).
Gelatine gels are nearly purely elastic but Eldridge & Ferry
(1954) observed that gelatine gels flowed under stress at very
long timescales. This flow behaviour in gelatine gels is
explained by the reversibility of the junction zones. An
equilibrium may exist between creation and destruction of
junction zones in the network under stress, allowing thus the
flow of the material without return to the initial state. This
rheological behaviour is also encountered in globular protein
gels or in particle gels in general.
3. Post gelation phenomena
3.1. Structural rearrangements in protein gels
Gels are materials with characteristics from both liquids and
solids. Many particle or emulsion gels can be described as
networks made up of particles connected by viscoelastic bonds
with long relaxation times (Mellema, Heesakkers, van
Opheusden, & van Vliet, 2000). They are thus in a metastable
state from a thermodynamic point of view. Bonds between
particles in such colloidal gels are not always static. They may
change during the observation time, either spontaneously or
due to external forces. The dynamic character of the bonds may
also lead to gradual changes in the structure that, in turn,
change the rheological properties. Such ageing phenomena are
spontaneous in the sense that they do not result from
mechanical disturbance such as shear-induced bond breaking
(Mellema, Walstra, van Opheusden, & van Vliet, 2002). The
ageing commonly involves a gradual coarsening of the
structure and a change in firmness. An ultimate effect of
structural rearrangement is syneresis or expulsion of liquid
determined both by the stress acting on the gel and the
permeability of the network. Syneresis can be either desired,
like in manufacture of cheese or undesired like in manufacture
of yoghurt. The question is at which spatial and time scales
these structural rearrangements inside the gel occur.
Syneresis and spontaneous rupture are macroscopic
phenomena can be caused by three types of microscopic
processes that are linked to the basic building blocks of protein
gels. As described before, most protein gels are fractal
structures of small (10500 nm) aggregates of denatured
protein units. Interparticle rearrangements or reorganisation
within these particles occur mainly during aggregation. These

particles further interact with each other to form a spacefilling

network. Intraparticle rearrangements or particle fusion on this
lengthscale occurring mainly during gel ageing may be probed
by electron microscopy or by the measurement of tangent delta
at low frequency by means of small amplitude oscillatory shear
measurements. Tangent delta (the loss modulus over the
storage modulus ratio) is a measure of the proportion of bonds
with a relaxation time about equal to the reciprocal of the
applied frequency. In other words, it is a measure of the
dynamics of the system at length scales from molecules to
particles. The lengthscale of these types of changes is in the
micrometer range and can be probed by computer simulations,
light scattering or confocal microscopy. Intercluster rearrangements also called coarsening or micro-syneresis and typically
involve the formation of water-channels in the structure. They
can be probed by confocal or classical microscopy, permeametry or by large deformation rheological measurements.
3.2. Intraparticle rearrangements
Intraparticle rearrangements were clearly observed in the
cold-gelation experiments carried out by Alting, Hamer, de
Kruif, Paques, and Visschers (2003). In these experiments, a
pre-heated solution of whey proteins with a well defined size
(usually around 50 nm) was gradually acidified with gluconod-lactone. By varying the amount of glucono-d-lactone it was
possible to control the time during which the system was in the
gelled state. The protein particle size grew significantly (up to
500 nm) during the time the system was in the gel-state.
Furthermore, this particle-fusion type of process depended
strongly on the availability of free thiols at the surface of the
aggregates. When these groups were chemically blocked, no
particle-fusion was observed. The time-scale of this process
was rather fast ranging from minutes to about one hour at room
temperature.
3.3. Interparticle and intercluster rearrangements
Interparticle and intercluster rearrangements are illustrated
for the case of rennet-induced casein gels in Fig. 6. Mellema
et al. (2002) observed that the storage modulus G 0 continues to
increase as a function of time after rennet addition. The
increase of G 0 in fresh gels can be due to an increased contact
area between the micelles by intraparticle rearrangements
(particle fusion). The total increase of G 0 depends strongly on
pH (lower pH yields lower G 0 ) and temperature (higher
temperatures yield lower G 0 ).
Interparticle rearrangements can occur when there is
sufficient freedom for the micelles to move around. This may
be the case in the early stages of gel formation. The occurrence
of intercluster rearrangements is supported by confocal
microscopy observations since thinning and fracturing of
strands are observed as a function of time during gel ageing
(Mellema et al., 2000). Also gel ageing is accompanied by a
gradual formation of larger pores. The authors summarize the
effect of pH and temperature on structural rearrangements and
rheological properties by concluding that lowering pH or

