G Model

ARTICLE IN PRESS

SUPFLU-3343; No. of Pages 8

J. of Supercritical Fluids xxx (2015) xxxxxx

Contents lists available at ScienceDirect

The Journal of Supercritical Fluids

journal homepage: www.elsevier.com/locate/supflu

Development of egg white protein aerogels as new matrix material

for microencapsulation in food
Ilka Selmer a, , Christian Kleemann b , Ulrich Kulozik b , Stefan Heinrich c , Irina Smirnova a
a

Institute for Thermal Separation Processes, Hamburg University of Technology, Eiendorfer Strae 38, 21073 Hamburg, Germany
Chair for Food Process Engineering and Dairy Technology, Research Center for Nutrition and Food Sciences (ZIEL)-Department Technology, Technische
Universitt Mnchen, Weihenstephaner Berg 1, 85354 Freising-Weihenstephan, Germany
c
Institute of Solids Process Engineering and Particle Technology, Hamburg University of Technology, Denickestrae 15, 21073 Hamburg, Germany
b

a r t i c l e

i n f o

Article history:
Received 16 February 2015
Received in revised form 24 May 2015
Accepted 25 May 2015
Available online xxx
Keywords:
Aerogel
Food
Egg white
Protein
Irreversible heat coagulation

a b s t r a c t
Egg white protein hydrogels formed by heat coagulation were used to obtain aerogel structures by supercritical drying. Hydrogels were prepared from pasteurized and spray-dried egg white at different pH, ionic
concentrations and protein content to modify the characteristics of the dried protein network. The largest
BET-surface areas were found at low and high pH, the most mechanically stable aerogels at alkaline pH.
It was shown that the protein network is preserved during supercritical drying. Egg white as precursor for
aerogels opens a new eld of application for those proteins as microencapsulation material for sensitive
or unpleasant tasting food additives.
2015 Elsevier B.V. All rights reserved.

1. Introduction
During the last years, a lot of research has been done on natural polysaccharide-based aerogels, which fulll the requirements
for food applications [1]. In principal, supercritical drying of an
alcogel to an aerogel is an extraction of a solvent from a gel by
supercritical carbon dioxide. The rafnate is represented by the
aerogel. Extraction by supercritical carbon dioxide has become a
well-established process in the food industry over the last years
[2,3], indicating that there should be a potential to establish foodgrade aerogels in industry, too. In this study, the irreversible heat
coagulation of egg white proteins is used to form a gel which is
afterwards supercritically dried to an aerogel. Aerogels based on
natural proteins can provide new opportunities for life science and
food applications because of their biocompatibility and biodegradability. Particularly hen egg white, which has been used for this
study, is well-known as staple food and, therefore, most reliable
for potential consumers. The general applicability of egg white protein as precursor for aerogels has already been shown by Kistler [4].

Corresponding author. Tel.: +49 40 42878 2846.

E-mail addresses: ilka.selmer@tuhh.de (I. Selmer), christian.kleemann@tum.de
(C. Kleemann), ulrich.kulozik@tum.de (U. Kulozik), stefan.heinrich@tuhh.de
(S. Heinrich), irina.smirnova@tuhh.de (I. Smirnova).

Furthermore, whey protein isolate out of milk [5,6] or soy protein

isolate [7] were investigated as food grade aerogel precursors.
Egg white protein is a high quality protein source with high
nutritive value. It offers versatile functional properties, for example foaming, emulsication, water-binding and heat coagulation
[812]. Therefore, it is widely used in the food industry [8,12].
Native egg white consists of about 10 wt% protein and 90 wt% water
[9]. The main protein fractions of egg white are Ovalbumin (54%);
Ovotransferrin (12%) and Ovomucid (11%) [13]. When egg white is
heated, the egg white proteins denature thermally and form a gel.
This process is described as a 3-step mechanism: rstly, due to heat,
the existing hydrogen bonds in particular between the polypeptide
chains of the protein molecule break, the polypeptide chains unfold
and hydrophobic reactive groups get exposed to the outside of the
protein [9,11]. As a second step, the unfolded protein molecules
rearrange due to hydrophobic and electrostatic interactions. Intermolecular disulde crosslinking stabilizes the arranged protein
network additionally. A gel is generated. Thirdly, the formed gel is
cooled and gets more elastic because of the formation of hydrogen
bonds, which stiffen the protein network [9,11,14]. The resulting
gel structure is inuenced by pH and ionic strength and the type of
added salt [10,15].
The main objective of this study was to develop protein-based
aerogels out of egg white as carrier material for food applications. The main requirements for such a carrier material consist of
high specic surface area coupled with high mechanical stability.

http://dx.doi.org/10.1016/j.supu.2015.05.023
0896-8446/ 2015 Elsevier B.V. All rights reserved.

