Bioscience, Biotechnology, and Biochemistry

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Effects of Lecithin Addition in Oil or Water Phase

on the Stability of Emulsions Made with Whey
Proteins

Yukiko Yamamoto & Megumi Araki

To cite this article: Yukiko Yamamoto & Megumi Araki (1997) Effects of Lecithin Addition in Oil or
Water Phase on the Stability of Emulsions Made with Whey Proteins, Bioscience, Biotechnology,
and Biochemistry, 61:11, 1791-1795, DOI: 10.1271/bbb.61.1791

To link to this article: https://doi.org/10.1271/bbb.61.1791

Published online: 12 Jun 2014.

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 Biosci. Biotech. Biochcm., 61 (11), 1791-1795, 1997

Effects of Lecithin Addition in Oil or Water Phase on the Stability of Emulsions Made
with Whey Proteins
Yukiko YAMAMOTO and Megumi ARAKI
Department of Food and Nutrition, Faculty of Human Life Science, Osaka City University, Sugimoto 3-chome, Sumiyoshi-ku,
Osaka 558, Japan
Received January 29, 1997

The effects of lecithin addition in oil or water phase on the stability of oil-in-water emulsions made
with 0.1 wt°l<, whey protein and 10 wt% n-tetradecane at neutral and acidic pH were studied by monitoring
the gravitational creaming and phase separation. The effects of lecithin addition on the interfacial behavior
of p-Iactoglobulin were also studied to compare with the results of emulsion stability. At neutral pH, crude
phosphatidylcholine (PC) from egg yolk or soybean increased the stability of the emulsion made with protein
and lowered the interfacial tension of protein films more effectively than pure egg PC. A more remarkable
effect on both the emulsion stability and the interfacial tension was found when crude PC was added in the
oil phase rather than in the water phase. The purity of lecithins and the way to add them are suggested to
be very important to make a stable emulsion with protein. On acidic pH (4.5 or 3.0), the increased creaming
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or phase separation in a whey protein-stabilized emulsion, but the lowered interfacial tension of p-Iactoglobulin
films, were found upon the addition of pure or crude PC in oil or water phase. These results suggest that
in acidic pH, densely packed films may be formed on a planar oil-water interface, but not on adsorbed
layers around oil droplets in an emulsion.

Key words: emulsion stability; interfacial tension; whey protein; p-Iactoglobulin; lecithin