D. Renard et al. / Food Hydrocolloids 20 (2006) 423431

427

Fig. 6. Development of G 0 (left panel) and microstructure (right panel) of casein micelle solutions as a function of pH and temperature during renneting. Panels a, b,
and c depict the aging/maturation of the gels in time. Reprinted with permission from (Mellema et al., Adv.Colloid Interf. Sci. (2002), 98, 25 and Mellema et al.,
Langmuir (2000), 16, 6847).

increasing temperature speeds up the gel ageing or rearrangement process.

Syneresis can be seen as the macroscopic consequence of
the transient character of the gel structure. This conclusion
supports the fact that a gel from a thermodynamic point of view
is in a metastable state and a significant amount of bonds within
the network have a reversible character. The driving force of
these structural rearrangements comes from the non equilibrium conditions of the gel material. As a consequence, the
permanent reorganisation within the material aims to minimize
the free energy of the system. Gels in that sense can be
considered as soft glassy materials where the non crystalline
and random organisation within the system induces a
metastable state.
4. Phase separated networks
4.1. Structures of phase-separated systems
Proteinpolysaccharide mixtures that are subject to phaseseparation are interesting for the creation of new structures
simply because the addition of polysaccharides at low
concentrations can create major differences in structure and
rheological properties of mixed systems as a result of
intertwining gelation and phase-separation processes. In
addition, they can also induce major differences in consistency
or texture with only minor effect on other organoleptic
properties. Three examples of such systems are briefly
presented here. A short impression of what is known about
the physical background of these phenomena and how this
helps to control the functionality in terms of structure and
texture for different mixtures will be given thereafter.
When phase separation in proteinpolysaccharide mixtures
occurs the included phase may form spherical domains. Their

size can vary but is commonly in the range of 220 mm. The
observed formation of spherical inclusions suggests that a
significant liquidliquid interface energy is acting within these
mixtures. For instance, in gelatinmaltodextrin mixtures, phase
separation quite often leads to the entrapment of droplets
within droplets (Norton & Frith, 2001). Gelation of one or both
phases is a good way to arrest the process of ripening of the
phase structure. Gelation of one phase has been observed by
several authors and is usually explained by an additional
separation which occurs within the droplets themselves rather
than by diffusion of the polymers to the already formed
droplets. The second example depicted on Fig. 7 is when
conditions lead to favourable electrostatic interactions between
b-lactoglobulin and arabic gum, associative phase separation
occurs and droplets called coacervates are formed that grow
markedly as a function of time (Schmitt, 2000). Ultimately, this
process leads to a structured phase that contains both types of
biopolymers.

Fig. 7. Typical structure of coacervates formed after complexation of blactoglobulin with acacia gum at pH 4.2 in water after 24 h, CtotZ3% (w/w),
protein to polysaccharide ratio 2:1. Scale bar represents 50 mm.Reprinted with
permission from (C. Schmitt, PhD Thesis, INPL Nancy (2000)).

