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www.ingentaselect.com=titles=02638762.htm Trans IChemE, Vol 81, Part A, October 2003

KEY FACTORS IN MEMBRANE EMULSIFICATION

S. BEROT1 , S. GIRAUDET 1 , A. RIAUBLANC 2 , M. ANTON2 and Y. POPINEAU1
1
Unité de Recherche sur les Protéines Végétales et leurs Interactions, Institut National de la Recherche Agronomique, Nantes, France
2
Laboratoire d’Etude des Interactions des Molécules Alimentaires, Institut National de la Recherche Agronomique, Nantes, France

I
n contrast to widely used emulsiŽ cation processes (high pressure homogenizers, rotor=
stator, etc.), emulsions can be made with mineral membranes in relatively low and
controlled shear conditions. In this system, the dispersed phase permeates through
membrane pores into the continuous phase circulating in the retentate loop. Droplets detach
from the membrane owing to the shearing of the continuous phase. This process produces only
a little heating, energy consumption is low. This is interesting both from economic and
technological points of view, because it may limit the denaturation of macromolecular
emulsiŽ ers. The in uence of some factors (membranes, working conditions, emulsiŽ ers) on
the droplet size of oil–water emulsions was studied. The sizes depended mainly on the
adsorption speed of emulsiŽ ers: emulsions were much Ž ner with emulsiŽ ers adsorbing quickly
at the interface, such as SDS (sodium dodecyl sulfate) than with emulsiŽ ers lowering the
interfacial tension more slowly, such as b-casein or 11S soya globulin. The membrane pore
size, the shear rate at the membrane surface and, to a lesser extent, the volume fraction of the oil
phase (between 0 and 30%) had also a signiŽ cant effect, unlike the oil  ux. The emulsions were
Ž ner and more stable than those obtained in the same conditions with a rotor=stator system.

Keywords: emulsiŽ cation; microporous membrane; casein; 11S globulin.

INTRODUCTION would be possible to process raw materials sensitive to great

Membrane emulsiŽ cation is a recent technique, developed
with the aim of preparing oil–water or water–oil emulsions
in controlled conditions (Schröder et al., 1998; Sotoyama
et al., 1999; Joscelyne and Trägardh, 2000). The mechanism
is based on the detachment in a circulating continuous phase
of droplets of dispersed phase which have been Ž ltrated by
permeation through pores of microŽ ltration membranes
(Figure 1).
Droplets grow at the surface of pores, distort and Ž nally
detach when they reach a certain size. This phenomenon
depends on the balance between forces which tend to detach
the droplets (the drag force from the circulation of con-
tinuous phase and the inertial force caused by the circulation
of dispersed phase through the pore) and the forces which
oppose this (interfacial forces).
It follows that the characteristics of the emulsions, parti-
cularly their size distribution, are in uenced by factors
bound to membranes (nature, hydrophobicity, pore size
and uniformity), working conditions (tangential velocity,
transmembrane pressure, dispersed phase  ux, volume
fraction of the dispersed phase, viscosity of the two
phases) and to emulsiŽ ers responsible for stabilizing the
emulsion (interfacial tension reduction, velocity of diffusion
to the interface).
This operation has many advantages, if compared with
other emulsiŽ cation techniques, such as low energy density
provided to the system: 103–106 vs. 105–108 J m¡3 for other
techniques (Joscelyne and Trägardh, 2000). Therefore, it
shear rates and=or high temperatures.
We have chosen in this study to examine the in uence of
several factors when producing oil–water emulsions con-
taining low volume fractions of oil, stabilized by a rapid
emulsiŽ er, SDS (sodium dodecyl sulfate): nominal pore size
of the membrane, wall shear stress and oil  ux. We have
used two proteins as macromolecular emulsiŽ ers: b-casein
and 11S soya globulin, at low then high oil volume fraction.
METHODS AND MATERIALS
Membrane EmulsiŽ cation Device
Aqueous solution (500 ml) containing the emulsiŽ er was
pumped (PFM10VRM rotary lobe pump, PCM, France) in
the retentate loop of a tangential microŽ ltration module
(Figure 2). The dispersed phase was pumped at a known
 ux from the permeate part of the module (307 piston pump,
Gilson, France) into the circulating retentate loop.
The module was equipped with a tubular membrane
(Pall-Exekia, France): 20 cm length, 7 mm inner diameter,
10 mm outer diameter. The a-alumina-based membranes
differed by their coating and their nominal pore size:
a-alumina (0.5 and 0.8 mm) or zirconium oxide (0.1 mm).
For some experiments, a stainless steel rod (5 mm diameter)
was put inside the tubular membrane in order to lower the
section and allow high tangential velocities, Vcis. Vcis
(m s¡1) was calculated from values of circulation  ow rate

1077
1078 BEROT et al.