Whey protein isolates (WPI) are widely used as food
ingredients in bakery, dairy, and meat production because
of their good functional and nutritional properties. 1.2)
Among them, excellent surface and emulsifying properties
are interesting and have been studied in detai1. 1 10) The
stability of emulsions made with protein is known to be
influenced by a number of factors such as the way to pre-
pare, phase volume fraction, pH, temperature, ionic
strength, and added surface-active emulsifiers. 2.6,11) As the
lack of uniformity in composition of commercial WPI, the
effect of WPI components is also an important factor in
the stability of emulsions made with whey proteins. 2,4,S,10)
Lecithin is an important 'natural' small-molecule emul-
sifier available for widespread use in food processing ap-
plications. 12 . 13 ) Lecithin is composed of many different
phospholipids, and the two most abundant phospholipid
species are phosphatidylcholine (PC) and phosphatidyl-
ethanolamine (PE). The most important commercial source
of lecithin for food production is soybean. Lecithins
purified from egg yolk also have been used widely for
parenteral emulsions for drag delivery and intravenous
nutrition. 12IS ) Lecithin has been used both to stabilize fine
emulsions as the sole stabilizer and to make stable emulsions
with another emulsifier, proteins. The effects of lecithin on
the stability of protein-stabilized emulsions are reported
with positive or negative effects depending on the amount
and the kind of added lecithin. 16 .1 7) The displacement of
lecithin to milk proteins from oil~water interface has also
been studied with the results not as effective as other
(water-soluble) surfactants.16.18.19)
In most emulsions with protein, the primary stabilization
is provided by the protein-containing adsorbed layers at the
oil-water interface. Thus, understanding of interfacial
properties of protein film is essential to make a stable
emulsion. Interfacial tension, interfacial rheology, and
interfacial concentration have been studied to monitor the
interfacial behavior of proteins at air-water and oil-water
interfaces. 16.20 -- 24) A monolayer technique has also been
often used for understanding the interaction of lecithin with
proteins,25.26) with results suggesting that the amounts of
adsorbed protein on the film at the oil-water interface are
influenced by lecithin addition.
As the pH affects the conformational changes of globular
proteins, the pH of the aqueous phase is also important for
the stability of emulsions made with proteins. It is known
that proteins tend to aggregate at the pH of their isoelectric
point, and that the pH to make emulsions should be away
from the isoelectric point for the prevention of coalescence
and creaming in protein-stabilized emulsions. 8,9)
A variety of tests for the stability of oil-in-water emulsion
have been studied with no single satisfactory method. These
include turbidimetric technique,2 7) conductivity measure-
ment,28,29) measurement of the amount of oil or cream
separated during a certain period of time with or without
centrifugation, 6. 7) or the average particle size or particle
size distribution. 6 10,30,31) Recently, Fligner et al. sug-
gested that the extent of gravitational and centrifugal
creaming, and not average particle size, is an adequate
predictor of short-term emulsion stability with emulsions
made with milk proteins. 6 )
In this experiment, we studied the effects of lecithin
addition in oil or water phase on the stability of emulsions
made with whey proteins at neutral or acidic pH. P-
Lactoglobulin, the most abundant whey protein, is mainly
used for the protein source. Stability was evaluated by
measuring the extent of gravitational phase separation. The
interfacial behavior of fJ-lactoglobulin with or without
lecithin in oil or water phase was also studied by measuring

