Functional Properties of the Great Northern Bean
(Phaseohs vdgaris L.) Proteins:
Emulsion, Foaming, Viscosity, and Gelation Properties
S. K. SATHE and D. K. SALUNKHE
ABSTRACT
Functional properties of the Great Northern bean (Phaseolus vul-
guris L.) flour, albumins, globulins, protein concentrates, and pro-
tein isolates were investigated. Protein concentrates had the highest
water and oil absorption capacity (5.93 and 4.12 g/g, respectively)
among all the samples studied. Protein concentrates registered the
highest emulsion capacity (72.60 oil emulsified/g) while albumins
had the highest emulsion stability (less than 5 ml separation of
phase in 780 hr at room temperature of 21°C). Foaming ability of
the Great Northern bean proteins was fair. Foamability of the pro-
teins was concentration dependent.
INTRODUCTION
IN THE U.S., the beans of Phaseolus vulgaris are an impor-
tant food crop, both nutritionally and economically. The
Great Northern beans (Phaseolus vulgaris L.) rank third in
production among the five major bean cultivars ofPhaseoZus
in the U.S. (Change and Satterlee, 1979).
Numerous researchers have reported the preparation and
functional properties of protein concentrates and protein
isolates from plant, animal, and microbial sources (Satterlee
et al., 1975; Vananuvat and Kinsella, 1975; Hutton and
Campbell, 1977; Ramanatham et al., 1978; Zakaria and Mc-
Feeters, 1978; Gwiazda et al., 1979; Burgess and Kelly,
1979). Such efforts are often aimed at effective utilization
of inexpensive proteins for nutritional and functional pur-
poses. Precision in defining “functionality” appears to be
lacking (Martinez, 1979; Hermansson, 1979). Excellent
reviews on functional properties of proteins have appeared
(van Kleef et al., 1979; Schroder, 1979; Chou and Morr,
1979; Craig, 1979) elucidating several parameters affecting
the functional properties. Hydration of proteins is vital
for several of the functional properties such as emulsion
capacity, foaming, viscosity, and gelation. Carbohydrates
deserve consideration while evaluating functional proper-
ties of proteins (Kinsella, 1979) as they are known to be
important for functionality. Recently, Susheelamma and
Rao (1979) reported the role of arabinogalactan (a polysac-
charide) of black gram (Phaseolus mungo) in the texture of
leavened foods (steamed puddings).
In a previous paper we (Sathe and Salunkhe, 1981)
reported the solubilization and electrophoretic characteri-
zation of Great Northern bean proteins. The purpose of the
present investigation was to study certain functional
properties of Great Northern bean proteins.
MATERIALS & METHODS
THE SOURCE of the beans, protein fractionation and composition
were reported earlier (Sathc and Salunkhe, 1981). All the analyses
were performed in triplicate and means reported. All the chemicals
(unless mentioned otherwise) were of reagent grade.
Scanning electron microscopy
The bean flour and the freeze-dehydrated albumins, globulins,
Authors Sathe and Salunkhe are with rhe Depr. of Nutrition & Food
Sciences, Utah Srafe Univ., Logan, UT 84322.
protein concentrates, and protein isolates were prepared for scan-
ning electron microscopicobservationsas follows. An appropriate
dry sample was sprinkled on an aluminum stub (with a double-stick
tape on it) and was coated completely with gold-palladium alloy
