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Food Research International 37 (2004) 355–365

www.elsevier.com/locate/foodres

Comparative study of the functional properties of bambarra


groundnut (Voandzeia subterranean), jack bean (Canavalia ensiformis)
and mucuna bean (Mucuna pruriens) flours
a,* b
K.O. Adebowale , O.S. Lawal
a
Department of Chemistry, University of Ibadan – Nigeria, Ibadan, Nigeria
b
Department of Chemical Sciences, Olabisi Onabanjo University, Ago-Iwoye, Nigeria
Received 14 August 2003; accepted 12 January 2004

Abstract

Functional properties of bambarra groundnut flour (BGF), jack bean flour (JBF) and mucuna bean (MBF) were determined. pH
dependent protein solubility profile revealed that highest solubility in all flours was at pH 10, while minimum solubility was obtained
at pH 4, which correspond to the isoelectric point. Gelation capacity was minimal at pH 4 for all of the flours. Increase in ionic
strength of the medium at low salt concentration ( 6 0.4 M) improved the gelation properties of the flours. Maltose, lactose, sucrose
and starch when added to the flours enhanced the gelation capacity of all flours. Oil absorption capacity of JBF, MBF and BGF
were 1.7, 1.6 and 1.3 ml g1 , respectively. Water absorption capacity of flours increased between ionic strength ranges of 0–0.2 M but
reduced with further increase in ionic strength. Emulsifying activity (EA) decreased as the concentration of flour in solution in-
creased. Maximum EA and emulsion stability (ES) were obtained at pH 10, while minimum values were read at isoelectric pH. EA
and ES of flours increased in the ionic strength range 0–0.4 M but reduced afterwards with further increase in NaCl concentration.
Foam stability (FS) of the flours increased as the concentration of flour solution increased and maximum values of 80.5%, 74.7%
and 77.0% were observed for JBF, BGF and MBF at 10% flour concentration. MBF had highest foam capacity (FC) of 68% at pH
2, while JBF and BGF recorded highest value of 50% and 61%, respectively, at pH 10. Foam stability was maximal at pH 4 for all
the fours. Low ionic strength (l 6 0:2 M) improved both foam capacity and stability of JBF while increases were recorded in FS and
FC of BGF and MBF up to l ¼ 0:4 M, after which further increase in ionic strength reduced the foaming properties of the flours.
Ó 2004 Elsevier Ltd. All rights reserved.

Keywords: Bambarra groundnut; Jack bean; Mucuna bean; Flours; Functional properties

1. Introduction & Davila-Ortiz, 2002) mucuna bean (Johnson & Brekke,


1983; Machuka, 2002) lupin seed (Lqari, Vioque, Pedr-
In Africa, malnutrition is prevalent due to lack of oche, & Millan, 2002), Pea (Johnson & Brekke, 1983),
sufficient animal protein, hence the search for alternative winged bean (Narayana & Narasinga Rao, 1984; Okezie
sources of protein from lesser-known legumes in lieu of & Bello, 1988), faba bean (Krause, Mothes, &
expensive and scarce animal protein. In view of this, Schwenke, 1996; Muschiolik, 1989; Muschiolik, Dick-
effort is geared at identifying and evaluating under-uti- inson, Murray, & Stainsby, 1987), chickpea (Liu &
lised protein sources. This development has stimulated Hung, 1998) and Gila bean (Siddhuraju, Becker, &
research on the utilisation of some under-utilised le- Makkar, 2001).
gumes such as mung bean (Dzudie & Hardy, 1996), lima The efforts geared towards legumes are predicated on
beans (Chel-Guerrero, Perez-Flores, Bentacur-Ancona, the fact that legumes have been established to be cheap
but abundant sources of protein (Aykroyd & Doughty,
*
Corresponding author.
1994). Seeds of mucuna beans (Mucuna pruriens),
E-mail addresses: adebowal@ictp.trieste.it, kay99esu@skannet. Bambarra groundnut (Voandzeia subterranean) and jack
com (K.O. Adebowale). beans (Canavalia ensiformis) are potential sources of