Figure 1. Principle of membrane emulsiŽ cation (Pe, input pressure; Ps, output pressure; Pp, pressure on the permeate side of the membrane; Vcis, tangential
velocity of circulation of the continuous phase; Qh, dispersed phase  ow rate; Dp, nominal pore size of the membrane).

of continuous phase obtained with a Mag 2500 electromag- The Reynolds number was calculated as:
netic  ow-meter (Danfoss, France). The wall shear stress tw rVcis Dh
(Pa) was calculated by: Re ˆ (4)
Z
2
lrVcis
tw ˆ (1) where r is the density (kg m¡3), Dh the hydraulic diameter
2 and Z the viscosity in Pa s.
A Contraves LS40 rheometer was used for the determina-
where l is the friction factor correlation and r the density of tion of the viscosity of emulsions at 20¯ C. It was equipped
the emulsion (kg m¡3). l values were calculated depending
with a Couette geometry (DIN 412). The shear rates varied
on the Reynolds number (Re) (Tatoud et al., 1997): from 0 to 100 s¡1.
16 Experiments were performed at constant temperature
Re < 2000 l ˆ (2) (20¯ C). Three piezoresistive pressure transducers P21
Re
(Philips, France) measured respectively the input pressure
and Pe of the module, the output pressure Ps and the permeate
pressure Pp, so allowed the calculation of the transmem-
Re > 2000 l ˆ 0:0792Re¡0:25 (Blasius model) (3) brane pressure Ptm by:
Pe ‡ Ps
Ptm ˆ Pp ¡ (5)
2

Materials
The continuous phase was an aqueous solution of SDS
(Sigma, France) at 10 g l¡1 or aqueous solutions (from 0.2 to
5.0 g l¡1) of b-casein (Lactalis, France) or 11S soya globulin
produced from deoiled  akes according to the method of
Howard et al. (1983) slightly modiŽ ed. The dispersed phase
consisted in non washed sun ower oil (Lesieur, France).

Figure 2. Schematic diagram of the device (1, feed tank temperature
sensor; 2, circulation pump; 3, heat exchanger; 4, retentate outlet valve; 5,
inlet pressure transducer; 6, permeate outlet valve; 7, microŽ ltration module;
8, permeate pressure transducer; 9, outlet pressure transducer; 10, circula-
tion  ow rate; 11, oil feed tank; 12, oil HPLC pump; 13, cryostat).
Procedure
Two experimental screening designs were used, for
experiments with SDS and proteins. For the SDS screening
design, the experimental factors (Table 1) were the nominal
pore size of the membrane (0.1 and 0.5 mm), the wall shear
stress (Ž ve values from 5 to 132 Pa) and the oil  ow rate
(three values from 0.5 to 2.5 ml min¡1, giving  ux between
8.8 and 44.1 l h¡1 m¡2). The Ž nal oil volume fraction
was 5%.
For the protein screening design, the experimental factors
were the nominal pore size of the membrane (0.1 and
0.5 mm), the wall shear stress (four values from 5 to 93 Pa),

Trans IChemE, Vol 81, Part A, October 2003

 KEY FACTORS IN MEMBRANE EMULSIFICATION 1079

Table 1. Experimental factors.

