Aerated Food Gels
Aerated Food Gels
Aerated Food Gels
Review
Introduction
Food gels are soft solids containing considerable
amounts of an aqueous phase (i.e., >80%) that have received
much attention lately among food scientists (Aguilera &
Rademacher, 2004; Hermansson, 2007; Nishinari, Zhang,
& Ikeda, 2000; Renard, van de Velde, & Visschers, 2006;
Totosaus, Montejano, Salazar, & Guerrero, 2002). The presence of gel-like structures is ubiquitous among most highmoisture processed foods: jellies, yogurt, processed meats,
etc. Air is also a component of several food products usually
present as a dispersed phase of bubbles or pores within a matrix. Air bubbles are abundant structural elements in solid
food foams, for example, bread, cakes, aerated chocolate
bars and meringue, in semi-solid foams such as whipped
* Corresponding author.
0924-2244/$ - see front matter 2007 Elsevier Ltd. All rights reserved.
doi:10.1016/j.tifs.2007.11.012
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177
extend the range of physical properties, to increase the interfacial area (at constant gas volume), to decrease syneresis and to disperse air (and possibly aromas) imperceptibly,
thus, reducing the caloric density. Air cells smaller than
80 mm would be largely unnoticeable to the eye. Bubbles
within a food increase crack-stopping (effectively enlarging
the radius of curvature of the crack tip), ductility and fracture toughness (Buckman & Viney, 2002; Vincent, 1998).
Control of bubble size and size distribution is a major challenge not yet achieved in industrial food processing. In conventional foaming methods, there is little control over the
formation of individual bubbles, therefore they are not uniformly distributed and the product presents a wide distribution of bubble sizes (including some large size outliers).
Decreasing the size of bubbles and avoiding polydispersity
would minimize the effect of buoyancy and the vertical
stratification of bubbles, thus giving a better appearance.
Monodispersed bubbles can greatly reduce Ostwald ripening by reducing the effective Laplace pressure difference
due to their similar size. From a scientific viewpoint monodispersed bubbles are useful in fundamental studies because
the interpretation of results is much simpler than for polydispersed populations (Yasuno et al., 2004). Alternatively,
bottom-up approaches can be used to incorporate gases
at the level of individual bubbles. Bulk (conventional)
and localized novel techniques to incorporate bubbles into
liquid or viscoelastic media are described schematically
in Fig. 1.
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Conventional
Novel
Bulk
Localized
gas
(a) Membrane
Bulk
+
(c) Electrochemical
sonotrode
Mechanical agitation
Fermentation
Chemical reaction
Orifice
liquid gas liquid
(b) Microdevices
(d) Ultrasound
Fig. 1. Conventional and novel mechanisms to incorporate bubbles in food (not at scale).
In membrane processes the energy-intensive, mechanically induced shearing is not required to create small bubbles and foaming is possible with an energy input orders of
magnitude smaller than in conventional methods (Boom,
2007). Hence, materials which are sensitive to localized
shear stresses such as proteins, are not affected to a large
extent (Bals & Kulozik, 2003a, 2003b; Charcosset et al.,
2004). However, if shear-induced protein denaturation or
liberation of substances is required to improve foaming,
shearing or heating may be done before membrane
processing.
In membrane processing, bubble diameter increases with
both gas flow rate and pore size (Bals & Kulozik, 2003a).
The porosity of the membrane surface is an important parameter because it determines the distance between two adjacent pores. This distance is critical to ensure that two
adjacent bubbles do not come sufficiently close to coalesce
(Charcosset et al., 2004). In SPG processing, mean diameters of microbubbles and polydispersity are larger for protein than for surfactant solutions (Table 1), probably due
to the different adsorption kinetics (Kukizaki & Goto,
2007).
The main limitation of the membrane process is a low
dispersed phase flux through the membrane associated
with monodispersed bubbles. However, membrane systems
are particularly suitable for large scale production because
they are easy to scale-up, by adding more membranes to
a module (Charcosset et al., 2004).
Microengineered devices
The application of micromachining techniques in nanotechnology has prompted the use of microfluidic devices
(MFDs). MFDs are process elements that deal with small
amounts of fluids (106e109 L) that flow in channels
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179
Process conditions
Continuous phase
Membranes
180e370
0.36e0.72
SDS, 0.3% wt
Tween 20, 1.0% wt
27.8
31.3
Sodium caseinate
solution, 1.0% wt
Bovine serum albumin
(BSA), 1.0% wt
39.5
SDS, 0.3% wt
33.6
39.1
48.9
Microchannel arrays
Microchannel dimension
(16 mm width 4 mm depth)
Spontaneous formation by
interfacial tension
41.1
51.1
5e120
w46
FF devices presents two main disadvantages for real industrial applications in which mass production of bubbles is
required: the gas fraction is limited to very small values and
the scale-up of these devices is a hard task due to the threedimensional centering of the injection needles with the exit
orifices (Gordillo et al., 2004).
Electrochemical reactions
Gas bubbles generated by electrochemical reactions
have attracted research interest in many disciplines. Since
electrochemical reactions occur primarily in aqueous solutions, gases like hydrogen and oxygen are usually generated
in the form of bubbles at the surface of electrodes (Fig. 1c)
(Wedin, Davoust, Cartellier, & Byrne, 2003; Zhang et al.,
2006). Gases detach from these surfaces as soon as the
buoyancy force overcomes the surface tension effects holding the bubble in place. Electrolysis can generate small
bubbles in the order of micro or nanometers (Lee, Sutomo,
Liu, & Loth, 2005; Wedin et al., 2003). Zhang et al. (2006)
using tapping mode AFM demonstrated that the formation
of bubbles at the surface of electrodes is a sequential
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process of formation, growth and coalescence of nanobubbles, followed by the release in the form of microbubbles.