0963-9969/$ - see front matter Ó 2004 Elsevier Ltd. All rights reserved.
doi:10.1016/j.foodres.2004.01.009
356 K.O. Adebowale, O.S. Lawal / Food Research International 37 (2004) 355–365

abundant plant protein for many developing nations was mixed with 25-ml distilled water and the solution
because of their rich protein content (bambarra pH was adjusted to between 2 and 10, using 0.5 M
groundnut 26.2%; jack beans 29.0% and mucuna beans NaOH and 0.5 M HCl. The slurries obtained were
35.0%) (Duke, 1981). mixed for 1 h at 24 °C using a magnetic stirrer, after
For efficient utilisation and consumer acceptance of which they were centrifuged at 12,000g for 20 min at
legume seed flours, it is desirable to study their func- 4 °C. The supernatant was filtered through glass wool to
tional properties. The functional properties, which affect obtain a clear solution. The nitrogen content in the su-
the sensory characteristics of foods, play important roles pernatant was determined by kjeldahl method (AOAC,
in the physical behaviour of food or its ingredient during 1990). Triplicate determinations were carried out and
preparation, processing and storage. These properties solubility profile was determined by plotting averages of
include foaming, emulsification, texture, gelation, water protein solubility (%) against pH. The percentage solu-
and oil absorption capacity and viscosity. Various food ble protein (Nitrogen solubility  6.25) was calculated as
industries intensify on the desirable functional proper- follows:
ties with a view to improving them to meet their Amount of nitrogen in the supernatant
requirements. Solubility ð%Þ ¼ :
Amount of nitrogen in the flour
Our research effort has been directed at a systematic
study of the chemical and physical modification of
tropical underutilised legume starches and protein con- 2.4. Water and oil absorption capacity
centrates (Adebowale & Lawal, 2003a, 2003b, 2003c). In
continuation of our studies, we have chosen to consider The method of Beuchat (1977) was employed for the
the functional characteristics of flours derived from jack water and oil absorption capacity determination. One
bean, mucuna bean and bambarra groundnut, with a gram of sample was mixed with 10 ml distilled water or
view to providing useful information towards effective oil (Executive Chef oil, Unilever Nig. PLC) for 30 s. The
utilisation of these legumes in various food applications. samples were then allowed to stand at room temperature
(30  2 °C) for 30 min after which they were centrifuged
at 5000g for 30 min. The volume of supernatant was
2. Materials and methods noted in a 10-ml graduated cylinder. Studies were con-
ducted to investigate the influence of ionic strength on
2.1. Materials water absorption capacity by varying the ionic strength
of the medium using 0.1, 0.2, 0.4, 0.6, 0.8 and 1.0 M
Mucuna bean seeds were obtained from International NaCl solutions. Studies were conducted in triplicates.
Institute for Tropical Agriculture, Ibadan, Jack bean
seeds were obtained from seed unit, Department of 2.5. Gelation properties
Agronomy, University of Ibadan, while bambarra seeds
were obtained from a local market in Ibadan, Nigeria Gelation properties were studied by employing the
and identified at the Genetic Resources Unit of the method of Coffman and Garcia (1977). Sample suspen-
IITA, Ibadan. All chemicals used were of analytical sions of 2–20% were prepared in distilled water. Ten
(Analar) grade. millilitres of each of the prepared dispersions was
transferred into a test tube. The test tube was heated in a
2.2. Preparation of flours boiling water bath for 1 h, after which they were cooled
in a bath of cold water. The test tubes were further
Cleaned seeds of legumes species were soaked in cooled at 4 °C for 2 h. The least gelation concentration
distilled water at 30  2 °C for 10 h after which they was taken as the concentration when the sample from
were manually dehulled. The cotyledons were dried in inverted test tube did not fall or slip.
air for 72 h at room temperature 30  2 °C. Two kilo- Studies on the effect of pH on gelation were con-
grams of seeds from each legume species was then milled ducted by preparing sample solution at various con-
in household flourmill (Braun multimix Deluxe, Ger- centrations after which the pHs were adjusted from 2.0
many). They were ground to pass through a BS60 mesh to 10.0 before heating. Least gelation concentration was
screen, after which they were kept in a refrigerator at determined as described earlier.
about 4 °C prior use. Effect of ionic strength was investigated by preparing
sample suspensions (2–20% w/v) at various concentra-
2.3. Protein solubility tions in NaCl solution of varying ionic strength ranging
from 0.1 to1.0 M. Effect of carbohydrates was also
pH dependent protein solubility was studied using the studied by adding maltose, sucrose, lactose and potato
method of Were, Hettiarachchy, and Kalapathy (1997). starch at 0.25 g g1 of the flour. The LGC was deter-
One hundred and twenty-five milligrams of each flour mined as described earlier.
K.O. Adebowale, O.S. Lawal / Food Research International 37 (2004) 355–365 357

