EMULSIFYING PROPERTIES OF SOY PROTEIN:
CHARACTERISTICS OF 7s AND IIS PROTEINS
H. AOKI, 0. TANEYAMA and M. INAMI
ABSTRACT
The emulsifying properties of the 7s protein rich fraction (7s PRF)
and the 1 IS protein rich fraction (11s PRF) were investigated using
refined soybean oil. The emulsifying capacity and emulsion stability
of the 7s PRF generally showed higher values than those of the 11s
PRF in the pH range 2-10. The same phenomenon was observed
with the 7s PRF and 11s PRF uartiallv hvdrolvzed bv dilute HCl.
The emulsifying properties of <he acid-precipitated protein (APP)
and the 7s PRF showed the lowest value at around pH 4.5, and
were closely related to the behavior of protein solubility. The emul-
sion stability of the 11s PRF, however, showed its lowest value at
around pH 7 and did not necessarily correlate with its solubility.
The breaking stress of the emulsions introduced from both the 7s
PRF and the 11s PRF increased in accordance with oil phase vol-
ume. While the breaking stress of the 7s PRF-introduced emulsions
were little affected by heat treatment of the protein solution, con-
siderable effect was observed with the 11s PRF-introduced emul-
sions. The breaking stress of the 11s PRF-introduced emulsions
increased markedly as the protein concentration increased. The heat
treatment of the protein solution at 95°C for 5 min prior to emulsifi-
cation increased the breaking stress to two to four times higher than
that of emulsions without the heat treatment.
INTRODUCTION
EMULSIFYING PROPERTIES are useful functional para-
meters which play an important role in the development of
soy protein products for use as food. The emulsifying
properties of soy protein have long been utilized as process-
ing aids in the comminuted meat field (Pearson et al., 1965;
Inklaar and Fortuin, 1969). Recently they have also begun
to be used in coffee whiteners, milk-type beverages, mayon-
naise, etc. (Smith and Circle, 1972; Eida et al., 1978). While
many reports on the emulsifying properties of soy protein
deal mainly with application or comparison of soy protein
products (Pearson et al., 1965; Inklaar and Fortuin, 1969;
Hutton and Campbell, 1977; McWatters, and Cherry, 1977;
McWatters and Holmes 1979a, b; Volkert and Klein, 1979),
papers on basic research are relatively few (Shibasaki et al.,
1972; Kamat et al., 1978). The present authors since 1975
have conducted studies on the basic factors affecting the
emulsifying properties of soy protein (Aoki and Nagano,
1975; Aoki and Matsuura, 1976; Aoki et al., 1977a, b;
1978a, b). In the present paper, the emulsifying characteris-
tics of the 7s protein rich fraction and 11 S protein rich frac-
tion are reported.
Many studies have been made on the 7s and 11s pro-
teins, the main components of soy protein, and much infor-
mation has been accumulated concerning their molecular
structure, subunits, and mechanisms of the dissociation and
association of these proteins (Wolf, 1972). In electron mi-
croscopy and x-ray light-scattering studies, Badley et al.
Authors Aoki, Taneyama, and lnami are with the Food Processing
Laboratory, Faculty of Home Economics, Ohtsuma Women’s Univ.,
Sanban-cho, Chiyoda-ku, Tokyo, Japan 102.
0022-1147/80/0003-0534$02.25/O
01980 Institute of Food Technologists
534-JOURNAL OF FOOD SCIENCE- Volume 45 (1980)
(1975) clearly indicated the subunit structure of the 11s
protein consisting of two opposed hexagonal-shaped rings,
each containing six alternating acidic and basic subunits.
Wolf and Tamura (1969) and Hashizume et al. (1975) in-
vestigated the influence of heating on the dissociation and
association of the 7S and 11s proteins. It has already been
reported that the 7S and 11s proteins differ very much in
their gelling, texurizing and film-forming prope.rties (Aoki,
1970; Saio et al. 1971, 1974; Saio and Watanabe, 1973;
Shirai et al., 1974; Ishino and Kudo, 1977). Comparative
studies on the physical properties of cold-, acid- and salt-
precipitated soy protein have also been reported (Bau et al.,
1978). However, no studies on the emulsifying properties
of the 7s and 11 S proteins have been reported as yet.
EXPERIMENTAL
Preparation of soy protein fractions
Acid-precipitated protein (APP) was prepared routinely from
hexane-defatted commercial soybean meal (Ajinomoto Co., Inc.,
Tokyo) by means of aqueous extraction, clarification lof the extract
by centrifuging (8,000 x G for 20 min), and acidification to pH 4.5
with HCl. The precipitated protein was washed thoroughly with
deionized water.
Modifying the methods of Saio and Watanabe (197 3) and Koshi-
vama (1965). the 7s orotein rich fraction (7s PRF) and 11s urotein
rich fraction’(llS PRF) were prepared as‘follows.’ For the 7’s PRF,
the extract was obtained through aqueous extraction (meal:water =
1:5) and clarification by centrifuging (8,000 x G for 20 min). The
aqueous extract was then stored overnight at 0°C after CaCl had
been added to it and the resultant concentration adjusted to
0.025N. The precipitated protein was then removed by centrifuging
(8,000 x G for 20 mm). The 7s PRF was obtained by acidifying the
supernatant to pH 4.5 with HCl and washing the precipitated pro-
tein thoroughly.
For the 11s PRF, the aqueous extract was obtained in the same
manner as that for the 7s PRF with the exception that no CaCl was
added. The extract was stored overnight at 0°C and the precipitated
protein was separated by centrifuging (8,000 x G for 20 mm) and
washed with deionized water at 0°C.
All of the proteins obtained were used for the preparation of the
emulsions after the pH and protein concentration had been adjusted
with 0.5N HCl or NaOH and deionized water. The protein content
in the samples was determined by the micro-Kjeldahl analysis of
nitrogen x 6.25.
Preparation of partially hydrolyzed proteins
Each soy protein fraction was partially hydrolyzed by the
method described previously (Aoki and Matsuura, 1976; Aoki et al.,
1977a). 5g net of each protein fraction, exhibiting a protein purity
of more than 90%, was mixed with HCl and deionized water in
proportions so as to obtain a protein concentration and HCl concen-
tration of 1.5% and 0.05-O.lON, respectively. The protein was
hydrolyzed by keeping the mixture at 95°C for 15 hr. The pH of
the mixture was maintained around 2 during hydrolysis. The hydrol-
yzed protein was introduced into the preparation of emulsions after
its pH and protein concentration were adjusted in the same manner
as in the case of unhydrolyzed proteins. Though the hydrolyzed
protein aquired a slightly greater ionic strength by pH-neutraliza-
tion, this was not so great as to affect the emulsifying properties
(Aoki and Nagano, 1975).
Determination of protein solubility
After the pH and protein concentration (1%) were adjusted with
O.lN HCl or NaOH and deionized water, the protein dispersion was
stirred by a magnetic stirrer for 30 min at room temperature. The
supernatant was separated by centrifuging at 8,000 x (; for 20 min.
 EMULSIFYING PROPERTIES OF SOY PROTEIN.. .