Please cite this article in press as: I. Selmer, et al., Development of egg white protein aerogels as new matrix material for microencapsulation in food, J. Supercrit. Fluids (2015), http://dx.doi.org/10.1016/j.supu.2015.05.023

G Model
SUPFLU-3343; No. of Pages 8

ARTICLE IN PRESS
I. Selmer et al. / J. of Supercritical Fluids xxx (2015) xxxxxx

Therefore, the inuence of pH, temperature, sodium chloride concentration and egg white source on the resulting aerogel structure
was investigated.
2. Materials and methods
2.1. Materials
Pasteurized egg white and dried egg white powder were
kindly donated from Ovobest Eiprodukte GmbH & Co., KG
(Neuenkirchen-Vrden, Germany). Sunower oil was provided
from Brckelmann + Co Oelmhle GmbH + Co (Hamm, Germany).
Sodium Chloride (purity 99%) was purchased from Carl Roth
GmbH & Co., (Karlsruhe, Germany). Ethanol of analytical grade was
purchased from Krayem GmbH (Ingoldstadt, Germany) and Merck
KGaA (Darmstadt, Germany). Carbon dioxide of food grade was
obtained from Yara GmbH & Co., KG (Dlmen, Germany).
2.2. Methods
2.2.1. Preparation of egg white protein gel samples
Commercially available pasteurized egg white was utilized as
primary aqueous protein solution. Alternatively, a solution of dried
egg white powder was prepared with deionized water, stored
at 4 C over night to allow for complete hydration and its protein content was adjusted to 10 and 15 wt%. The protein content
was determined using the method of Dumas with an accuracy of
0.1 wt% (Vario MAX CUBE, Elementar Analysensysteme GmbH,
Hanau, Germany). The protein content of the powder solutions was
determined for every new solution, the protein content of the pasteurized egg white randomly for new packages. The pH-values were
adjusted with hydrochloric acid and sodium hydroxide to 2, 3.5, 4.6,
7, 9, and 11.5. To investigate the sodium chloride inuence on the
gel structure, additionally, sodium chloride was added to the liquid
egg white in concentrations of 5 and 400 mmol/L in crystalline form
and dissolved completely. The egg white protein solutions were
then immersed dropwise into hot sunower oil with a temperature
of 80 and 90 C, using a 0.9 mm syringe. After a time interval of 10
and 5 min, respectively, the hardened gel spheres were transferred
into sunower oil at room temperature for cooling. Gel spheres
were dabbed with a lint free tissue to take away the major part of
oil residue. The remaining small oil amounts on the surface of the
gel spheres were dissolved in ethanol and removed during solvent
exchange. For each variation, 20 gel spheres were produced.
2.2.2. Solvent exchange and supercritical drying of egg white gels
The solvent exchange from water to ethanol was started directly
after gelation to avoid altering effects of the gel structure. The
gels were put into 99.8% ethanol to mix the pore lling water
inside the gels with ethanol. An ethanol to gel volume ratio of 50
was used. After 24 h, the gels were put into fresh ethanol. This
was repeated at least three times to reach at least 97 wt% in the
gel surrounding ethanolwater mixture. The ethanol concentration was measured indirectly by measuring the density of the
ethanolwater mixture at 20 C (Density Meter DMA 4500 M, Anton
Paar, Ostldern-Scharnhausen, Germany).
The supercritical drying was conducted at 12 MPa and 40 C in
a 250 mL autoclave for three hours using a continuous supercritical CO2 ow (Fig. 1). At 12 MPa and 40 C the system CO2 -ethanol
is in the single phase region [16], and therefore, no phase boundary leading to capillary forces inside the gel could occur. Also the
drying temperature was below the denaturation temperature of
the egg white proteins [17] to avoid further changes of the protein
structure.
First, the autoclave was heated to 40 C by a thin electrical
band heater. The alcogels were packed in lter paper, placed into