428

D. Renard et al. / Food Hydrocolloids 20 (2006) 423431

4.2. Physical background of phase separation

Mixed solutions of chemically or conformationally different
biopolymers are unstable and separate into two liquid phases.
The chemical analysis of the phases is usually presented in the
form of a phase diagram (Doublier, Garnier, Renard, &
Sanchez, 2000). Phase diagrams establishment allows the
distinction between the one phase region of miscibility and the
two phase region of incompatibility where two liquid phases
are formed when the system reaches the thermodynamic
equilibrium. The binodal line delimits the fronteer between the
miscibility and the incompatibility areas. The points located on
the binodal give the composition of each phase at equilibrium.
These points are connected by the tie-lines. The spinodal line
separates the metastable and unstable regions of the two-phase
system. This overall behaviour is a common rule for
biopolymer mixtures in solution.
Phase separation in mixed biopolymer solutions is always
accompanied by rheological changes. The rheological behaviour of mixed systems differ noticeably from pure biopolymer
solutions. Micellar caseinguar gum mixtures are a typical
example. The viscoelastic behaviour of pure guar gum is that of
a regular macromolecular solution with G 0 lower than G 00 at
low frequency and a crossover at high frequency (Fig. 8).
Response from micellar casein is typical of a suspension with
also a strong variation of G 0 with frequency. Both onecomponent systems do not evidence any organisation of the
medium. In contrast, caseinguar gum mixtures exhibit
viscoelastic moduli less dependent upon frequency and their
value is much higher than for guar gum alone (Bourriot,
Garnier & Doublier, 1999). In addition, the G 0 curve tends to
Two-phases region

level off towards the low frequency range and to cross the G 00
curve (Fig. 8). These results suggest a solid-like behaviour
resulting from a structuration of the medium. The storage
modulus of such a gel-like system appears however very low.
The corresponding microstructures revealed by confocal
scanning laser microscopy of the mixtures located in the onephase region or two-phase region are also shown. Fluorescence
of the mixtures in the one-phase region is regularly distributed
indicating that casein is spread all over the medium (Fig. 8). In
the case of the mixtures located in the two-phase region,
distribution of the fluorescence is not regular. Casein is
localized in white areas which have a broad size distribution,
these large zones originate from a concentration of casein
micelles. Two phases coexist obviously in the system, one
containing mainly casein micelles whereas the other one is
enriched with guar gum.
To understand the behaviour of these systems we need to
realise that hydrocolloids can form mixed gels when the
concentration of each of them in the mixed solution exceeds the
minimum concentration for gelation. Normally, the minimum
concentration for heat-induced gelation of biopolymers varies
from 0.1 to 15% weight/weight. The minimum concentration
for gelation usually decreases when another incompatible
biopolymer is added. This is due to an excluded volume effect
in the single phase mixed solution. In the phase separated
biopolymer systems, the same effect may be due to water
redistribution between phases during gelation. The range of
minimum concentrations for hydrocolloid gelation is usually
lower than that of the phase separation threshold. This means
that a mixture of biopolymer gelling agents can form gels in
concentration areas lying both above and below the binodal

G', G" (Pa)

101
100
0.2% G + 3% MC
101
0.2% G
102
0.2% G + 0.3% MC
3% MC

103
One-phase region
104 2
10

101

100
(rad/s)

101

102

Fig. 8. Viscoelastic properties of a micellar casein suspension (3%), a guar gum solution (0.2%) and guar gummicellar casein mixtures with the corresponding phase
microstructures. Reprinted with permission from (S. Bourriot et al., Food Hydrocolloids (1999), 13, 4349).