lo- 80.

2
2 4 6 8 IO
PH PH

Fig. l-Effect of pH on emulsifying capacity Fig. 2-Effect of pH on emulsion stability Fig. 3-Effect of pH on emulsifying capacity
(EC) of APP, 7.S PRF and 1 IS PRF. (ES) of APP, 7s PRF and 11s PRF. (EC) of partially hydrolyzed proteins.

Protein solubility was indicated by the ratio of the protein concen-

tration in the supernatant to that in the original protein dispersion.
Measurement of emulsifying capacity
The method of Swift et al. (1961) was modified and applied to
measure the emulsifying capacity, using commercially available soy-
bean oil (Ajinomoto Co., Inc., Tokyo). A protein solution of 0.2%
was put into a vessel with oil at various ratios of the protein solution
to the oil, keeping a total volume of 100 ml (by using a separate
vessel for each ratio) in order to maintain a constant stirring effi-
ciency. The samples in each vesselwere emulsified by homogenizing
with a propeller-type mixer (Homeogenizer Model HC, Nihon Seiki
Co., Tokyo) at 16,000 rpm for 1 min. The emulsifying capacity was
expressed as g of oil per mg of nitrogen at the critical point, i.e., the
point of collagse (Swift et al., 1961) where the O/W emulsion broke
down as the ratio of oil to protein solution increased. The critical
point was clearly determined by the behavior of the emulsion as a
small amount of it was added to water. The test for emulsifying
capacity was repeated three times.
Measurement of emulsion stability
Emulsion stability was measured according to the method of
Acton and Saffle (1970). Soybean oil and the 0.2% protein solution
were homogenized at the volume ratio of 35:65 by the above
method. Ten grams of emulsion were immediately placed into a 15
x 150 mm test tube. After standing for 30 min at room tempera-
ture, 5g of the emulsion were removed from the bottom and the
moisture content determined. The emulsion stability was calculated
as follows:
100 - M test
Emulsion stability = x 100%
100 - M original
where M test = % of moisture after 30 min, and M original = % of
moisture of original emulsion The test for emulsion stability was
repeated three times.
As is well known, the emulsifying capacity and emulsion stabil-
ity of soy proteins generally decrease to the minimum level in their
apparent isoelectric region (around pH 4-4.5) and indicate higher
values in the more acidic or alkaline regions (Aoki and Nagano,
1975; Volkert and Klein, 1979). Thus, in order to compare the
emulsifying properties of samples on the whole, the following four
pH’s were selected for measurement of the emulsifying capacity and
emulsion stability: pH 4.5 as representative of the isoelectric region,
pH 2 as representative of the acidic region, pH 10 the alkaline
region, and pH 7 the neutral region.
Measurement of breaking stress of emulsion
The breaking stress of the emulsion was measured by the Curd
Meter (Model 301, Iio Electric Co., Tokyo), which was initially
developed to evaluate the texture of soft milk curd (Toda et al.,
1971). The weight is hung on a spring with a known instrumental
constant. The plunger is set at the bottom of the weight. A sample
of the emulsion is placed just under the plunger on a moving plate.
The plate is moved upward at a constant rate (9 set/cm), subjecting
the sample to an increasing load. The sample becomes deformed and
then broken at a breaking point. The breaking stress is indicated as
follows:
Fig. 4-Effect of pH on emulsion stability (ES) of partially hydrol-
yzed proteins.
Breaking stress = F/A dyne/cm’
where F is the load at the breaking point and A is the cross section
area of the plunger. In this experiment, 90 ml of emulsion was
placed in 50 x 70 mm beakers and a disk-type plunger with a 30
mm diameter was used. The test for breaking stress was repeated
three times.
RESULTS & DISCUSSION
Effect of pH on emulsifying properties
Figure 1 shows the effect of pH on the emulsifying ca-
pacity of the 7s PRF and 11 S PRF. Just as with the APP,
both the 7s PRF and 11s PRF indicated the lowest levels
in their isoelectric region and increased at pH’s above and
below this region. Figure 2 shows the effect of pH on the
emulsion stability. The behavior of the 7s PRF was sirnil?:
to that of the APP, showing the lowest level in the isoelec-
tric region. The 11 S PRF, on the other hand, exhibited the
particular behavior of reaching the lowest level at neutral
pH. The particular behavior of the 11s PRF is note-
worthy in contrast to the common trend wherein the emul-
sifying properties of vegetable proteins indicate the lowest
value in their isoelectric region (Aoki and Nagano, 1975;
Franzen and Kinsella, 1976; Kamat et al., 1978; Ramana-
tham et al., 1978; Volkert and Klein, 1979). Figure 3 shows
the effect of partial hydrolysis with dilute acid on the emul-
sifying capacity of the 7s PRF and 11s PRF. With the
partial hydrolysis, a remarkable increase in the emulsifying
capacity of both the aforementioned kinds of proteins was
observed in comparison with that of the unhydrolyzed pro-
teins, especially in the isoelectric and neutral regions. The
behavior of both the hydrolyzed 7s PRF and 11 S PRF was
similar to that of the hydrolyzed APP. Figure 4 shows the