2.6. Emulsifying properties strength. Studies were conducted in solution of ionic


strength of 0.0, 0.1, 0.2, 0.4, 0.6, 0.8, and 1.0 M before
Emulsifying activity and stability were determined whipping vigorously. The effect of pH on foaming
using the method of Neto, Narain, Silvia, and Bora properties was studied by preparing flour dispersions at
(2001). Five millilitres portion of flour dispersion in various pH 2–10, using 0.5 M NaOH and 0.5 M HCl,
water (10 mg ml1 ) was homogenised with 5 ml oil followed by vigorous whipping as earlier described.
(Executive chef Unilever PLC) for 1 min. The emulsions Triplicate determination of each experiment was carried
were centrifuged at 1100g for 5 min. The height of out.
emulsified layer and that of the total contents in the tube
was measured. The emulsifying activity was calculated 2.8. Statistical analysis
as
Height of emulsified layer in the tube Statistical analysis of the results was done with sta-
EA ð%Þ ¼ tistics for windows 5.0 (1995) and the t test was used to
Height of the total content in the tube
determine significance of differences between means.
 100: Trends were considered significant when means of
Emulsion stability was determined by heating the compared sets differed at P < 0:05.
emulsion at 80 °C for 30 min before centrifuging at
1100g for 5 min
3. Results and discussion
Height of emulsified layer after heating
ES ð%Þ ¼ :
Height of emulsified layer before heating 3.1. Protein solubility
Effect of concentration on emulsifying activity and sta-
bility of flours was studied by preparing 2–10% w/v Protein solubility of flours is presented in Fig. 1. The
solution before conducting experiments as described result indicates that minimum solubility for all the flours
above. Influence of ionic strength was studied by pre- was at pH 4, while in all cases, the maximum solubility
paring flour dispersions in water at 10 mg ml1 of water was observed at pH 10. Generally, solubility reduced as
in solution of various ionic strength of 0.1, 0.2, 0.4, 0.6, the pH increased until it reached minimum at pH 4,
0.8 and 1.0 M NaCl solutions. followed by progressive increase in solubility as the pH
Influence of pH was studied by preparing flour dis- increased. At pH 7, which is the neutral pH, maximum
persions in water at 10 mgml1 of water in solution of solubility of 49.7% was observed in MBF while BGF
various pH (2–10). Experiments were conducted in had the least value of 43.6%. Earlier, similar results have
triplicates. been reported for flours of different phaseolus species
such as blackgram (Sathe & Salunkhe, 1981) and mung
2.7. Foaming properties bean (Thompson, 1977). In addition, such pattern has
also been reported for peas and faba bean (Sosulski &
The method of Coffman and Garcia (1977) was used Mc Curdy, 1987) and winged bean (Okezie & Bello,
for the determination of the foaming capacity and sta-
bility of legume flours. A weighed amount of flour was
dispersed in 100-ml distilled water, after which the sus- 70
pension was whipped vigorously for 2 min using a
Phillips kitchen blender set at speed 2. Volumes were 60
Protein solubility (%)

recorded before and after whipping. The percentage


volume increase was calculated according to the fol- 50
lowing equation:
40
%Volume increase ¼ ðV2  V1 Þ=V1  100;
where V2 is the volume of protein solution after whip- 30
MBF
ping and V1 is the original volume of protein solution. JBF
Foam stability (FS) was determined as the volume of 20 BGF
foam that remained after 8 h expressed as a percentage
of the initial foam volume. 10
Studies were conducted to study the effect of con- 2 4 6 8 10

centration on the foaming properties by whipping 2, 4, pH


6, 8 and 10% w/v of the dispersion as described above. Fig. 1. Protein solubility profile of flours. BGF – bambarra groundnut
Influence of ionic strength was studied by dispersing flour; MBF – mucuna bean flour; JBF – jack bean flour. Error bars:
2 g of flour in 100 ml NaCl solutions of various ionic Standard deviations. Results are means of triplicate determinations.
358 K.O. Adebowale, O.S. Lawal / Food Research International 37 (2004) 355–365