D. Renard et al. / Food Hydrocolloids 20 (2006) 423431

curve. Accordingly, gelation of the mixed solution leads to

filled gels above the binodal and to single-phase mixed gels
below the binodal (Zasypkin, Braudo & Tolstoguzov, 1997).
Filled gels correspond to gel rich in one polymer and filled with
liquid particles rich in the other polymer or to gels filled with
gel particles, each phase being a filled gel. Single-phase mixed
gels correspond to single-phase gel of polymer 1 for example
filled with polymer 2 or conversely.
In all these systems, the final structure and morphology of
the composite system is determined by the interface between
the phases. Much progress has been made to be able to measure
the interfacial tension in mixed systems (Scholten, Tuinier,
Tromp, & Lekkerkerker, 2002). In order to design the
microstructure of mixed systems, one clue for food industries
will be to understand the role and importance of the interface
between the phases in particular at the molecular level. In
addition, the development of predictive models for material
properties of composites based on their microstructure will be
necessary (Norton & Frith, 2001).
5. Relation between gel structure, texture and flavour
perception
5.1. Texture design in dairy industry
From a perception point of view, firmness and creaminess
are the major sensory attributes important for consumer
preference of fermented dairy products such as yoghurt,
cheese, fermented cream and milk based desserts. These are
extremely complex attributes that can not be captured with a
single physical property. From the rheological point of view,
two important characteristics of dairy products can be
distinguished: viscosity and elasticity. Both properties are
important for the organoleptic quality of a product and for its
appealing appearance and pleasant mouth feel. Viscosity is the
property of a material to resist deformation. In the context of
fermented dairy products viscosity relates directly to attributes
such as as slimy, thin and fluid. Elasticity represents the
property of a material to recover after a deformation occurred.
This property corresponds to simple attributes such as firm
body and gum-like.
Exopolysaccharides (EPSs) are synthesised by lactic acid
bacteria during fermentation and act both on firmness and
creaminess of these products. EPSs increase the viscosity of the
serum phase, bind hydration water and, thus, reduce the water
flow in the matrix space. Moreover, exopolysaccharides
decrease syneresis and improve product stability. Dairy
industries have rationalised the relationship between these
sensory attributes and the applications of exopolysaccharides
in these products (Duboc & Mollet, 2001) in the following
way.
Different lactic acid bacteria are known to produce neutral
and charged EPSs (de Vuyst & Degeest, 1999; Ruas-Madiedo,
Hugenholtz & Zoon, 2002). These two classes of EPSs have
quite distinct functional properties (Duboc & Mollet, 2001).
The viscosity of the product with neutral exopolysaccharide
increased with time and was about ten times higher than

429

the viscosity of a control product obtained with a nonpolysaccharide producing strain. Surprisingly, the viscosity of
the product with the charged exopolysaccharide was comparable to the control product. In contrast, the elasticity (as
measured the storage modulus G 0 ) was significantly higher in
the product containing a negatively charged polysaccharide.
These experiments show that neutral exopolysaccharide
contributes to the viscosity but not to the elasticity. On the
other hand, negatively charged polysaccharide contributes to
the elasticity, but not to the viscosity, since they interact with
the positively charged casein particles by electrostatic
interactions, reinforcing the strength of the network and
consequently increasing G 0 . As a consequence different strains
of lactic acid bacteria that produce either charged or neutral
EPSs can be selected to tailor mouthfeel.
5.2. Flavourmatrix interactions
Besides texture, flavour release is the second important factor
determining the perception of gelled food products. Addition of
hydrocolloids to foods causes a change in the flavour perceived.
The mechanism for this change is not well understood. In the
case of proteins flavour molecules can bind to the protein,
causing a decrease in effective concentration and therefore a
decrease in flavour perception. Since flavours are present in food
at low levels anyway, a relatively small amount of binding can
exert a significant effect in terms of perceived flavour. However,
binding of flavours to most other hydrocolloids (gums) is
minimal in high water containing food products.
If the binding of flavours to hydrocolloids is minimal, then
alternative explanations need to be invoked to explain the
decrease in flavour perception. One suggestion is that the
increased viscosity of products containing hydrocolloids
causes slower mass transfer, therefore slower flavour release
and decreased flavour perception from these products during
eating. MS-nose technology has been developed to follow the
concentration of volatile flavours in the noses of people eating
food (Fig. 9) (Taylor, Besnard, Puaud, & Linforth, 2001). By
obtaining sensory information from the subjects in conjunction
with the concentration measurements on the same samples, it is
possible to study the link between the perceived intensity of
flavour chemicals to their actual concentration and release from
the food. These techniques have been applied to study how

Fig. 9. Schematic representation of the MS-nose technology. Reprinted with

permission from (A.J. Taylor et al., Biomolecular engineering (2001), 17, 143
150).