Fig. 1. Process ow diagram of the equipment used for the supercritical drying of protein aerogels. Tags: V1V7 = valves; HE1 = heat exchanger for heating;
P1 = compressor; A1 = 250 mL autoclave with sapphire window; S1 = separator;
PI = pressure gauges; SV1 = safety valve; TI = thermocouple; FI = ow meter.

the autoclave (A1 in Fig. 1) and soaked in ethanol to prevent

shrinkage due to evaporation of ethanol from the alcogel network
before exposure to supercritical CO2 . The system was pressurized
to 11.012.0 MPa with CO2 by a compressor (P1). The outlet regulating valve V7 was adjusted to a ow of CO2 of 24 NL/min,
continuous CO2 ow was provided for 3 h. Finally, the pressure was
released slowly within 4060 min at constant temperature (40 C)
until atmospheric pressure was reached.

2.2.3. Physical characterization

Scanning electron micrographs of the samples were done at
5 kV using a detector for secondary electrons (Leo Gemini Zeiss
1530, Oberkochen, Germany). To analyze the internal structure of
the aerogel spheres, the samples were crushed into smaller pieces
which were then investigated. To avoid charging of the samples,
they were sputtered with gold (7 nm thickness).
Low temperature N2 adsorptiondesorption analysis was used
to investigate the physical properties of the aerogels (Nova
3000e Surface Area Analyzer, Quantachrome Instruments, Boynton Beach, USA). The specic surface area was determined
using the BET (BrunauerEmmetTeller) method. The pore volume and mean pore diameter were estimated by the BJH
(BarrettJoynerHalendia) method. All samples were degassed
under vacuum at 40 C for 20 h prior to analysis.
Bulk density was calculated from measured weight with a deviation of 0.0001 g and from measured diameter of the aerogel
spheres with an accuracy of 0.05 mm. The measurements were
repeated ve times with different aerogel spheres.
Breaking and compression tests were done to analyze the
mechanical stability (Texture Analyzer TA.XT plus, Stable Micro
Systems, Godalming, UK). The spherical samples were compressed
uniaxially to 8% strain or rather to the rst fracture of the structure
(0.01 mm/s test speed). In order to analyze the dry aerogel structure, the samples were dried additionally for 10 h under vacuum at
50 C and then stored in an exicator with silica gel particles inside.
The mechanical tests were done inside a tempered room (T = 20 C).
Each sample was measured directly after taken out of the exicator.
Five replicates for each test were done.

Please cite this article in press as: I. Selmer, et al., Development of egg white protein aerogels as new matrix material for microencapsulation in food, J. Supercrit. Fluids (2015), http://dx.doi.org/10.1016/j.supu.2015.05.023

G Model
SUPFLU-3343; No. of Pages 8

ARTICLE IN PRESS
I. Selmer et al. / J. of Supercritical Fluids xxx (2015) xxxxxx

Fig. 2. SEM pictures of aerogels from pasteurized egg white protein at different pH and gelation temperatures (5 kV, magnication: 40,000).

Please cite this article in press as: I. Selmer, et al., Development of egg white protein aerogels as new matrix material for microencapsulation in food, J. Supercrit. Fluids (2015), http://dx.doi.org/10.1016/j.supu.2015.05.023

G Model
SUPFLU-3343; No. of Pages 8

ARTICLE IN PRESS
I. Selmer et al. / J. of Supercritical Fluids xxx (2015) xxxxxx

Error analysis was done using student-t-distribution with a signicance level of 95%. N2 adsorptiondesorption analysis was done
only once with all 20 aerogel spheres to achieve the highest accuracy. Therefore, the error was estimated with 10%.