Micro-fabrication of electrolytic bubble generators
could allow direct control of bubble size and size dispersion, release location and release frequency (Lee, Sutomo,
et al., 2005). Tuning the applied voltage or the reaction
time, the formation of nanobubbles and the release of microbubbles can be controlled (Zhang et al., 2006). In addition, some studies on electrochemically generated bubbles
have shown a decrease in bubble size and a narrower bubble size distribution with greater applied voltages and the
concomitant increase in gas production (Lee, Sutomo,
et al., 2005; Shin & Yiacoumi, 1997; Zhang et al., 2006).
Monodisperse bubbles with diameters within the range of
100 50 mm were formed by an electrochemical bubble
generator designed by Wedin et al. (2003). Lee, Sutomo,
et al. (2005) were able to produce microbubbles (100 mm
in diameter and 90% of the bubbles within 20 mm of the
mean diameter) by varying the area and spacing between
electrodes.
Although electrolytic bubble generators may prove practical at laboratory scale, they may not be viable at production levels due to high cost, low energy efficiency, etc.
Further development is needed before such devices become
practical for large scale applications requiring formation of
a cloud of bubbles (Lee, Sutomo, et al., 2005).
Ultrasound
Another way of creating microbubbles is acoustic cavitation (Fig. 1d) that implies the formation, growth, and implosive collapse of microscopic bubbles in liquids subjected
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Strong
Gel strength
Gellan
Soy protein isolate
Whey protein isolate
Weak
Brittle
Ductil
Type of fracture
181
182
Example
Basis of mechanism
Heat setting
Protein
Globular proteins
Unfolding or dissociation of native protein by heat exposing reactive sites. Unfolded molecules
associate and aggregate leading to the formation of the junction zones of the gel.
The mechanism is predominantly tailetail association via non-covalent bonding. Domains of the
molecule undergo a conformational change that exposes previously hidden amino acid side-chains
to the solvent, resulting in increased proteineprotein interactions allowing the formation of
junction zones.
During gelatinization of starch, amylose and amylopectin are released and become solubilized.
Upon cooling, the free amylose (single helices) become ordered into microcrystalline regions
surrounding swollen granules, forming the junction zones. Starch gels are composites of amylose
matrices filled with swollen granules.
Myosin
Polysaccharide
Starch
Cold setting
Protein
Polysaccharide
Gelatine
Agar
Junction zones created by partial reformation of the triple helices found in collagen during cooling.
When hot solutions are cooled below 40 C bundles of double or single helices are formed. These
helices are precursors of superjunctions of helices and of the junction zones.
High pressure
Protein
Globular proteins
Pressures above 200 MPa induce conformational changes leading to denaturation, aggregation and
formation of the junction zones. Particulate gels formed are stabilized mainly by hydrogen bonds,
although disulphide bonds may be present at higher pressures.
Ionic
Polysaccharide
Gellan gum
Formation of double helices followed by ion-induced association of the double helices to form the
junction zones.
Helical chains become associated of into double helices. Because of the anionic nature of the
molecule, carrageenans require counter-ions to form the junction zones.
Junction zones are regions of polyguluronic (alginate) or polygalacturonic acid (pectin) linked to
similar regions in another polymer chain by calcium ions (so-called eggbox arrangement).
The junction zones are aggregates of chains of various sizes promoted by hydrogen bonding and
hydrophobic interaction.
Carrageenans
Alginate, low methoxil pectin
High methoxil pectin
Cold gelation
Protein
Globular proteins
Soluble protein aggregates are prepared by heat treatment at a pH well above the isoelectric point
and in the absence of salts. After cooling, formation of junction zones is induced by lowering the
pH or adding salts.
Acid
Protein
Lowering the pH, changes the net charge of proteins and allows denaturation to form clusters or
aggregates. These clusters may be considered as the junction zones of the gel.
Upon acidification, colloidal calcium phosphate in the micelles is solubilized and aggregation of
the partly disintegrated micelles occurs due to charge neutralization. At temperatures above 10 C
junction zones and network structure is formed.
Casein
Enzymatic
Protein
Globular proteins
Casein
Formation of junction zones is based on the introduction of covalent cross-links between proteins
by the action of the enzyme transglutaminase.
Enzymatic hydrolysis of k-casein by the proteolytic enzyme chymosin releases the so-called
caseinomacropeptide (CMP) and causes the casein micelles to destabilize and aggregate to form
the junction zones and lead to a particle gel (curd).
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Types
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183
Fig. 4. Nomenclature of gels based on the type and number of phases forming their structure.
Table 3. Examples of the effect of adding a second polymer on selected properties of mixed gelsa
Ratiob
System
Property
Firmness
1.7e1.9
Elastic modulus
1.1e1.3
Hardness
1.5e2.2
Hardness
0.34e0.77
0.84e1.59
Shear modulus
1.43e2.29
Syneresis
0.25e0.86
Youngs modulus
0.54e0.94
Force at fracture
Strain at fracture
1.33e1.86
1.12e1.39
a
b
References
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Conclusions
Gels are ubiquitous structures in high-moisture foods.
The ample availability of edible gelling materials and the
improved properties of mixed systems and emulsion gels
provide a wealth of opportunities for the design of simple
or complex structures with tailored properties. Introducing
a gaseous phase in the form of bubbles or open pores may
increase the spectrum of possibilities for texture formation
and perception, flavor encapsulation and/or release, delivery of bioactive molecules, control of satiety and creation
of gastronomic structures. New technologies that allow
control of the elements in the dispersed phase at the micron
scale are actively explored to make better aerated
structures.
Acknowledgments
Work on aerated gels is financed by the National Committee for Science and Technology (Chile) FONDECYT
project 1060713.
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