430

D. Renard et al. / Food Hydrocolloids 20 (2006) 423431

Fig. 10. Effect of gel texture on the flavour-release: (A) sensory flavour
perception vs the gelatine concentration, (B) measured time-intensity curves
for two different gels. Reproduced with permission from (A. J. Taylor, personal
communication, Dijon, October 2000).

hydrocolloids cause a change in flavour perception and direct

effects of texture on the perceived intensity (so-called crossmodal interactions) could be demonstrated (Weel et al., 2002).
Taylor and collaborators at the Samworth Flavour Laboratory in UK (Taylor et al., 2001) studied the effect of gelatine
concentration on the intensity of furfuryl acetate perception.
There is a strong trend of decreasing perception with increasing
gelatine concentration (Fig. 10A) (Taylor, 2000). Measuring
the in-nose concentration shows a delay in the timing of the
maximum intensity of the flavour signal reaching the nose but
no difference in maximum intensity of release (Fig. 10B)
(Taylor, 2000). The texture of the gelled food containing the
flavour has an effect on the perception of the flavour, whereas
the amount of flavour released is unaffected. In addition, Taylor
concluded that the rate of release is best correlated with the
observed change in sensory perception from the different gel
samples.
In another study Boelrijk and co-workers at NIZO food
research demonstrated that the perception diacetyl and
ethylbutyrate was directly influenced by the hardness of gels
(Personal data). In their experiments it was clear that although
similar concentrations of the flavours were released into the
nose, gels with increased hardness were perceived as less
intense flavoured.
6. Outlook and concluding remarks
We would like to conclude with the following French quote:
Ce nest pas assez de savoir les principes, il faut savoir
manipuler that translates into Its not enough to know the
principles, we have to know how to manipulate. This sentence
was found in the first edition of the chemical manipulations
written by Michael Faraday. This quote is simply to say that the
chemical and physical principles applied in food science are
not always at our convenience from a desired sensations point
of view. Anyone who cooks daily knows that it is quite easy to
fail in the preparation of a mayonnaise or a souffle. From this
simple consideration, we may imagine how difficult it can be in
the scale up applications encountered in food processes.
Acknowledgements
First of all, DR would like to thank the organisers and more
particularly professor Hamer for the invitation to be a keynote
speaker in the WCFS Food Summit.