Volume 45 (1980)-JOURNAL OF FOOD SCIENCE-535


PH
Fig. &i-Effect of pH on solubility of APP, 7s PRF, and 11s PRF.
effect of partial hydrolysis on the emulsion stability. In
comparison with the unhydrolyzed 7S PRF, the emulsion
stability of the hydrolyzed 7S PRF indicated a remarkably
high level in the isoelectric and neutral regions. The hydrol-
yzed 11s PFR showed a similar increase except in the
acidic region, whereas the emulsion stability of the hydrol-
yzed APP was observed to increase throughout the pH
range 2- 10.
It is known that partial hydrolysis shows some effect on
the forming and emulsifying properties of proteins (Hori-
uchi and Fukushima, 1978; Eida et al., 1978), and some
hydrolyzed protein products are already on the market.
The marked effect of the partial hydrolysis manifests itself
only under certain optimum conditions which vary depend-
ing on hydrolyzing methods, kind of proteins, etc. For in-
stance, the partial hydrolysis of APP with dilute acid, hav-
ing a high degree of specificity for preferential cleavageand
selectively liberating aspertic acid (Schultz et al., 1962),
indicates a remarkable effect on improving the emulsifying
properties in the range within which only aspertic acid is
liberated and other amino acids remain virtually unliberated
(Aoki and Matsuura, 1976; Aoki et al., 1977a). Figures 3
and 4 show the effect of hydrolysis on the 7S PRF and 11 S
PRF under the optimum conditions for the APP. The fact
that the 7S PRF and 11 S PRF show a lower emulsion sta-
bility than that of the APP (Fig. 4) may likely be explained
by the difference between the optimum hydrolyzing condi-
tions for the two proteins and those for the APP. However,
the exact causeis still uncertain.
The partial hydrolysis of protein sometimes shows a
negative effect on their emulsifying properties. Cherry et al.
(1979) reported the emulsifying capacity of peanut protein
to decreaseby treating with proteolytic enzymes. It is diffi-
cult to explain this apparent discrepancy at present as the
mechanism of the effect of partial hydrolysis on emulsify-
ing properties still remains equivocal. However, the follow-
ing causesmay be presumed empirically: first, the effect of
hydrolysis differs markedly depending on the kinds of pro-
tein and the conditions of hydrolysis; second, the effect of
hydrolysis on emulsifying capacity and emulsion stability
does not necessarily maifest itself in the same way. At any
rate, these differing phenomena should be admitted as fact.
Solubility of soy protein fractions
As shown in Figure 5, the solubility of the APP, the 7S
PRF and the 11S PRF indicated minimum values at pH 4.5.
A comparison of Figure 5 with Figure 2 calls attention to
the fact that there are two different types of relationship
between solubility and emulsion stability, i.e., the emulsion
536-JOURNAL OF FOOD SCIENCE-Volume 45 (19801
!i-
11
20 40 60 80 100
Heating Temperature ‘C
Fig. 6-Effect of heating temperature on emulsifying capacity (EC)
of 7s PRF and 1 IS PRF.
stability of the APP and 7S PRF correlates with their solu-
bility, whereasthat of the 11 S PRF does not.
A number of studies have shown that the pH-emulsifying
property profile of various proteins, including soy protein,
resembles the pH-solubility profile (Pearson et al., 1965;
Swift et al., 1961; Hegarty et al., 1963; Sosulski et al.,
1976; Crenwelge et al., 1974). On the other hand, Wang
and Kinsella (1976) showed that the soluble protein frac-
tion of alfalfa indicates maximum emulsifying capacity at
pH 5 and suggestedthat proteins remaining soluble in this
pH region had a- higher emulsifying capacity than those
solubilized above or below this pH region. According to the
experiments done by McWatters and Holmes (1979a, b)
using soy,and peanut flour, high levels of nitrogen solubility
were not necessarily associated with maximum emulsifying
capacity. Although the behavior of the 11s PRF shown in
Figure 2 may be partly explained by the suggestion given
by Wang, the definitive answer should depend on more ex-
tensive studies in the future.
When the APP partially hydrolyzed with dilute acid and
as a result having approximately 60% solubility at pH 4.5
was separated at pH 4.5 into soluble and insoluble protein
fractions, and the emulsion stability of the respective frac-
tions was measured at 4.5, the former indicated values as
low as less than 10% while the latter indicated values as
high as around 90% (Aoki and Taneyama, 1979). Similar
results were obtained from acetylated APP and APP dena-
tured with alcohols. Moreover, some results are being ob-
tained which suggest that the hydrophobic region of the
surface of these modified and insolubilized protein frac-
tions is greater than that of the unmodified APP (Aoki et
al., 1978a; Aoko and Taneyama, 1979). Although in order
to clarify the behavior of the 11s PRF shown in Figure 2
there seemed to be a need for examinations made from
viewpoints different from the above, it is presumed certain
that at least slight liophilization of the protein molecules
greatly contributes to an increase of the emulsifying proper-
ties exhibited by the insolubilized soy protein. In any case,
the relationship between emulsifying properties and protein
solubility is diverse and it is necessaryto study individual
casesfurther.
Effect of heat treatment on emulsifying capacity
The emulsifying properties of soy protein generally tend
to decrease if the protein solution is heated previously
(Aoki and Nagano, 1975). Figure 6 shows the effect of heat
treatment on the emulsifying capacity of the 7S PRF and
11s PRF. The protein solution was heated for 5 min at
selected temperatures between 50°C and 95’C. Based on
 EMULSIFYING PROPERTIES OF SOY PROTEIN.. .