3. Results and discussions

3.1. Inuence of pH and gelation temperature on aerogel
structure
The structure of heat-induced egg white gels is inuenced by the
pH-value during gelation [10]. Therefore, gels were prepared at pH
2, 3.5, 4.6, 7, 9 and 11.5 to obtain egg white aerogels with different
structural properties. The gel samples were spherical with a very
smooth surface when the pH was 7 or 9. At pH 2, 3.5 and 4.6, the surface was slightly structured. At pH 11.5, the gel spheres appeared
transparent and very stable. The resulting inner structures of these
aerogels are shown in Fig. 2. The effect of the pH is clearly visible.
At a pH lower and higher than the isoelectric point of the main
protein Ovalbumin (pH 4.6), the structure of the aerogels appears
dense, homogeneous and well cross-linked, whereas the structure
of gels that were generated at pH-values near the isoelectric point
is coarser and appears to be formed by aggregation of spherical
subunits. This tendency is in accordance with Handa et al.s investigations of the pH-inuence on the hydrogel produced by egg
coagulation [10]. During heat denaturation of egg white proteins
the native globular proteins unfold partially, existing hydrogen
bonds break and otherwise hidden hydrophobic thiol-groups get to
the outer surface of the protein molecule [9,11,14]. Following the
unfolding process, the protein molecules rearrange and aggregate,
building intermolecular -sheets due to hydrophobic interactions
[9]. The resulting gel stiffens by sulfhydryl-disulde-interchanges
[14]. During network formation, high protein net charges (at low
or high pH) induce strong repulsive forces between the protein
molecules and slow down the aggregation process of the molecules.
This leads to an increased ratio of unfolded protein molecules, as
there is more time to unfold before the aggregation occurs [15]. A
dense homogeneous network is formed as shown for the aerogels
coagulated at pH 2, 3.5, 9 and 11.5 (see Fig. 2). At the isoelectric point, the aggregation process takes place unhindered due to
a lack of electrostatic repulsion between the protein molecules,
which leads to fast aggregation with a lower quantity of unfolded
molecules [15]. Additionally, partly positive and partly negative
charged protein subunits attract each other and generate many
aggregates resulting in a more coarse and heterogeneous network.
This corresponds particularly to the aerogel structure coagulated
at pH 4.6 (see Fig. 2).
Changing the gelation temperature from 80 C to 90 C inuences, the aerogel structure not signicantly. Therefore, the
temperature dependence is not further discussed.
Fig. 3 indicates a strong pH-dependence for the specic surface
areas (BET-surface areas) of the aerogels. The highest specic surface area of 380 m2 /g is reached at pH 2, the lowest specic surface
area of 16 m2 /g at pH 4.6 close to the isoelectric point. In general,
the specic surface area for a ne structured network (at low and
high pH values) is larger than for aggregated molecules (pH near
the isoelectric point), since the ne structured network contains a
large amount of pores with smaller diameters (Fig. 3).
Figs. 4 and 5show the pore size distribution and the pore volume
of the investigated egg white aerogels in dependence of pH.
Both diagrams are limited to the pore diameter range of
3200 nm (based on limitations in nitrogen absorption measurements), covering the mesoporous and part of the macroporous
region. The corresponding bulk densities are given in Fig. 6.

Fig. 3. BET-surface area of aerogels from pasteurized egg white protein at different
pH and gelation temperatures.

Fig. 4. Pore size distribution of aerogels out of pasteurized egg white proteins in
dependence of pH, gelled at 80 C (pore diameter range: 3200 nm).

Fig. 5. Pore volumes of aerogels based on pasteurized egg white proteins as a function of pH values and temperature (pore diameter range: 3200 nm).

Obviously, the gelation near the isoelectrical point leads to

dense aerogels with low pore volume, whereas the gelation at
low pH results in low density and high porosity in the mesoporous range (Figs. 4 and 5). Gelation under alkaline conditions
leads to formation of small mesopores; and therefore, decreases
the pore volume (within the pore diameter range 3200 nm)
(Figs. 4 and 5). At pH 4.6, the bulk density (covering micro-, mesoand macroporosity) and the pore volume (within the pore diameter range 3200 nm) is the lowest in comparison to the other
samples, which is contradicting (Figs. 5 and 6). The only possible
explanation would be the presence of the micro- or macropores, which are not accessible by the used nitrogen adsorption
measurement technique. A necessary assumption of this consideration would be a skeletal density independent from pH. The

Please cite this article in press as: I. Selmer, et al., Development of egg white protein aerogels as new matrix material for microencapsulation in food, J. Supercrit. Fluids (2015), http://dx.doi.org/10.1016/j.supu.2015.05.023