The authors gratefully acknowledge Dr Alexandra Boelrijk

(NIZO food research), Dr Els de Hoog (Wageningen Centre for
Food Sciences & NIZO food research), Ir. Marja Kanning
(NIZO food research), Dr Ir. Ton van Vliet (Wageningen
Centre for Food Sciences & Wageningen University), Ir.
Mireille Weijers (Wageningen Centre for Food Sciences &
Wageningen University) for critically reading (parts of) the
manuscript.
References
Alting, A. C., Hamer, R. J., de Kruif, C. G., Paques, M., & Visschers, R. W.
(2003). Number of thiol groups rather than the size of the aggregates
determines the hardness of cold set whey protein gels. Food Hydrocolloids,
17, 469479.
Atkins, P. W. (1990). Physical chemistry (4th ed.). Oxford: Oxford University
Press p. 706.
Aymard, P. (1995). Agregation thermique de la b-lactoglobuline: Influence des
interactions sur les proprietes statiques et dynamiques des agregats et
incidences sur les processus de croissance. PhD thesis, Universite du Maine.
Aymard, P., Gimel, J.-C., Nicolai, T., & Durand, D. (1996). Experimental
evidence for a two-step process in the aggregation of b-lactoglobulin at pH
7. Journal de Chimie Physique, 93, 987997.
Aymard, P., Nicolai, T., Durand, D., & Clark, A. (1999). Static and dynamic
scattering of b-lactoglobulin aggregates formed after heat-induced
denaturation at pH 2. Macromolecules, 32(8), 25422552.
Bourriot, S., Garnier, C., & Doublier, J.-L. (1999). Phase separation, rheology
and microstructure of micellar caseinguar gum mixtures. Food Hydrocolloids, 13, 4349.
Bryant, C. M., & McClements, D. J. (2000). Influence of sucrose on NaClinduced gelation of heat denatured whey protein solutions. Food Research
International, 33(8), 649653.
Cayot, P., & Lorient, D. (1997). Structurefunction relationships of whey
proteins. In S. Damodaran, & A. Paraf (Eds.), Food proteins and their
applications (pp. 225256). New York: Marcel Dekker.
Clark, A. H., & Lee-Tuffnell, C. D. (1986). Gelation of globular proteins. In J. R.
Mitchell, & D. A. Ledward (Eds.), Functional properties of food
macromolecules (pp. 203272). London: Elsevier Applied Science Publishers.
de Vuyst, L., & Degeest, B. (1999). Heteropolysaccharides from lactic acid
bacteria. FEMS Microbiology Reviews, 23, 153177.
Doi, E., & Kitabatake, N. (1997). Structure and functionality of egg proteins. In
S. Damodaran, & A. Paraf (Eds.), Food proteins and their applications (pp.
325340). New York: Marcel Dekker.
Doublier, J.-L., Garnier, C., Renard, D., & Sanchez, C. (2000). Protein
polysaccharide interactions. Current Opinion in Colloid and Interface
Science, 5(34), 184196.
Draget, K. I., Smidsrd, O., & Skjak-Brk, G. (2002). Alginates from algae. In
E. J. Vandamme, S. De Baets, & A. Steinbuchel, Biopolymers polysaccharides
from eukaryotes (Vol. 6) (pp. 215244). Weinheim: Wiley.
Duboc, P., & Mollet, B. (2001). Applications of exopolysaccharides in the
dairy industry. International Dairy Journal, 11(9), 759768.
Eldridge, J. E., & Ferry, J. D. (1954). Studies of the cross-linking process in
gelatin gels. III. Dependence of melting point on concentration and
molecular weight. Journal of Physical Chemistry, 58, 992995.
Ferry, J. D. (1980). Viscoelastic properties of polymers (3rd ed.). New York:
Wiley.
Godard, P., Biebuyck, J. J., Barriat, P. A., Naveau, H., & Mercier, J. P. (1980).
Cinetique de cristallisation de la gelatine en solution aqueuse. Influence des
differents composes moleculaires. Makromolekulare Chemie, 181,
20092018.
Grant, G. T., Morris, E. R., Rees, D. A., Smith, P. J. C., & Thom, D. (1973).
Biological interactions between polysaccharides and divalent cations: The
egg-box model. FEBS Letters, 32, 195198.
Ikeda, S., & Morris, V. J. (2002). Fine-stranded and particulate aggregates of
heat-denatured whey proteins visualized by atomic force microscopy.
Biomacromolecules, 3(2), 382389.

D. Renard et al. / Food Hydrocolloids 20 (2006) 423431

Mellema, M., Heesakkers, J. W. M., van Opheusden, J. H. J., & van Vliet, T. (2000).
Structure and scaling behavior of aging rennet-induced casein gels examined by
confocal microscopy and permeametry. Langmuir, 16, 68476854.
Mellema, M., Walstra, P., van Opheusden, J. H., & van Vliet, T. (2002). Effects
of structural rearrangements on the rheology of rennet-induced casein
particle gels. Advances in Colloid and Interface Science, 98, 2550.
Morris, E. R., Gidley, M. J., Murray, E. J., Powell, D. A., & Rees, D. A. (1980).
Characterization of pectin gelation under conditions of low water activity,
by circular dichroism, competitive inhibition and mechanical properties.
International Journal of Biological Macromolecules, 2(5), 327330.
Morris, V. J. (1998). Gelation of polysaccharides. In S. E. Hill, D. A. Ledward,
& J. R. Mitchell (Eds.), Functional properties of food macromolecules (pp.
143226). Gaithersburg, MD: Aspen Publishers.
Normand, V. (1995). Comportement rheologique des gels de gelatine, relations
proprietes - structures. PhD thesis. Nancy I: Universite Henri Poincare.
Norton, I. T., & Frith, W. J. (2001). Microstructure deign in mixed biopolymer
composites. Food Hydrocolloids, 15, 543553.
Ralet, M.-C., Bonnin, E., & Thibault, J.-T. (2002). Pectins. In E. J. Vandamme,
S. De Baets, & A. Steinbuchel, Biopolymers. Polysaccharides from
eukaryotes (Vol. 6) (pp. 345380). Weinheim: Wiley.
Renard, D., Lavenant, L., Sanchez, C., Hemar, Y., & Horne, D. (2002). Heatinduced flocculation of microparticulated whey proteins (MWP); consequences for mixed gels made of MWP and b-lactoglobulin. Colloids and
Surfaces B: Biointerfaces, 24, 7385.
Renard, D., Robert, P., Faucheron, S., & Sanchez, C. (1999). Rheological
properties of mixed gels made of microparticulated whey proteins
and b-lactoglobulin. Colloids and Surfaces B: Biointerfaces, 12, 113121.
Renard, D., Robert, P., Garnier, C., Dufour, E., & Lefebvre, J. (2000). Gelation
by phase separation in a whey protein system: In-situ kinetics of
aggregation. Journal of Biotechnology, 79, 231244.
Renkema, J. M. S., Gruppen, H., & van Vliet, T. (2002). Influence of pH and
ionic strength on heat-induced formation and rheological properties of soy
protein gels in relation to denaturation and their protein compositions.
Journal of Agricultural and Food Chemistry, 50(21), 60646071.
Ruas-Madiedo, P., Hugenholtz, J., & Zoon, P. (2002). An overview of the
functionality of exopolysaccharides produced by lactic acid bateria.
International Dairy Journal, 12(23), 163171.