4- 4
t
Fig. 7-Effect of oil phase volume on break-
ing stress (6s) of emulsions from 7s PRF: I
b
o, unheated; A, 50°C; A, 7@C; 0, 8gC; 0, “0
x 3- 95” c. - 3
x
2 2
Y t
5
c
= 2-
Ii
m

1 1
Fig. &-Effect of oil phase volume on break-
ing stress (6s) of emulsions from 11s PRF:
o, unheated; A, 50°C; A, 7U’C; 0, 85°C; 0,
0 95” c. 0
40 50 60 70 40 50 60 70
Oil Phase Volume. % oil Phase Volume. %

the preliminary test result that, within 10 min the emulsify- the heat treatment, whereas on the other hand the emulsion
ing capacity of soy proteins was hardly affected by the from the 11 S PRF was greatly affected. That is, when com-
influence of the heating time, 5 min was selected for the pared at the same dispersed phase volume, the breaking
heating time interval. The emulsifying capacity of both the stress of emulsions introduced from the 11 S PRF decreased
proteins decreasedas a result of the heat treatment with the with a heating temperature of 50°C then increased as the
lowest value being observed at 85’C. The 11S PRF showed temperature went up to 85’C. It then again showed a slight
a greater decreasethan the 7S PRF. decrease when heated at 95’C. When compared at the same
The emulsifying capacity of the APP measured under the dispersed phase volume, the 11 S PRF emulsions tended to
same conditions indicated hardly any influence of the heat- indicate a higher breaking stress than the 7S PRF emulsions
ing temperature, and its influence on the 11S PRF con- except when the heat treatment was performed at 5O’C.
tained in the APP was not discernable (Aoki and Nagano, The breaking stress of emulsion introduced from the 7S
1975). Although all of the differences in the emulsifying PRF might be affected more by heat treatment, depending
capacity of the 7S PRF and 11s PRF as a result of heat on the conditions. However, the fact that, under given con-
treatment are not evident in Figure 6, it is obvious that, ditions, the breaking stress of the 11 S PRF emulsion is more
when compared under identical heating conditions, at least, sensitive to heat treatment than that of the 7S PRF emul-
changes which are not observed in the emulsifying capacity sion is very interesting in relation to the fact that the gelling
of the APP or of the 7S PRF do appear in the case of the and the texturizing properties of the 11 S PRF are more
11s PRF. sensitive to heat treatment than those of the 7S PRF (Aoki,
Reports on the influence of heat treatment upon pro- 1970; Saio et al., 1969, 1974).
teins have been made by Cherry et al. (1973, using peanut Figure 9 shows the effect of protein concentration on the
protein, and by Wolf and Tamura (1969) and Hashizume et breaking stress of emulsions introduced from the 11s PRF.
al. (1975), using soy protein. With the 11 S protein, at pH The heat treatment in this test consisted of heating protein
7.6 and at an ionic strength of 0.5, within 5 min at 100°C solution at 95OC for 5 min. The emulsions were formed at
dissociation and associatior occur simultaneously (Wolf and pH 7 with the critical ratio of oil phase to water phase
Tamura, 1969). The 11s protein is stabilized against ther-
mal aggregation, up to 80°C, by high ionic strength solu-
tions. By contrast, the 7S protein is more stable at low
ionic strength (Hashizume et al., 1975). Although it does
not seem that such changes in the 7S and 11s proteins
caused by heating directly reflect the emulsifying capacity
measured by this type of method, further detailed studies
will be necessary to determine the influence of heat treat-
ment on the emulsifying properties of the 7S PRF and 11 S
PRF.
Breaking stress of emulsions
The emulsion viscosity generally increases as the ratio of
dispersed phase to continuous phase increases. The emul-
sions sometime enter a semi-solid or solid state, depending
on conditions. In order to compare the emulsions intro-
duced from the 7S PRF and 11 S PRF in the process of
changing from fluid to solid, their breaking stress was meas-
ured in relation to the heat treatment of the protein solu-
tions (Fig. 7 and 8). The protein solutions were heated for
5 mm at selected temperatures. The emulsions were formed I.‘!
03 0.6 U.Y
at pH 7 using 0.4% protein solution. The breaking stress of PrOteill COnCentratiOIl. X
both the 7S PRF and 11s PRF emulsions increased with
the increase of oil phase volume. The breaking stress of Fig. g-Effect of protein concentration on breaking stress (6s) of
emulsion introduced from the 7S PRF was little affected by emulsions from 1 IS PRF.