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 1792 Y. YAMAMOTO and M. ARAKI
the interfacial tension.
Materials and Methods
Materials. Bovine fJ-lactoglobulin (LOI30.lot no. 51 H7210) was obtained
from Sigma Chemicals (U.S.A.). Three kinds oflecithin were also obtained
from Sigma Chemicals: 'pure egg PC' [P2772, "'-' 99% L-a-phosphatidylcho-
line (PC). dissolved in chloroform], 'crude egg PC' (P9671, ",60% PC),
'crude soybean PC' (P3644, ......,40°;;) PC). Pure egg PC was used after
removal of chloroform by N 2 gas flushing. The phospholipid eon tents
measured by the method of Raheja ct al. .12) were 93 and 97% in crude
egg and soybean PC, respectively. These crude lecithins were used without
adjusting the difference in phospholipid contents. The phospholipid
composition of crude lecithin analyzed by HPLC was as follows: crude
egg Pc. PC 54%, PE 43%. phosphatidyIinositol (PI) 1.3%, unknown
J .7%: crude soybean PC, PC 67%. PE 23'%, pr 2.G%, unknown 7.4%.
Lyso-type of PC and PE, and phosphatidylserine were not detected. A
sample of whey protein isolates (WPI) was a gift from Taiyo Kagaku
(Japan) (San-lacto I-I) with a protein content > 93% (together with
<3% ash and <1% fat). As an oil phase. Il-tetradecane (>99%) from
Sigma Chemicals or commercial corn oil from Nissin Syokuhin (Japan)
were used without further puritication. Buffer solutions were prepared with
analytical grade reagents from Wako Pure Chemical Industries (Japan)
and double-distilled water.
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Emulsion preparatioll. A j3-1actoglobulin solution was prepared with
0.02 M bis-tris buffer (pH 7.0) or 0.02 M acetate bufft.:r (pH 4.5 or 3.0). A
protein-stabilil.ed oil-in-water emulsion was prepared at room temperature
by homogenizing OJ g of n-tetradecane with 2.7 g of j1.lactoglobulin
solution at 15,000 rpm for 3 min in a Polytron homogenizer and then
sonicating for 1 min with a ultrasonic generator (Nihonseiki Kaisha, Model
US-50) at maximum power. The emulsions were degassed for 30 min using
a water pump to remove entrapped air bubbles. The emulsions with 0.1 wt%
f3-lactoglobulin with 10.0 wt% oil, which were found to be unstable (Fig.
1). were used mostly in this experiment to study the stabilizing effect of
added lecithin. In some cases, 1.0 wt % of lecithin was added before
emulsification by dissolving or dispersing in the oil or water phase. WPI
was also used as a protein source instead of f)-lactoglobulin, and corn oil
as an oil source instead of n-tetradecane.
Emulsion Sfobility. Emulsion samples were transferred into a 7-mm i.d.
and 100-mm length test tube, tightly capped and stored in a water bath
at 25 I "c. Creaming and/or coalescent behavior in samples was followed
by monitoring visually the changes in the length of distinct cream and/or
oil layers at the top and vvater layer at the bottom of the stored emulsions.
lntelfacial tellsion. Interfacial tension at the n-tetradecane-water inter-
face was measured using a Wilhelmy plate surface tensiometer (Kyowa
Interface Science Co., CBVP-A3) with a cell thennostatted at 25°C.
f3-Lactoglobulin "vt %) dissolved in 0.002 M bis-iris buffer (pH 7.0)
or 0.002 M acetate bulTer (pH 4.5) was used as a water phase. and the oil
phase was put on it. In some experiments. lecithin ( 10- 3 wt%) was added
by dissolving in the oil 0]" water phase before the start of the experiment.
Results and Discussion
The stability of oil-in-water emulsions made with [3-
lactoglobulin or WPI was strongly dependent on the con-
centration of the emulsifier protein (Fig. 1). [3-Lactoglob-
ulin-stabilized emulsion started to cream soon after the
emulsification at the concentration of 0.1 or 0.2 %. Emulsion
with 0.5 or 1.0°;() [3-lactoglobulin was stable without
creaming for 6 h, and after that slightly creamed. In con-
trast, the WPI was found to make a stable emulsion at a
concentration of 0.5% without creaming for 5 days. Among
whey proteins, a-lactalbumin is more surface active than [3-
lactoglobulin and bovine serum albumin. 23l Other surface-
active components of WPI are small molecule emulsifiers,
phospholipids. The stabilizing effects of these surface-active
components have been studied with uncertain results
because of the lack of uniformity in composition of
commercial Wp[,2.4.5.10l
25
20
~
I-<
Q.)
15
§
§
Q.)
10
I-<
()
5
0
0 2 3 4 5
Time (days)
Fig. 1. Stability of Oil-in-Water Emulsions Prepared with j1-Lacto-
globulin or WPI.
Oil-in-water emulsions were prepared with 10 wt % n-tetradecane and p-lactoglobulin
or WPI dissolved in 0.02 M bis-tris buffer (pH 7.0). The time-dependent stability of
emulsions was expressed as a volume percentagc of cream layer: e, 0.1 wt% fJ-
lactoglobulin; .,0.2 wt % fJ-lactoglobulin; +,0.5 wt% fJ-lactoglobulin; .A., 1.0 wt%
fJ-lactoglobulin: O. 0.1 wt% WPI; <), 0.5 wt% WPI; T, 0.1 wt% Ii-lactoglobulin
with commercial corn oil instead of l1-tetradecane.
As expected, emulsions with corn oil are more stable than
emulsions with n-tetradecane. The facts that triglycerides
are more surface active than pure carbohydrate, and that
commercial corn oil contains surface active mono- and
di-glycerides explain the stability of emulsion with corn oiL
Although n-tetradecane is not used for food production, we
used it as an oil source mostly in this experiment for
experimental reproducibility.
The effects of lecithin addition on the stability of
emulsions made with [3-lactoglobulin at neutral and acidic
pH are summarized in Table. At neutral pH, the addition
of three types of lecithin in the water phase before
emulsification is effective to improve the stability, but
insufficient to prevent creaming. The effects of added lecithin
are seen to be markedly dependent on the purity and the
source of lecithin used. Emulsions made with [3-1acto-
globulin are more stable by the addition of crude lecithin
than the pure lecithin, and by the addition of crude lecithin
from soybeans than from egg yolk. The high contents of
both minor components of phospholipids other than PC
and surface-active impurities other than phospholipids may
be the reason why crude soybean lecithin is a more effective
stabilizer than the others. Rydhag and Wilton have reported
that crude lecithin is more effective than pure lecithin as a
sole emulsifier, and emulsions made with pure lecithin are
very unstable. 14l They suggested that the minor ionic
surfactants like PA and PS in crude lecithin have a sta-
bilizing action via their electrostatic and hydration forces.
Fang and Dalgleish suggested the importance of the kind
and purity of added lecithin by showing the stabilizing effects
of egg yolk PC 16 ) and destabilizing effects of synthetic
lecithin, dipalmitoyl PC 1 7) on the emulsion made with
case111.
The stabilizing effects of crude PC at pH 7.0 were found
to be more pronounced when added to the oil phase than
when added to the water phase, and this is not the case
with pure egg PC. So far, the method of lecithin addition
to an emulsion has not been studied systematically; some
results are with lecithin dissolved in the oil phase14.1Sl and
the other is with lecithin dissolved in the water phase. 1 7)
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 Stability of Emulsions Made with Whey Proteins 1793