431

Sanchez, C., Pouliot, M., Renard, D., & Paquin, P. (1999). Uniaxial
compression of thermal gels based on microfluidized blends of WPI and
heat-denatured WPI. Journal of Agricultural and Food Chemistry, 47(3),
11621167.
Schmitt, C. (2000). Etude de la coacervation complexe entre la
b-lactoglobuline et la gomme dacacia en solution aqueuse. PhD thesis,
Nancy: INPL.
Scholten, E., Tuinier, R., Tromp, R. H., & Lekkerkerker, H. N. W. (2002).
Interfacial tension of a decomposed biopolymer mixture. Langmuir, 18,
22342238.
Tanaka, T. (1987). Gels. In A. Klingsberg, & R. Piccininni, Encyclopedia of
polymer science and engineering (Vol. 7) (p. 514). New York: Wiley.
Taylor, A.J. (2000). Personal communication, Dijon, October 2000.
Taylor, A. J., Besnard, S., Puaud, M., & Linforth, R. S. T. (2001). In vivo
measurement of flavour release from mixed phase gels. Biomolecular
Engineering, 17(45), 143150.
Utsumi, S., Matsumura, Y., & Mori, T. (1997). Structurefunction relationships
of soy proteins. In S. Damodaran, & A. Paraf (Eds.), Food proteins and
their applications (pp. 227292). New York: Marcel Dekker.
van de Velde, F., & de Ruiter, G. A. (2002). Carrageenan. In E. J. Vandamme,
S. De Baets, & A. Steinbuchel, Biopolymers. Polysaccharides from
Eukaryotes (Vol. 6) (pp. 245274). Weinheim: Wiley.
van de Velde, F., Rollema, H. S., Grinberg, N. V., Burova, T. V., Grinberg,
V. Y., & Tromp, R. H. (2002). Coil-helix transition of i-carrageenan as a
function of chain regularity. Biopolymers, 65(4), 299312.
Viebke, C., Piculell, L., & Nilsson, S. (1994). On the mechanism of gelation of
helix-forming biopolymer. Macromolecules, 27, 41604166.
Weel, K. G., Boelrijk, A. E., Alting, A. C., Van Mil, P. J., Burger, J. J.,
Gruppen, H., et al. (2002). Flavor release and perception of flavored whey
protein gels: Perception is determined by texture rather than by release.
Journal of Agricultural and Food Chemistry, 50(18), 51495155.
Weijers, M., Visschers, R. W., & Nicolai, T. (2002). Light scattering study of
heat-induced aggregation and gelation of ovalbumin. Macromolecules,
35(12), 47534762.
Zasypkin, D. V., Braudo, E. E., & Tolstoguzov, V. B. (1997). Multicomponent
biopolymer gels. Food Hydrocolloids, 11(2), 159170.