G Model
SUPFLU-3343; No. of Pages 8

ARTICLE IN PRESS
I. Selmer et al. / J. of Supercritical Fluids xxx (2015) xxxxxx

Fig. 6. Bulk density of aerogels out of pasteurized egg white protein gelled at 80 C
or 90 C and at different pH-values.

electron microscope images (see Fig. 2) conrm this consideration,

as the gures of pH 4.6 show macropores with diameters up to
1 m.
Overall, it is shown that it is possible to generate different protein aerogel structures by changing only the pH of the primary
aqueous protein solution. No additional cross-linker is needed.
Moreover, the shown SEM images of the egg white aerogels at
different pH are in accordance with Handa et al.s images of egg
white hydrogels at similar pH values [10]. This leads to the assumption that the protein network is not signicantly inuenced by
supercritical drying and can be well preserved in the form of
aerogels.

Fig. 8. BET-surface area of aerogels out of pasteurized egg white protein at different
pH and sodium chloride concentrations (coagulated at 80 C).

3.2. Inuence of sodium chloride on aerogel structure

The structure of heat-induced egg white gels can be inuenced
by the presence of salts [15]. In this study, the effect of sodium
chloride on the aerogel structure was investigated, for this purpose
sodium chloride was added before the coagulation of pasteurized
egg. The resulting gels were supercritically dried and analyzed. The
electron micrographs of these aerogels are shown in Fig. 7.
The higher the sodium chloride concentration is, the more pores
are observed leading to the coarser visible structure. These results
are in accordance with Croguennec et al.s investigations to the salt
impact on egg white hydrogel structures [15].

Fig. 7. SEM pictures of aerogels out of pasteurized egg white protein at different pH and sodium chloride concentrations (5 kV, magnication: 40,000).

Please cite this article in press as: I. Selmer, et al., Development of egg white protein aerogels as new matrix material for microencapsulation in food, J. Supercrit. Fluids (2015), http://dx.doi.org/10.1016/j.supu.2015.05.023

G Model
SUPFLU-3343; No. of Pages 8
6

ARTICLE IN PRESS
I. Selmer et al. / J. of Supercritical Fluids xxx (2015) xxxxxx

Fig. 9. SEM pictures of spray-dried egg white aerogels coagulated at 80 C for 10 min (5 kV, magnication: 40,000).

Fig. 8 shows that the BET-surface area of aerogels decreases with

increasing sodium chloride concentration, especially at pH 2 and
11.5. The charges of the protein molecule are shielded by salt ions
resulting in a reduction of the intermolecular repulsive forces and
faster aggregation with less unfolded [15] and less ordered protein molecules. Thus, more heterogeneous protein structures with
large aggregates, large pores and low surface area are formed at
high sodium chloride concentrations. This effect is comparable with
the observation at pH-values near the isoelectric point. Thus, the
net charge of the molecules is most relevant for the nal aerogel
structure, which is either balanced by an equal number of positive
and negative charges within the molecule or shielded by ions in
the solution. Both situations enhance the formation of aggregated
protein structures.
3.3. Inuence of egg white source and protein concentration on
aerogel structure
Towards the further applications of the investigated aerogels, it
is important to ensure the availability of the raw materials for their
production.

Two main egg white sources are available on the market: pasteurized and spray-dried egg white. Spray-dried egg white is more
expensive, but has the particular advantage: the protein content
of the primary aqueous solutions can be chosen freely, whereas
in case of the pasteurized egg white it is xed (10 wt%). In order
to investigate the inuence of the protein concentration on the
aerogel structures, gels out of spray-dried egg white powder were
produced. The protein concentration in the aqueous solution was
adjusted either to 10 or to 15 wt%. Analogous to the previous study
with egg white the pH values, the temperature and the duration of
the gelation were varied. These aerogels were compared with the
aerogels out of pasteurized egg white (Figs. 2 and 9).
At pH 4.6 and 7, the aerogel structure from spray-dried egg
white is denser, better connected and less pH dependent in comparison to that of pasteurized egg white (Figs. 2 and 9). Comparing
the protein content of the primary solution, the structures of the
aerogels from 15 wt% solution do not differ signicantly from aerogels with 10 wt% protein. With 15 wt% protein and a pH of 3.5,
spontaneous gel formation was observed before heat treatment
was applied. Therefore, no samples could be prepared with the
described method.