two speeds, 100 at 25 frames per second and then 100 at
SDS Protein 1 frame per second. Interfacial tension was calculated by the
experiments experiments software apparatus by Ž tting the droplet shape with the
Membrane 0.1 0.1
Young–Laplace equation.
pore size (mm) 0.5 0.5
Concentration of 10 0.2
emulsiŽ er (g l¡1) 1 RESULTS
5
During emulsiŽ cation, the permeation of the apolar phase
Oil  ow rate 0.5 1.25
(ml min¡1) 1.25
through the hydrophilic membrane led to an increase of
2 the membrane resistance: it reached 0.18 £ 1012 and 1.62£
1012 m¡1 for the 0.5 and 0.1 mm membranes, vs. 0.04 £ 1012
Vcis tw Vcis tw
Shear (m s¡1) Re (Pa) (m s¡1) Re (Pa)
and 0.15 £ 1012 m¡1, respectively, when water permeated.
The cleaning procedure containing the sequence with apolar
1 1417 5 1 1417 5 solvents allowed a complete recovery of performance of the
2.2 3201 25 2.2 3201 25 membranes after each emulsiŽ cation.
3.4 4984 55 3.4 4984 55 The repeatability of experiments was measured using a
4.6 6756 93 4.6 6756 93
5.6 8230 132
triple point. The standard deviation of the results was less
than 1% for the membrane resistance average and than 5%
for the volume diameter averages of the droplets.
We neglected the effect of the variation of the surface
the protein content of the solution (three values from 0.2 to material (a-alumina and zirconium oxide) and considered
5 g l¡1). The oil  ow rate was 1.25 ml min¡1 (giving a  ux that the membranes differed only by their nominal pore size.
of 22.1 l h¡1 m¡2) and the oil volume fraction was 5%
(Table 1). Finally, emulsions stabilized by 11S globulin Emulsions with SDS
were produced with an oil volume fraction ranging from 7
to 32%. The results of the experimental screening design applied
At the end of the experiments, emulsions were recovered, to emulsions stabilized with 1% SDS show that, among the
then the retentate loop was cleaned by 15 min sequences of three factors studied (nominal pore size, wall shear stress
successively 1 M caustic soda at 70¯ C, ethanol, a 3:2 (v:v) and oil  ow rate), only the membrane nominal pore size
heptane:isopropanol mixture for the cleaning of the dis- signiŽ cantly in uenced the droplet sizes (Figure 3). On the
persed phase and Ž nally ethanol. opposite, the wall shear stress was signiŽ cant only for
The membrane resistances R (m¡1) were determined the 0.1 mm membrane: the higher tw, the lower d[4, 3],
before each experiment, after emulsion recovery and after particularly for tw up to 60 Pa corresponding to Re values
cleaning of the apparatus by: under 5000 (Table 1). This was not the case for the 0.5 mm
Ptm membrane (Figure 4). The in uence of the oil  ow rate was
Rˆ (6) not signiŽ cant (results not shown).
JZ
where J is the permeate  ux in m s¡1.
Emulsions with Proteins
All the four factors studied (type of protein, nominal pore
Droplet Size Analysis
size of the membrane, wall shear stress and concentration of
Emulsion droplet sizes and their distribution in numbers protein) had a signiŽ cant effect on the droplet sizes.
and volumes were determined with a Saturn Digisizer 5200
laser diffraction instrument (Micromeritics, France) without
dilution with a de occulation buffer. The volume average
d[4, 3] and the number average d[1, 0] diameters were
calculated. A dispersion factor was calculated as:
d90 ¡ d10
Dispersion ˆ (7)
d50
where di is the diameter under which i% of the droplets were
in the cumulative distribution. Some emulsions were photo-
graphed after examination with an Axioskop2 optic micro-
scope (Zeiss, France).

Interfacial Tension Kinetic

Interfacial tension kinetic was measured using a drop
tensiometer (Cam 200, KSV, Helsinki, Finland). An ascen-
dant drop of sun ower oil (5–10 ml) was produced in 0.5 s in
the solution containing emulsiŽ er (concentration 1 g l¡1). Figure 3. In uence of the nominal pore size of the membrane on averages
Images of the drop were recorded with a digital camera at d[4, 3] of emulsions stabilized by SDS 1%.