Volume 45 (1980)-JOURNAL OF FOOD SCIENCE-537

 corresponding to each protein concentration. The breaking A&i, H., Orimo, N., Simazu, R., and Wakabayashi, K. 1!378a. Effect
of acylation on the emulsifying properties of soybean proteins.
stress of the emulsions introduced from both the unheated J. Jap. Sot. Food Sci. Technol. 25: 668 (Japanese).
and heated 11 S PRF solutions increased as the protein con- A&i, H., Orimo. N.. Kitagawa, I., Shimazu, R., and Wakabayashi,
centration increased. The difference in breaking stress be- K. 197813. Improvement of emulsifying properties of soy pro-
teins. Presented at The 5th International Congress of Food Sci-
tween the two became clear starting around 0.5% of protein ence and Technology. Sept. 17-22, Kyoto, Japan.
concentration, i.e., the breaking stress of the heated 11 S Aoki, H. and Taneyama. 0. 1979. Effect of alcohol treatment on
emulsion stability of soy proteins. Presented at The 26th General
PRF indicated four times as great at 0.6%, and, at 0.9% Meeting of Japanese Society of Food Science and ‘Technology.
1.2%, twice as great a value as that of the unheated. June 4-6, Send& Japan.
As main factors affecting the viscosity or breaking stress Badley, R.A., Atkinson, D., Hauser. H., Oldani. D., Green, J.P.. and
Stubbs. J.M. 1975. The structure. physical and chemical proper-
of emulsions, the following two effects can generally be t4i;; o;l;he soybean protein glycinin. Biochim. Biophys. Acta
considered: (1) the effect which depends on the volume Bau, H:M., F&llain. B Beaufrand M.J., and Debry G 1978 Com-
ratio of dispersed phase to continuous phase and (2) the parison of cold-, aiid- and salt-Grecipitated soy &o&ins. J: Food
effect which depends on the property of the continuous Sci. 43: 106.
Catsimpoolas. N. and Maeyer, E.W. 1970. Gel&ion phenomena of
phase. In Figure 9, at the critical ratio the oil phase volume soybean globulins. 1. Protein-protein interactions. Cereal Chem.
of both the unheated and heated proteins increased remark- 47: 55s.
Cherry, J.P.. McWatters K.H.. and Holmes, M.R. 1975. Effect of
ably with the increase of protein concentration, The oil moist heat on solubility and structural components of peanut
phase volume at 0.3% protein concentration was, for exam- proteins. J. Food Sci. 40: 1199.
ple, about SO%, and at 1.2% protein concentration, it indi- Cherry, J.P., McWatters. K.H.. and Beuchat, L.R. 1979. Oilseed pro-
tein properties related to functionality in emulsions and forms.
cated about 75%. On the other hand, the effect depending American Cemical Society Symposium Series 92: 1.
on the properties of the continuous phase is considered Circle, S.J.. Meyer, E.W., and Whitney, R.W. 1964. Rheology of SOY
protein dispersions. Effect of heat and’other factors on rrelation.
very small because of the low protein concentration below &real Chem. 41: 157.
1.2%. Therefore, the increase in breaking stress shown in Crenwelge, D., DiII, C., Tybor, P., and Landmann, W. 1!374. A corn-
parison of the emulsification capacities of some protein concen-
Figure 9 should be attributed mainly to the former effect, trates. J. Food Sci. 39: 175.
i.e., the effect of volume ratio of dispersed phase to contin- Eida. T., Harakawa, K.. S&oh, T., Suematsu. A., and Yam&o, C.
uous phase. 1978. Development of mayonnaise-like food with soybean pro-
tein. Presented at the 5th.International Congress of- FoodSci-
When comparing the difference between the unheated ence and Technology, Sept. 17-22, Kyoto. Japan.
and the heated solution. however, the oil phase volume of Franzen, K.L. and KinseIIa, J.E. 1976. Functional properties of suc-
cinylated and acetylated soy protein. J. Agric. Food Chem. 24:
the heated solution tends to be lower-though only a lit- 788.
tle-than that of the unheated. Consequently, in regard to Hashizume, J.. Nakamura, H.. and Watanabe, T. 1975. Influence of
ionic strength on conformation change of soybean protein
the effect of dispersed phase volume on breaking stress, the caused by heating, and relatiohship of its conformation change
unheated solution can be more advantageous than the to gel formation. Agric. Biol. Chem. 39: 1339.
heated. Neverthress, the breaking stress of the heated solu- Hegerty, G.R., Blatzler, L.J., and Pearson, A.M. 1963. Studies on
emulsifying properties of some intercellular beef muscle pro-
tion clearly shows a higher value than that of the unheated. teins. J. Food Sci. 28: 663.
These suggest strongly that the latter effect, i.e., the effect Horiuchi, T. and Fukushima, D. 1978. Studies on enzyme-modified
proteins as forming agents: Effect of structure on form stability.
depending on the physical property of the continuous Food Chem. 3: 35.
phase, plays the decisive role in this case. Hutton, C.W. and Campbell, A.M. 1977. Functional properties of a
soy concentration and a soy isolate in single systems and in a
Many studies have been reported on the heat-induced gel food system: Emulsion properties, thickening function and fat
of soy protein (Aoki and Sakurai, 1969; Circle et al., 1964; absorption. J. Food Sci. 42: 457.