Table Effects of Lecithin Addition on the Stability of Emulsion Prepared with p-Lactoglobulin at Neutral or Acidic pH

pH 7.0 pH 4.5 pH 3.0

Lecithin
Cream Oil Water Cream Oil Water Cream Oil Water
(%)
- -------------------

Not added IS.0 0 0 57.5 0 42.0 19.9 0 0

( 6.8 0 0) (30.S 0 69.7) (14.3 0 0)
Lecithin was added in water phase
Crude Soybean PC 7.1 0 0 0.4 3.6 0 1.3 9.7 0
Crude PC 9.8 0 0 95.9 0 4.1 2.3 10.9 0
Pure Egg PC 14.6 0 0 27.1 0 72.9
Lecithin was added in oil phase
Crude Soybean PC 1.9 0 0 0.5 11.3 0 1.3 11.2 0
Crude Egg PC 3.2 0 0 97.3 0 2.7 3.1 10.6 0
Pure Egg PC 15.8 0 0 39.3 0 60.7

Oil-in-water emulsion was prepared with 10wt% n-tetradecane and 0.1 wt% p-Iactoglobulin dissolved in 0.02M bis-tris buffer (pH 7.0) or acetate
buffer (pH 4.5 or 3.0). Commercial corn oil was also used as an oil phase (results in parenthesis). Lecithin was added in buffer solution or oil before
emulsification at a concentration of 1.0 wt %. The stability of emulsions was measured by monitoring visually the changes in the length of each distinct
layers, and expressed as volume percentages of cream or oil layer (top) and water layer (bottom) after incubation for 24 h.
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For pure egg yolk lecithin, Fang and Dalgleish showed the 60
similar mean droplet size of casein-stabilized emulsions with
e
lecithin in the oil or water phase. 16 ) Our results in the Table
clearly show that the method to add a lecithin as an
z§ 50
emulsifier is 'a very important factor, and crude PC should c 40
.900 .... - .............
be dissolved in the oil phase to make a more stable emulsion 30
C
with whey proteins. II)
+-'