Trans IChemE, Vol 81, Part A, October 2003

1080
Figure 4. In uence of the wall shear stress on averages d[4, 3] of emulsions
stabilized by SDS 1%.
Emulsions stabilized by 11S globulins were Ž ner than those
stabilized by b-casein (Figure 5). For both proteins, emul-
sions were much coarser than those stabilized by SDS, and
they were rarely monodisperse. The effect of the membrane
nominal pore size was diminished when compared with SDS
emulsions (Figures 3 and 5). The protein content of the
solutions had a negative effect on the droplet sizes (Figure 6).
Lastly, the Ž ner emulsions were obtained at high wall shear
stress; this effect was more obvious than with SDS.
Emulsions at High Oil Volume Fraction
Emulsions containing up to 32% of dispersed phase were
prepared without any problem by microŽ ltration. The drop-
let sizes were still dependent on the wall shear stress
(Table 2) and the nominal pore size of the membrane, and
not signiŽ cantly dependent on the oil  ow rate (results not
shown). Increasing the volume fraction involved a greater
droplet size and a greater dispersion, mainly for volume
phases higher than 25% (Figure 7). Even at high oil volume
fraction, the greater the wall shear stress, the Ž ner the
droplets (results not shown).
Figure 5. In uence of the nominal pore size of the membrane on averages
d[4, 3] of emulsions stabilized by proteins.
BEROT et al.
Figure 6. In uence of the concentration in proteins and wall shear stress on
averages d[4, 3] of emulsions stabilized by proteins.
Table 2. In uence of tw on droplet sizes at high
oil volume fraction (24.2%).
tw (Pa) 12.5 25.3 41.9
d[4, 3] (mm) 12.2 7.2 5.0
Emulsions stabilized by 11S soya globulin
(0.2 mm membrane, concentration in 11S:
20 g l¡1, oil  ow rate 2 ml min¡1).
The resistance to coalescence of the emulsions was much
better than that of emulsions produced in the same con-
ditions (volume fraction 12%) with a Polytron PT-DA
3012=2TS rotor=stator system: only 6% of released oil vs.
80% after a centrifugation treatment equivalent to 104g
during 30 min.
Figure 7. In uence of the oil volume fraction on the size distribution (d[4, 3]
and dispersion) of droplets of emulsions stabilized by 11S soya globulin
(0.8 mm membrane; tangential velocity, 2.3 m s 1; concentration in 11S,
20 g l 1; oil  ow rate, 1 ml min 1).
Trans IChemE, Vol 81, Part A, October 2003
 KEY FACTORS IN MEMBRANE EMULSIFICATION
DISCUSSION
The difference in droplet size between emulsions stabi-
lized by a small molecule such as SDS and macromolecules
such as proteins has already been described (Schröder et al.,
1998). It is related to (i) the velocity of decreasing the
interfacial tension very high for SDS and (ii) the value of the
plateau of this interfacial tension, much lower for SDS
(Figure 8).
Nevertheless, the number distribution of the droplet sizes
of the emulsions shows that protein-stabilized emulsions
were mainly composed of sub-micronic droplets (conŽ rmed
by microscopic examination) and for a small proportion of
droplets having a very great diameter (Figure 9). These big
droplets were formed even at very small oil  ow rate
(experiences at 0.1 vs. 1.25 ml min¡1), although this low
oil  ux would allow proteins to stabilize droplets detaching
from the pore outlet. Probably, these big droplets were
created by coalescence of small droplets. This phenomenon
may be in relation with the shear applied to the emulsion
during the continuous circulation in the retentate loop,
either at the membrane surface or in the accidents of the
loop or in the circulation pump. In a same way, emulsions
can be destabilized in tangential microŽ ltration loops
(Hong et al., 2002).
The in uence of nominal pore size of the membrane on
the droplet size of emulsions is in accordance with Joscelyne
and Trägardh (1999). Nevertheless, this effect was much
less with proteins than with SDS.
The comparatively low efŽ cacy of b-casein vs. 11S
globulin for producing Ž ne emulsions may seem to be
paradoxical: (i) b-casein is a smaller protein (24 kg mol¡1
molecular mass vs. 360 kg mol¡1 for 11S globulin); and
(ii) this protein exhibits a marked amphiphilicity as its
sequence is divided into two halfs, one hydrophobic and
the other hydrophilic (Rollema, 1992).
However, both of the proteins diffuse at the interface not
as unique molecules, but probably as aggregates for 11S
globulin (they are responsible for the rigidiŽ cation of the
interfacial Ž lm, which is beneŽ cial for its stabilization) and
as 20–50 nm micelles for b-casein (Dickinson et al., 1999).
On the other hand, the decrease of the droplet size due to
shearing is in accordance with the results obtained by
Figure 8. Decrease of the interfacial tension by SDS and 11S soya globulin.
Trans IChemE, Vol 81, Part A, October 2003
1081
Figure 9. Droplet sizes (d[1, 0]) of emulsions stabilized by SDS, 11S soya
globulin and b-casein. Experimental conditions: 0.5 mm membrane; wall
shear stress, 93.3Pa; concentration in SDS, 10 g l 1; and in proteins
0.2 g l 1 (d[4, 3] were 2.26, 6.10 and 6.50 mm respectively for SDS, 11S
and b-casein).
Joscelyne and Trägardh (1999) on emulsions stabilized by
small emulsiŽ ers included in the dispersed phase.
The increase of droplet size in function of the protein
content of the solution may be judged as surprising. In fact,
only d[4, 3] was signiŽ cantly increased, whereas d[1, 0]
decreased. This evolution of d[1, 0] is in accordance with
many related results, showing that an increase of the
emulsiŽ er concentration tends to provoke a decrease of the
droplet size, due to a better resistance to coalescence, at least
for low concentrations; besides, at higher concentration,
there is often a plateau in the droplet size. The increase in
d[4, 3] may be related to the presence of not adsorbed
proteins in the form of aggregates or micelles (in a great
proportion considering the low oil volume fraction, 5%)
which induces depletion forces between emulsion droplets,
that favour their aggregation and Ž nally some coalescence
(Riaublanc et al., 2002).
CONCLUSION
In this work, we could quantify the contribution of several
factors to the recovery of Ž ne oil–water emulsions, stabi-
lized by emulsiŽ ers differing in their type. Both nominal
pore size of the membrane and shear rate greatly in uence
the droplet size of the emulsions, unlike the dispersed phase
 ux, in the range of 0–22 l h¡1 m¡2. Although protein stabi-
lized emulsions were coarser than those stabilized by
emulsiŽ ers which quickly lower the interfacial tension,
such as SDS, some noteworthy differences have been
measured depending on the type of macromolecule. Conse-
quently, some further studies must be done, according to two
directions:
the use of peptidic emulsiŽ ers, eventually functionalised,
which would decrease the interfacial tension more quickly
and in a greater proportion, and would make an interfacial
Ž lm stronger than those stabilized by small emulsiŽ ers;
the addition in the dispersed phase of a small lipophilic
emulsiŽ er: this would decrease capillarity forces inside
the membrane pores, therefore induce a lower transmem-
1082 BEROT et al.