Catsimpoolas and Maeyer, 1970; Hashizume et al., 1975), InkIaar, P.A. and Fortuin, J. 1969. Determination and emulsion
stabilizing capacity of protein meat additives. Food Technol. 23:
and it is also known that with emulsions introduced from 103.
the APP solution over IO%, the latter factor plays a more Ishino, K. and Kudo, S. 1977. Gelation phenomena induced by
alkali-alcohol treatment of 7S and 11s components in soybean
decisive role than the former under certain conditions globlins. Agric. Biol. Chem. 41: 1347.
(Aoki et al., 1977b). There are, however, no reports on the Kamat, V.B., Graham, G.E., and Davis. A.F. 1978. Vegetable pro-
tein: Lipid interactions. Cereal Chem. 55: 295.
gel formation with a soy protein solution below 1%. It Koshimyama. I. 1965. Purification of 7S component of soybean
seems difficult to explain the difference between the un- proteins. Agric. Biol. Chem. 39: 885.
heated and the heated solution shown in Figure 9 by the McWaters, K.H. and Cherry, J.P. 1977. Emulsification, foaming and
protein solubility properties of defatted soybean, peanut, field
difference in gelling property of the 11s PRF brought by pea and pecan flours. J. Food Sci. 42: 1444.
the heat treatment. At any rate, this phenomenon will need McWatters, K.H. and Holmes, M.R. 1979a. Influence of pH and salt
concentration on nitrogen solubility and emdsification proper-
to be studied as an interesting case of behavior of the ties of soy flour. J. Food Sci. 44: 770.
special system containing the protein which is spread on the McWatters. K.H. and Holmes, M.R. 197Sb. Influence of moist heat
on solubility and emulsification properties of soy and peanut
interface between oil and water. flours. J. Food Sci. 44: 774.
Pearson, A.M., Spboner, M.E:. Hegarty, G.R.. and Bratzler. L.J.
1965. The emulsifying capacity and stability of soy sodium pro-
REFERENCES teinate, potassium caseinate and nonfat dry milk. Food Technol.
19: 1841.
Acton, J.C. and Saffle. R.L. 1970. Stability of oil-in-water emulsion. Ramanatham, G.. Ran, L.H. and Urs, L.N. 1978. Emulsification
1. Effect of surface tention, level of oil, viscosity and type of properties of groundnut protein. J. Food Sci. 43: 1270.
meat protein. J. Food Sci. 35: 852. Silo, K., Kamiya, M., and Watanabe, T. 1969. Food processing
Aoki, H. and Sakurai, M. 1969. Studies on the gel&ion of soybean characteristics of sovbean 7s and 11s nroteins. 1. Effect of dif-
protein. 5. On the effect of heat denaturation. J. Agri. Chew ference of protein components am&~ soybean varieties on for-
Sot. Japan 43: 488 (Japanese). mation of Tofu-gel. Agric. Biol. Chem. 33: 1301.
A&i, H. 1970. Changes in soybean protein components during its Saio, K., Kajikawa, M., and Watanabe, T. 1971. Food processing
gel formation process. J. Jap. Sot. Food Sci. Technol. 17: 129 characteristics of soybean 7S and 11s proteins. 2. Effect of sul-
(Japanese). fhydril group on physical properties of Tofu-gel. Agrc. Biol.
A&i, H. and Nagano. H. 1975. Studies on emulsifying properties of Chem. 45: 890.
soybean proteins. 1. Factors affecting the emulsifying properties. Saio, K. and Watanabe. T. 1973. Food use of soybean 7S and 11s
J. Jap. Sot. Food Sci. Technol. 22: 320 (Japanese). proteins: Extraction and functional properties of their fractions.
Aoki, H. and Matsuura, H. 1976. Studies on the emulsifying proper- J. Food Sci. 38: 1139.
ties of soybean proteins. 2. Effect of partial hydrolysis. J. Jap. Saio, K., Satoh. I., and Watanabe, T. 1974. Food use of soybean 7S
Sot. Food Sci. Technol. 23: 26 (Japanese). and 11s proteins: High temperature expansion characteristics of
Aoki, H., Okamura, H., and Inami, M. 1977a. Studies on emulsify- gels. J. Food Sci. 39: 777.
ing properties of soybean proteins. 3. Effect of partial hydrolysis &h&z. J., Allison, H., and Grice, M. 1962. Specificity of the cleav-
by dilute hydrochloric acid. J. Jap. Sot. Food Sci. Technol. 24: age of proteins by dilute acid. 1. Release of aspertic acid from
511 (Japanese). insulin. ribonuclease. and glucagon. J. Biochem. 1: 694.
A&i, H., Nagatomo, R.. Hotta, K., and Yamaguchi, H. 197713. Stud- Shibasaki. K., Okubo, K., and Sato, T. 1972. Food chemical studies
ies on emulsifying properties of soybean proteins. 4. Emulsifying on soybean proteins: Shifting of protein to cream layer of soy-
behavior at high protein concentration. J. Jap. Soa. Food Sci. bean milk and emulsifying capacity. J. Jap. Sot. Food Sci. and
Technol. 24: 618 (Japanese). Technol. 19: 589 (Japanese).
-Con hued on page 546
538-JOURNAL OF FOOD SCIENCE-Volume 45 (1980)
cate that soybeans should serve a greater role in providing Kakade. M.L., Rackis. J.J.. McGhee. J.E.. and Puski. G. 1974. Deter-
dietary protein for humans. Why, then, has this not hap- mination of trypsin inhibitor activity of SOY p&ducts: a collabo-
rative analysis of an improved procedure. Cereal Chem. 51: 376.
pened? As one should expect, there are numerous responses Li. J.C.R. 1975. “Introduction to Statistical Inference.” Edwards
to such a question; however, at least two reasons seem para- Brothers, Ann Arbor, Mich.