Please cite this article in press as: I. Selmer, et al., Development of egg white protein aerogels as new matrix material for microencapsulation in food, J. Supercrit. Fluids (2015), http://dx.doi.org/10.1016/j.supu.2015.05.023

G Model
SUPFLU-3343; No. of Pages 8

ARTICLE IN PRESS
I. Selmer et al. / J. of Supercritical Fluids xxx (2015) xxxxxx

Fig. 12. Compression test curve.

Fig. 10. BET-surface areas of aerogels from spray-dried egg white in comparison to
pasteurized egg white.

Fig. 13. Stiffness of aerogels out of pasteurized egg white depending of pH.
Fig. 11. Pore volumes of aerogels from spray-dried and pasteurized egg white in
dependence of pH and temperature (pore diameter range: 3200 nm).

Specic surface areas of spray-dried egg white aerogels are

higher than those of pasteurized egg white aerogels, especially near
the isoelectric point (Fig. 10).
Since dried egg white has a higher impact of heat due to the
production process than pasteurized egg white [17], it is assumed
that it leads to an increased ratio of partially unfolded ovalbumin molecules [9,14,18]. With more unfolded proteins, stronger
interactions of protein molecules take place independently of the
pH-value. Therefore, a better connected protein network with
smaller pores and higher specic surface areas is created. This
assumption is conrmed by the comparison of the pore volumes
of the spray-dried and pasteurized egg white aerogels, shown in
Fig. 11.
The volume of mesopores and small macropores increases due
to the higher degree of denaturation of the egg white, because
smaller pores are formed due to better crosslinking of protein
molecules.
Overall, spray-dried egg white powder should be only used as
protein source, if the gelation needs to be done at a pH close to the
isoelectric point of ovalbumin. In all other applications the cheaper
pasteurized egg white can be used to get aerogels with high BETsurface areas.
3.4. Mechanical stability
For future application, it is important that the aerogels are
stable enough to stay undamaged during transportation and storage. Therefore, the mechanical stability of all aerogel samples was
investigated. Two uniaxial compression tests were performed: (a)
spherical aerogels were compressed and decompressed without

Fig. 14. Breakage force of aerogels out of pasteurized egg white depending on pH.

breakage to investigate the deformation behavior and (b) spherical aerogels were compressed up to the primary breakage point to
obtain the breakage behavior (Section 2.2.3). Fig. 12 shows a typical
compression test curve without breakage.
All investigated compression tests showed a nearly linear forcedistance curve during compression. Therefore, the slope of the
compression curve is assumed as a measure for the stiffness [19]:
the larger the slope the stiffer is the investigated aerogel.
The stiffness and the primary breakage point of the pasteurized
egg white aerogels depends on the pH value (Figs. 13 and 14).
Aerogels gelled at low and high pH showed relatively high stiffness resulting from dense, well-connected structures with small
pores (see Section 3.1), whereas aerogels, which gelled close to
the isoelectric point of the main protein ovalbumin were very
soft, due to less connected aggregate structures (see Section 3.1).
For the breaking behavior, it is assumed that the reactivity of the

Please cite this article in press as: I. Selmer, et al., Development of egg white protein aerogels as new matrix material for microencapsulation in food, J. Supercrit. Fluids (2015), http://dx.doi.org/10.1016/j.supu.2015.05.023

G Model
SUPFLU-3343; No. of Pages 8

ARTICLE IN PRESS
I. Selmer et al. / J. of Supercritical Fluids xxx (2015) xxxxxx

hydrophobic thiol-groups increases with increasing pH. Therefore,

the number of sulfhydryl-disulde interchanges increases as well,
leading to a more viscoelastic protein network with larger breaking
forces [10].
4. Conclusions
Aerogels based on egg white proteins were successfully prepared by gelation of pasteurized and spray-dried egg white
solutions and subsequent supercritical drying. It was proven that
the structure of the aerogels is well preserved during the drying
step. The porosity and surface area of the aerogels can be tailored
by controlling the pH and ionic strength of the solution during the
gelation process. In order to produce mechanically stable aerogels
with high surface areas, pH values above the isoelectrical point
should be used. These aerogels are principally suitable for food
applications, for instance as carrier materials. Our ongoing research
shall reveal whether the high surface area of egg white protein aerogel matrix is suitable for impregnation with active substances and
give information about shelf life and their applicability in different
food systems.
Acknowledgements
This research project was supported by the German Ministry of
Economics and Energy (via AiF) and the FEI (Forschungskreis der
Ernhrungsindustrie e.V., Bonn). Project AiF 17485 N. Additionally, I. Selmer was supported by a doctoral scholarship from Pro
Exzellenzia (City of Hamburg).
References