in a Polaron E 5000 Sputter Coater (U.K.). The specimens were
then observed and photographed in an AMR 1OOOBScanning Elec-
tron Microscope (Cambridge, Mass.) at an accelerating voltage of 20
KV and suitable magnification.
Viscosity
The appropriate sample was dispersed in distilled water and mag-
netically stirred for 2 hr at room temperature (21°C) prior to ViS-
cosity measurements. Each sample was prepared at concentrations
of 1, 2, 3, 4, 5, 7, and 10% (w/v) and viscosity measured at room
temperature (21°C) employing an Ostwald type viscometer (Sargent-
Welch Scientific Co., U.S.A.; size # 200, approximate constant =
0.1 centistokes/s). All the measurements were performed in tripli-
cate and means (relative to distilled water) were reported.
Gelation
The method of Coffmann and Garcia (1977) was employed with
slight modifications. Appropriate sample suspensions of 2, 4, 6,
8, 10, 12, 14, 16, 18, and 20% (w/v) were prepared in 5 ml distilled
water. The test tubes containing these suspensionswere then heated
for 1 hr in a boiling water bath followed by rapid cooling under
running cold tap water. The test tubes were then further cooled for
2 hr at 4°C. The least gelation concentration was determined as that
concentrationwhen the samplefrom the inverted test tube did not
fall down or slip.
Oil and water absorption
For oil (Crisco Vegetable Cooking oil, Procter & Gamble, Cincin-
nati, Ohio) and water absorption determinations,the method of
Beuchat (1977) was followed. One gram of the sample was mixed
with 10 ml distilled water or oil for 30 set in a mixer (Vari-Whirl,
mixing control-“fast”). The sampleswere then allowed to stand at
room temperature (21°C) for 30 min, centrifuged at 5000 x G for
30 min, and the volume of the supernatant noted in a 10 ml gradu-
ated cylinder. Density of water was assumed to be 1 g/ml and that
of oil was determined to be 0.88 g/ml. Results were expressed on a
dry weight basis.
Emulsion capacity and stability
Emulsions were prepared according to the method by Beuchat
(1977). The sample (2g) was blended in a Waring Blendor with 100
ml of distilled water for 30 set at “HI” speed. Oil was added in S-
ml portions continuing blending. The drop in consistency (from a
maximum) judged by a decreasein resistanceto blending (subjec-
tively) was considered to be the point of discontinuation of oil
addition. The amount of oil added upto this point was interpreted
as the emulsifying capacity of the sample. The emulsion so prepared
was then allowed to stand in a graduated cylinder and the volume of
water separatedat time intervalsof 10, 20, 35, 60, 100, 120, 140,
160, 180, 200, and 780 hr was noted in each case, to study the
emulsion stability. All the experiments were conducted at room
temperature (21’C).
Foaming capacity and stability
Foaming capacity and stability of the samples was studied ac-
cording to the method of Coffmann and Garcia (1977). One gram of
sample was whipped with 100 ml distilled water for 5 min in a
Volume 46 (198lI--JOURNAL OF FOOD SCIENCE-71
 Waring Blendor at speed setting “HI” and was poured into a 250 ml
cylinder and the total volume at time intervals of O.O,O.S,1.0,2.0,
2.5, 3.0, 8.0, and 36 hr was noted. Specific volume and volume
‘increase (%) were calculated according to the following equations:
Vol. after whipping (ml)
Specific vol. =
Wt. after whipping (9)