Liener, I.E. 1972. Nutritional value of food protein products. In
mount. Most Americans either are unaccustomed to eating “Soybeans: Chemistry and Technology.” Ed. Smith. A.K. and
soybeans or they do not like the soy taste. Because soy- Circle, S.J., Vol 1. Avi Publ. Co., We&&, Corm.
beans could contribute to the betterment of human nutri- Liener. I.E. 1979% Anti-nutritional factors as determinants of soy-
bean quality. University of Minnesota, St. Paul, Minn. Paper pre-
tion, greater attention should be directed toward research sented at World Soybean Research Conference II, North Caro-
leading to utilization of soybeans as food products. lina State University, Raleigh, March 26-29.
Liener. I. 1979b. Significance for humans of biologically active fac-
tors in soybeans and other food legumes. J. Am. Oil Chemists’
REFERENCES SW. 56: 121.
Liener. I.E. and Kakade, M.L. 1969. Protease inhibitolrs. In “Toxic
Anderson, R.L., Rackis. J.J., and Taller& W.H. 1979. Biologically Constituents of Plant Foodstuffs.” Ed. Liener. I.E. Academic
active substances in SOY products. In “SOY Protein and Human Press, New York.
Nutrition.” Ed. WiIke, H.L.. Hopkins, D.T., and Waggle, D.H. p. Rackis, J.J. 1965. Physiological properties of soybean trypsin inhibi-
209. Academic Press. New York. tors and their relationship to pancreatic hypertrophy and arowth
Andrews, F.E. 1976. Personal communication. College of Home inhibition of rats. Fed. P&c. 24(6): part 1, i488..
Economics, The University of Tennessee, Knoxville. Rackis, J.J. 1972. Bjologically active components. In “Soybeans:
AOAC. 1975. “Official Methods of Analysis.” 12th ed. Association Chemistry and Technology, ” Ed. Smith, A.K. and Circle, S.J..
of Official Analytical Chemists, Washington. D.C. Vol. 1. Avi Publ. Co.,Westport, Corm.
AOCS. 1974. “Official and Tentative Methods,” 3rd. ed. American Rackis, J.J. 1974. Biological and physiological factors in soybeans.
Oil Chemist’s Society.Champaign, Ill. J. Am. Oil Chemist’s Sot. 51: 161A.
Bates, R.P. and hlatthews, R.F. 1975. Ascorbic acid and O-carotene Rackis, J.J. 1978. Biochemical changes in soybeans: Maturation,
in soybeans as influenced by maturity, sprouting. processing and postharvest storage and processing, and germination. In “Posthar-
storage. Proc. Fla. State Hort. Sot. 88: 266. vest Biology and Biotechnology,” Ed. Hultin, H.O. and Milner,
Bates. R.P.. Weiss. D.D.. and Matthews. R.F. 1977a. Pickled soy- M., p. 34. Food & Nutrition Press, Westport. Corm.
beans as a nutritious snack. Proc. Fla: State Hort. Sot. 89: 210. Rackis, J.J., McGhee, J.E., and Booth, A.N. 1975. Biological thres-
Bates, R.P., Knapp, F.W., and Arauio, P.E. 1977b. Protein quality hold levels of soybean trypsin inhibitors by rat bioassay. Cereal
of green-mature. dry mature and sprouted soybeans. J. Food Sci. Chem 52: 85.
42: 271. Rackis, J.J., McGee, J.E.. Gumbmann, M.R., and Booth, A.N. 1979.
Burtis, E.L. 1950. World soybean production and trade. In “Soy- Effect of soy proteins containina trvpsin inhibitors in lone term
beans and Soybean Products,” Ed Markey, K.L., Vol 1, p. 61. feeding studies in rats. J. Am. Oi<Ch&ists Sot. 56: 162. -
Interscience Publishers, Inc., New York. Rasmussen, A.I. 1978. Nutrient comparison of fresh and field-dried,
Collins; J.L., McCarty, I.E.. and Swingle, H.D. 1971. Shelling ma- green-seeded soybeans. J. Am. Diet. Assoc. 72: 604.
ture. green soybeans with roller-type sheller. Tennessee Farm Roquib. M.A. 1977. Soybean for health. Bull. 4. General Printers
Home Sci. 78: 2. and Publishers Pvt. Ltd.. 119, Lenin Sarani. Calcutta. India.
Collins. J.L. and Sanders. G.G. 1973. Deep-fried snack food pre- Sanchez, J.F. 1978. Effect of added soymeal and cheese on quality
pared from soybeans and onions. Food Technol. 27(j): 46. and nutritional value of a corn-based product. M.S. thesis, Uni-
De, S.S. 1971. Technology of production of edible f&&s and pro- versity of Tennessee Library, Knoxville.
tein products from soybean. Agricultural Services Bull. 11, Food Sanders, W.L. 1978. Personal communication. Institute of Agzicul-
and Agricultural Organization, United Nations, Rome. ture, The University of Tennessee, Knoxville.
Hale, J.K. 1941. Soybeans in the diet. Circular 74. The University of Sinclair, P.. Vettel, R.S., and Davis, C.A. 1974. Soybeans in family
Tennessee, Knoxville. meals. USDA Home and Garden Bull. 208. Washington, D.C.
Isselbacher, K.J. and Alpers, D.H. 1969. Fatty liver: biochemical Smith, A.K. and Circle, S.J. 1972. Historical background. In “SOY-
and clinical aspects. In “Diseases of the Liver,” Ed. Schiff. L. J. beans: Chemistry and Technology,” Ed. Smith, A.K. and Circle,
B. Lippencott Co., Philadelphia. S.J.. Vol 1, P. 1. Avi Publ. Co., Westport. Corm.
Jones, J.H. and Foster, C. 1942. A salt mixture for use with basal MS received 7/14/79; revised 11/16/79; accepted 11/20/79.
diets either low or high in phosphorus. J. Nutr. 24: 245.
Kakade. M.L., Simons, N., and Liener. I.E. 1969. An evaluation of
natural vs synthetic substrates for measuring the antitryptic activ-
ity of soybean samples. Cereal Chem. 46: 518.