[3] J.W. King, Modern supercritical uid technology for food applications, Annu.
Rev. Food Sci. Technol. 5 (2014) 215238.
[4] S.S. Kistler, Coherent expanded-aerogels, J. Phys. Chem. 36 (1931) 5264.
[5] M. Betz, C. Garca-Gonzlez, R.P. Subrahmanyam, I. Smirnova, U. Kulozik,
Preparation of novel whey protein-based aerogels as drug carriers for life
science applications, J. Supercrit. Fluids 72 (2012) 111119.
[6] H.-B. Chen, Y.-Z. Wang, D.A. Schiraldi, Foam-like materials based on whey
protein isolate, Eur. Polym. J. 49 (2013) 33873391.
[7] J.C. Arboleda, M. Hughes, L.A. Lucia, J. Laine, K. Ekman, O.J. Rojas, Soy protein
nanocellulose composite aerogels, Cellulose 20 (2013) 24172426.
[8] T. Strixner, U. Kulozik, Egg proteins, in: G. Phillips, P. Williams (Eds.),
Handbook of Food Proteins Woodhead Publishing Series in Food Science,
Technology and Nutrition Woodhead Publishing, Cambridge, 2011, pp.
150209.
[9] Y. Mine, Recent advances in the understanding of egg white protein
functionality, Trends Food Sci. Technol. 6 (1995) 225232.
[10] A. Handa, K. Takahashi, N. Kuroda, G.W. Froning, Heat-induced egg white gels
as affected by pH, J. Food Sci. 63 (1998) 403407.
[11] C.-Y. Ma, J. Holme, Effect of chemical modications on some physicochemical
properties and heat coagulation of egg albumen, J. Food Sci. 47 (1982)
14541459.
[12] L. Campbell, V. Raikos, S.R. Euston, Modication of functional properties of
egg-white proteins, Food 47 (2003) 369376.
[13] L. Stevens, Egg white proteins, Comp. Biochem. Physiol. B: Comp. Biochem.
100 (1991) 19.
[14] Y. Mine, T. Noutomi, N. Haga, Thermally induced changes in egg white
proteins, J. Agric. Food Chem. 38 (1990) 21222125.
[15] T. Croguennec, F. Nau, G. Brul, Inuence of pH and salts on egg white
gelation, J. Food Sci. 67 (2002) 608614.
[16] C.J. Chang, K.-L. Chiu, C.-Y. Day, Densities and P-x-y diagrams for carbon
dioxide dissolution in methanol, ethanol, and acetone mixtures, J. Supercrit.
Fluids 12 (1998) 223237.
[17] H.-D. Belitz, W. Grosch, P. Schieberle, Food Chemistry, 4th ed.,
Springer-Verlag, Berlin, 2009.
[18] N. Matsudomi, H. Takahashi, T. Miyata, Some structural properties of
ovalbumin heated at 80 C in the dry state, Food Res. Int. 34 (2001)
229235.
[19] S. Antonyuk, S. Heinrich, J. Tomas, N.G. Deen, M.S. van Buijtenen, J.A.M.
Kuipers, Energy absorption during compression and impact of dry
elastic-plastic spherical granules, Granular Matter 12 (2010) 1547.

[1] K.S. Mikkonen, K. Parikka, A. Ghafar, M. Tenkanen, Prospects of

polysaccharide aerogels as modern advanced food materials, Trends Food Sci.
Technol. 34 (2013) 124136.
[2] G. Brunner, Supercritical uids: technology and application to food
processing, J. Food Eng. 67 (2005) 2133.

Please cite this article in press as: I. Selmer, et al., Development of egg white protein aerogels as new matrix material for microencapsulation in food, J. Supercrit. Fluids (2015), http://dx.doi.org/10.1016/j.supu.2015.05.023