Vol. increase(%) =
(Vol. after whipping -Vol. before whipping) (ml) x loo
Vol. before whipping (ml)

Fig. l-Scanning electron
flour 11500 Xl.
Egg albumin (Fisher Scientific Co., Fairlawn, N.J.) powder was em-
ployed as a reference standard. All the experiments were conducted
at room temperature (21’).
To study the effect of concentration on foamability; 1,2, 3,4,
5, 7, and 10% (w/v) aqueous suspensionswere whipped identically
as described above and the final volume was noted in each casein a
250 ml cylinder.
photomicmgraph of Great Northern bean

Fig. P-Scanning electron photomicrograph of Great Northern bean Fig. I-Scanning electron photomicrograph of Great Northern bean
albumins (1500 Xl. protein concentrates (3750 Xl.

Fig. 3-Scanning electron photomicrograph of Great Northern been Fig. B-Scanning electron. photomicrograph of Greet Northern bean
globulins (3750 Xl. protein isolates (3750 Xl.

72-JOURNAL OF FOOD SCIENCE-Volume 46 (1981)

 FUNCTIONAL PROPERTIES OF BEAN PROTEINS.. .

RESULTS & DISCUSSION
THE CRUDE PROTEIN CONTENT of the bean flour, al-
bumins, globulins, protein concentrates, and protein iso-
lates was 26.10, 81.70, 92.30, 85.40, and 92.40% (dry
weight basis) respectively (Sathe and Salunkhe, 198 1).
Scanning electron microscopy
The scanning electron microscopic observations (Fig.
1-5) indicated that albumins had rod-like structures with
relatively smooth surface topography while globulins con-
sisted of different shapes and sizes with relatively rougher
surfaces than albumins. Protein concentrates and protein
isolates, as expected, consisted of both albumins and
globulins, and hence possessedcharacteristics of both.
surfactants etc.), solubility of the protein molecules, and
others (Chou and Morr, 1979). However, polar amino
groups of protein molecules are the primary sites of protein-
water interactions. Cationic, anionic, and nonionic sites
bind different amounts of water (Kuntz, 1971). The
difference in water absorption by albumins and golbulins
(3.18 and 2.77 g/g dry sample, respectively), may have been
due to the protein concentration and possibly the conforma-
tional characteristics of these proteins. Water absorption by
the protein isolates and the globulins (2.73 and 2.77 g/g
dry sample, respectively) were comparable.
Oil absorption trends were similar to those for water
absorption. Protein concentrates registered the highest oil

Viscosity
The results of viscosity measurements are presented in Table l- Viscositv data on Great Northern bean proteinsa
Table 1. As can be seen from this table, viscosity appeared Relative
Cone
to be a function of not only the solids concentration but Sample % (WI4 viscosityb
also of the type of proteins. Albumins registered com-
parable viscosity to that of globulins at corresponding con- Albumins 1 1.21
centrations. Protein concentrates and protein isolates had 2 1 .83
comparable viscosities at corresponding concentrations. 3 2.55
4 3.66
Protein concentrates and isolates, however, were more 5 4.38
viscous than both the albumins and globulins at a particu- 7 9.51
lar concentration suggesting that when albumins and glob- 10 12.11
ulins were together, they behaved in different manner than
Globulins 1 1.29
when they were separate. These data further support our 1.65
2
earlier observations on electrophoretic mobility and col- 3 2.06
umn chromatographic behavior of the Great Northern bean 4 3.15
proteins (Sathe and Salunkhe, 198 1). 5 3.71
7 5.47
Gelation 10 10.99

The least gelation concentrations for the bean flour, al- Protein concentrates 1 1.65
2 2.59
bumins, protein concentrates, and protein isolates were 10,
3 4.59
18, 8, and 12% (all w/v) respectively. Globulins did not 4 7.81
form a firm gel up to 20% (w/v) concentration range. These 5 12.15
results further suggest that gelation is not only the function 7 23.25
of quantity of protein but also the type of protein(s) and 10 28.79
the nonprotein component(s) as well.
Protein isolates 1 1.61
2 2.57
Oil and water absorption 3 4.11
Results of the oil and water absorption are embodied 4 6.34
in Table 2. Protein concentrates registered the highest oil 5 11.34
and water absorption (5.93 and 4.12 g/g, respectively) 7 21.49
10 32.35
among all the samples studied. The bean flour had the low-
est oil and water absorption (1.67 and 1.O g/g, respectively). t Mean of triplicate analyses
Sosulski and Fleming (1977) reported water absorption Relstive viscosity (relative to distilled water) at room temperature
(21 C). The time required for water or sample dispersion to tra-
by soybean flour, soybean concentrate, sunflower flour, verse the fixed distance between the two marks on the viscometer
and sunflower concentrate to be 2.4, 3.6, 1.8, and 3.9 g/g. was measured.
Water absorption by the Great Northern bean flour ob-
served in the present investigation was lower than those by
soybean and sunflower flour reported by Sosulski and
Fleming (1977). However, water absorption by the Great
Northern bean protein concentrates noted in the present
investigation (5.93 g/g) was higher than those by soybean Table P-Water and oil absorption capacity of Great Northern bean
oroteins
and sunflower protein concentrates (Sosulski and Fleming,
1977); succinylated peanut flour (Beuchat, 1977); sunflower Water absorbeda Oil absorbeda
protein concentrate (control, succinylated, and acetylated) Sample k3lg) (9l9)
(Canella et al., 1979); soyflour, soy concentrate, and soy
isolate (Lin et al., 1974). Bean flour 1.67 1 .oo
It is known that water binding by proteins is a function Albumins 3.18 3.29
of several parameters including size, shape, conformational Globulins 2.77 3.23
Protein concentrates 5.93 4.12
characteristics, steric factors, hydrophilic-hydrophobic Protein isolates 2.73 1.57
balance of amino acids in the protein molecule, lipids and
carbohydrates associated with the proteins, thermodynamic a Mean of triplicate analyses
properties of the system (energy of bonding, interfacial
tension, etc.), physicochemical environment (pH, ionic
strength, vapor pressure, temperature, presence/absence of