EMULSIFYING PROPERTIES OF SOY PROTEIN. . .From page 538

Shirai, M., Watanabe, K., and Okamoto. S. 1974. Contribution of 7s of principal component analysis to food texture measurement. J.
and 11s globulins of soybean protein to the formation and Texture Study 2: 207.
properties of Yuba-film. J. Jap. Sot. Food Sci. Technol. 21: 324 Volkert, M.A. and Klein. B.P. 1979. Protein dispersibility and emul-
(Japanese). sion characteristics of four soy products. J. Food !;ci. 44: 106.
Smith, A.K. and Circle, S.J. 1972. “Soybeans: Chemistry and Tech- Wang, J.C. and Kinsella. J.E. 1976. Functional properties of novel
nology,” Ch. 9 and 10. Avi Publishing Co., Inc., Westport, Corm. proteins: Alfalfa leaf protein. J. Food Sci. 4i: 286.
Sosulski. F.. Humbert. E.S., Bui. K.. and Jones. D.J. 1976. Func- Wolf, W.J. and Tamura. T. 1969. Heat denaturation of soybean 11s
tional properties of rapeseed flours, concentrate and isolate. J. protein. Cereal Chem. 46: 331.
Food Sci. 41: 1349. Wolf, W.J. 1972. “Soybeans: Chemistry and Technology,” Ch. 4.
Swift. C.E., Lock&t, C., and Fryar, J. 1961. Cornminuted meat Avi Publishing Co., Inc., Westport. Corm.
emulsions. The capacity of meats for emulsifying fat. Food MS received 7/15/79; revised 10/13/79: accepted 10/20/79
Technol. 15: 468.
Toda, J., Wada, T.. Yasumatsu, K., and Ishii, K. 1971. Application

541%JOURNAL OF FOOD SCIENCE-Volume 45 (1980)