brane pressure for a given  ux of dispersed phase, and Joscelyne, S.M. and Trägardh, G., 2000, Membrane emulsiŽ cation—a
litterature review, J Membrane Sci, 169: 107–117.
would lower the interfacial tension at the pore outlet, Riaublanc, A., Llamas, G., Lopez, C. and Brossard, C., 2002, In uence of
which could avoid the immediate coalescence of droplets. temperature on rheological properties of sodium caseinate stabilised
emulsions, Rec Res Dev Agric Food Chem Food Emuls Dispers, 41–48.
Rollema, H.S., 1992, Advanced Dairy Chemistry, 1: Proteins, Fox, P.F. (ed)
NOMENCLATURE (Elsevier, London, UK), p 111.
d[1, 0] number average diameter, mm Schröder, V., Behrend, O. and Schubert, H., 1998, Effect of dynamic
d[4, 3] volume average diameter, mm interfacial tension on the emulsiŽ cation process using microporous,
J permeate  ux, m s 1 ceramic membranes, J Colloid Interface Sci, 202: 334–340.
Pe input pressure, Pa Sotoyama, K., Asano, Y., Ihara, K., Takahashi, K. and Doi, K., 1999,
Pp permeate pressure, Pa Water=oil emulsions prepared by the membrane emulsiŽ cation method
Ps output pressure, Pa and their stability, J Food Sci, 64: 211–215.
Ptm transmembrane pressure, Pa Tatoud, L., Decloux, M., Nissan, N. and Liou, J.K., 1997, Mesure de la
R resistance of the membrane, m 1 contrainte pariétale dans les membranes tubulaires de différentes conŽ gu-
Re Reynolds number rations, Entropie, 207: 41–51.
Vcis tangential velocity, m s 1

Greek symbols
Z viscosity, Pa s ACKNOWLEDGEMENTS
l friction factor correlation The authors thank Pall-Exekia (France) for free providing of microŽ ltra-
r density, kg m 3 tion membranes. They thank Christian Blassel and Dominique Guibert for
tw wall shear stress, Pa their technical assistance.

REFERENCES
Dickinson, E., Golding, M. and Casanova, H., 1999, Food Emulsion and
Foams, Interfaces, Interactions and Stability, Dickinson, E. and
Rodriguez Patino, J.M. (ed) (Royal Society of Chemistry, Cambridge,
UK), p 327.
Hong, A.C., Fane, A.G. and Burford, R.P., 2002, The effects of intermittent
permeate  ow and cross ow on membrane coalescence of oil-in-water
emulsions, Desalination, 144: 185–191.
Howard, P.A., Lehnhardt, W.F. and Orthoefer, F.T., 1983, 7S and 11S
vegetable protein fractionation and isolation, US patent no. 4,368,151.
Joscelyne, S.M. and Trägardh, G., 1999, Food emulsions using membrane
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ADDRESS
Correspondence concerning this paper should be addressed to:
Dr S. Berot, Unité de Recherche sur les Protéines Végétales et leurs
Interactions, Institut National de la Recherche Agronomique, rue de la
Géraudière, 44316 Nantes cedex 3, France.
E-mail: berot@nantes.inra.fr
The paper was presented at the 9th Congress of the French Society of
Chemical Engineering held in Saint-Nazaire, France, 9–11 September
2003. The manuscript was received 20 March 2003 and accepted for
publication after revision 9 September 2003.

Trans IChemE, Vol 81, Part A, October 2003