Volume 46 (1981)-JOURNAL OF FOOD SCIENCE-73

 Table 3-Emulsion capacity and stability of Great Northern bean proteins

Initial Vol. of water separated (ml) at room temp (2l’C)

Oil vol. of after time fhr)
emulsified emulsion
Sample klld (ml) 10 20 35 60 100 120 140 160 180 200 780

Bean flour 39.6 208 104 104 116 120 120 120 120 120 120 120 120
Albumins 63.8 230 0 0 0 0 trace trace 1 1 1 1 5
Globulins 44.0 218 26 30 32 32 32 32 32 32 32 32 32
Protein cone 72.6 270 0 0 0 0 0 trace 1 1 1 1 30
Protein isolates 63.8 250 150 150 155 155 155 155 155 155 155 155 155

Table 4-Foaming capacity and stability of Great Northern bean proteins

wt Vol. Vol. (ml) at room temperature (21°C1

after after Vol. Specific after time fhr)
whipping whipping increase vol.
Sample (9) (ml) !%I (ml/g) 0.5 1.0 1.5 2.0 2.5 3.0 8.0 36.0

Egg albumin 91.50 140 40 1.53 140 135 130 125 125 125 125 115
Bean flour 99.80 132 32 1.32 132 128 110 106 104 102 100 100
Albumins 98.98 180 80 1.82 170 164 160 156 154 150 114 100
Globulins 96.44 140 . 40 1.45 130 126 120 118 116 114 104 100
Protein cone 99.67 164 64 1.65 150 122 107 104 104 102 100 100
Protein isolates 98.27 106 6 1.10 100 100 100 100 100 100 100 100

Emulsion capacity and stability

150 - Emulsion capacity of the Great Northern bean flour, al-
140 -
bumins, globulins, protein concentrates, and protein iso-
lates was,’respectively, 39.6, 63.8, 44.0, 72.6, and 63.8g
130 - oil/g dry sample (Table 3). Satterlee et al. (1975) studied
the emulsion capacity of the Great Northern bean proteins
120 - and found the emulsion capacities of the bean protein
concentrates, albumins, and globulins to be 13 1, 204, and
t 110 - 113 ml oil emulsified/g dry sample. They also found that
globulin emulsion was more stable than the albumin emul-
z 100 - sion. The present investigations indicated that the albumins
were better emulsifiers than globulins in relation to both
.E 90 - capacity and stability. Albumins registered the highest
emulsion stability (5 ml phase separation ater 780 hr stand-
: BO- ing at a room temperature of 21’C); protein concentrates,
kl however, had the highest emulsion capacity among all the
2 70- samples investigated. The differences observed in the emul-
z sion behavior in the present studies and those of Satterlee
= tio- et al. (1975) may have been predominantly due to the
s .llll~~~~~~. Albumins
0-v Protein concentrates
methods of preparation of the protein fractions.
.; 50 -
h--d Protein isolates
I
; 40- l ==S====O
Globulins Foaming
2 13-a-14 Bean flour The foaming capacity of the albumins was the highest
30 - while that of the protein isolates was the lowest among
the samples studied (Table 4). Protein concentrates per-
formed better than egg albumin powder in foamability and
globulins were comparable to the egg albumin powder.
However, none of the samples studied equalled egg albu-
II I I I I I I II mins in foam stability. Therefore, the foaming ability of
1 2 3 4 5 6 7 8 9 10 Great Northern bean proteins was rated as fair.
Concentration (e/l00 ml Water)- Foamability of the Great Northern bean proteins was
concentration dependent (Fig. 6). All the samples registered
increasing foamability with the increase in concentration of
Fig. 6-Effect of concentration on foaming ability of Great North-
solids, reaching a maximum at 10% (w/v) solids concentra-
ern bean proteins. tion.

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74-JOURNAL OF FOOD SCIENCE-Volume 46 (1981)

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Volume 46 (1981)-JOURNAL OF FOOD SCIENCE-81