Table also shows the effects of pH on the stability of :iu9 20

- - - - --0
emulsions made with f3-1actoglobulin with or without ~
I-<
lecithin. Emulsion made with f3-lactoglobulin (pI = 5.2) II) 10
+-'
alone at pH 4.5 were very unstable, and those made at pH .B
0
3.0 were not so unstable as at 4.5. Recently Hunt and 0 5 10 15 20 25
Dalgleish also showed an increased instability of emulsions
Time (h)
made with milk proteins at the pI values by the droplet size
distribution technique. 8 . 9 ) The solubility of proteins de- Fig. 2. Effects of Lecithin Addition in Oil or Water Phase on the
Interfacial Tension between n- Tetradecane and P- Lactoglobulin Solution
creases and tends to aggregate at the isoelectric point. At at Neutral pH.
near the isoelectric point (pH 4.5), f3-1actoglobulin molecules Interfacial tension at the interface of n-tctradecane and 1O-4 wt % p-lactoglobulin
on the surface of oil droplets may aggregate with each other solution in 0.002M bis-tris buffer (pH 7.0) with or without added 1O-3 wt% crude
soybean PC in the oil or water phase was expressed as time-dependent changes: . ,
not only on the same oil droplets but also on neighboring p-lactoglobulin: 0, crudc soybean PC (in water phase); e, p-lactoglobulin+crude
oil droplets, leading to creaming, flocculation and phase soybean PC (in water phase): 0, crude soybean PC (in oil phase); . , p-lacto-
separation. Thus, the pH of the emulsion should be away globulin + crude soybean PC (in oil phase).

from the isoelectric point to make a stable emulsion with

protein.
At acidic pH (4.5 and 3.0), emulsions made with f3-
lactoglobulin were not stabilized by lecithins added in the
oil or water phase. Separation of oil or water phase was
found upon the addition of crude PC and an increased
creaming was found upon the addition of pure PC. These
results suggest that added lecithin in oil or water phase at
acidic pH markedly weakens the adsorbed protein layers
around oil droplets.
As the primary stabilization of emulsions made with
protein is provided by the protein-containing adsorbed
layers at the oil~water interface, the effects of lecithin
addition in the oil or water phase on the interfacial tension
of protein films at the planar oil~water interface were studied
(Fig. 2). The tension at the interface of n-tetradecane and
f3-1actoglobulin solution at pH 7.0 was lowered by the
addition of crude soybean PC, and the effect was stronger
when leeithin was added in the oil phase than when added
in the water phase. The effects of lecithin added in the oil
phase as a sole surfactant are also strong.
The changes of tension at the interface of oil and f3-
lactoglobulin solution at pH 7.0 as a function of added
crude soybean PC concentration are expressed in Fig. 3.
The changes in the interfacial tension of lecithin alone
dissolved in the oil or water phase are also shown. By the
lecithin addition in oil phase even at a very low concen-
tration, 10- 4 %, the interfacial tension of f3-lactoglobulin
film was lowered markedly, suggesting the formation of
densely packed layers with both lecithin from the oil phase
and f3-lactoglobulin from the water phase. However, the
decrease in tension was rather moderate when crude soybean
PC was dissolved in the water phase even at high concen-
trations. Then, lecithin dissolved in water phase seems
to be not as effective to make interfacial layers with 13-
lactoglobulin. These results are consistent with the facts
that the displacement of lecithin from water phase to milk
proteins in the oil~water interface is not as effective as other
(water-soluble) surfactants. 16 ,18,19) In excess water, PC

NII-Electronic Library Service

 1794 Y. YAMAMOTO and M. ARAKI

60 60
S
50
S 50
Z Z
g g
t: 40 t: 40
.9 .9
rtl rtl
t: 30 t: 30
.....OJ .....OJ
~(.) 20 ]
(.)
20
~
I-< ~OJ
OJ
..... 10 ..... 10
..s 111,,1
..s
0 ""11,,1
0
-00 -5 -4 -3 -2 -1 0 5 10 15 20 25
Log10C (wt%) Time (h)

Fig. 3. Effects of the Concentration of Added Crude Soybean PC on the
Interfacial Tension between n- Tetradecane and [3- Lactoglobulin Solution.
Interfacial tension at the interj~lce of n-tetradecane and 1O- 4 wtO;;) fI-Iactoglobulin
solutIOn after 24 h was expressed as a functIon of the concentration of crude soybean
PC added in the oil or water phase; 0. crude soybean PC (in water phase); . ,
[i-lactoglobulin + crude soybean PC (in water phase); O. crude soybean PC (in oil
phase); II, {1-1actoglohulin tcrude soybean PC (in oil phase).
Downloaded by [80.5.1.128] at 13:52 17 December 2017
Fig. 5. Effects of Lecithin Addition in Oil or Water Phase on the
Interfacial Tension between n-Tetradecane and f1-Lactoglobulin Solution
at Acidic pH.
Interracial tensIOn at the interface of n-tetradecane and 10-4 wt% f3-lactoglobulin
solution in 0.002M acetate buffer (pH 4.5) with or without added 1O- 3 wt% crude
soybean PC in oil or water phase was expressed as time-dependent changes. Symbols
represent the same as in Fig. 2.

60
S isoelectric point have already been reported. 20 )
Z 50 The interfacial tension of [3-lactoglobulin at pH 4.5 was
g
-------------~
lowered to a very low value by the lecithin addition in the
t: 40 oil or water phase (0.3 or 6.9 mN m -1). Protein-lecithin
.9
rtl
30
complexes are known to be formed by sonication 34 ,35l or
t: ,,
lowering ofpH. 36 - 38 ) Although PC and PE are zwitterionic
\
OJ
..... ... \
...
~(.) 20 .. ... \

~ 'Ill....
I-<
10
.....OJ '\
..s __ ~~I~ft~1~~I~I~I~"w"I_ _~I~I~I!~lIlld~~,~I..~,~~,_.
0
-00 -5 -4 -3 -2
Fig. 4. Effects of the Concentration of Pure Egg PC on the Interfacial
Tension between 1/- Tetradecane and (3- Lactoglobulin Solution.
InterfaCial tension at the interlace of II-tetradecane and 10'-" wt% [J-lactoglobulin
slutlOn after 24 h was expressed as a function of the concentration or pure egg PC
added in oil or water phase: 0, pure PC (in water phase); •. fJ-Iactoglobulin +
pure egg PC (in water phase); pure egg (in oil phase); II, Ii-lactoglobulin + pure
egg PC (in oil phase).
exists as a mixture of lamellar mesophases and vesicles, and
the less hydrophilic PE forms reversed hexagonal phases. 33 )
This may be the reason for a lower surface activity oflecithin
added in the water phase than that added in the oil phase
with or without 13-lactoglobulin.
The concentration of pure egg PC dissolved in water
phase with and wihtout fJ-lactoglobulin affected its inter-
facial tension very weakly (Fig. 4). Even when dissolved in
the oil phase, a very high concentration is needed to lower
the tension with or without fJ-lactoglobulin in the water
phase. The less tendency of pure PC to lower interfacial
tension than crude PC seems to be agreed well with the
emulsion stability experiment.
Figure 5 shows that the interfacial tension of [3-
lactoglobulin at pH 4.5 continued to decrease for 24 h,
and reached a lower value than pH 7.0 (Fig. 2). The
f3-lactoglobulin molecule near the isoelectric point will be
more hydrophobic and compact in shape, and then ar-
ranged into interfacial film more slowly and densely than
at pH 7.0. The considerable adsorption of j3-1actoglobulin
molecules on the surface of oil droplet~; at pH near the
\
over a wide range of pH, acidic phospholipids (phosphatidic
\, acid, PS, PI, etc.) are negatively charged, and then interact
.. \
with positively changed [3-lactoglobulin molecules at pH
'"
4.5. This complexing of [3-1actoglobulin with lecithin at the
oil-water interface will make densely packed films and lower
the surface tension. In the emulsion at pH 4.5, the increased
complexing between [3-1actoglobulin and lecithin in aqueous
phase during sonicating emulsification may weaken the film
formation around oil droplets, and then destabilize the
emulsion.
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