1988). Also, Narayana and Narasinga Rao (1982) had BGF


reported minimum nitrogen solubility of 23% at pH 4.5 6.0
MBF
for winged bean while cowpea powder had a minimum 5.5

Water absorption capacity (Ml.g -1)


JBF
5.0
nitrogen solubility of 19.36% at pH 4.0 (Okaka &
4.5
Potter, 1979). At high acidic pH, the protein molecules
4.0
got net positively charged while they became net nega-
3.5
tively charged at alkaline pH. These developments fa- 3.0
cilitated repulsion among the molecules and increased 2.5
the solubility of the protein molecules. Variations ob- 2.0
served in the solubility profile of different legume flours 1.5
are possibly due to physiological composition differ- 1.0
ences. Similar reason has been advanced earlier (Chau & 0.5
Cheung, 1998). 0.0
0.0 0.1 0.2 0.4 0.6 0.8 1.0
Ionic strength (M)
3.2. Oil and water absorption capacity
Fig. 3. Effect of ionic strength on water absorption capacity of flours.
BGF – bambarra groundnut flour; MBF – mucuna bean flour; JBF –
Oil absorption capacity of flours is presented in
jack bean flour. Error bars: Standard deviations. Results are means of
Fig. 2. Maximum lipophilic tendency of 1.7 ml g1 was triplicate determinations.
observed in JBF, followed by 1.67 ml g1 as observed in
MBF while the least value of 1.37 ml g1 was recorded in pacity of flours increased with increase in ionic strength
BGF. The values are consistent with those previously of solution up to 0.2 M. Further increase in ionic
reported for flours of P. angularis (1.47 ml g1 ), strength from 0.4 to 1.0 M reduced the WAC of the
P. calcaratus (1.287 ml g1 ), D. Labalab (1.197 ml g1 ), flours progressively. In the control solution, highest
soybean (1.937 ml g1 ) (Chau & Cheung, 1998), lupin hydrophilic tendency of 5.06 ml g1 was observed in
seed bean (1.67 g g1 ) (Sathe, Deshpande, & Salunkhe, JBF. MBF had WAC of 2.3 ml g1 while the least WAC
1982), great Northern bean (3.29 g g1 ) (Sathe & was recorded in BGF. In previous reports, 2.65 and
Salunkhe, 1981) and P. lunatus flour (1.83 g g1 ) (Chel- 3.80 g g1 WAC had been reported for P. lunatus flour
Guerrero et al., 2002). Variations in the presence of non- and C. ensiformis flours, respectively (Chel-Guerrero
polar side chains, which might bind the hydrocarbon et al., 2002). 3.9 g g1 for Tepary bean flour (Idouraine
side chains of oil among the flours, possibly explain et al., 1991), 1.67 g g1 for great Northern bean flour
differences in the oil binding capacity of the flours. (Sathe & Salunkhe, 1981) and winged bean flour,
However, the flours are potentially useful in structural 2.75 g g1 (Okezie & Bello, 1988). Different protein
interaction in food especially in flavour retention, im- structure and the presence of different hydrophilic car-
provement of palatability and extension of shelf life bohydrates might be responsible for variations in the
particularly in bakery or meat products where fat ab- WAC of the flours. It is suggested that initial increase in
sorption is desired. ionic strength enhanced protein unfolding and this
Effect of ionic strength on water absorption capacity caused exposure of buried functional groups, which en-
of flours is presented in Fig. 3. Water absorption ca- hanced water absorption capacity. At higher salt con-
centrations, much of the water was bound to the salt ions
and this led to dehydration of flours, with subsequent
1.8
reduction in water absorption capacity. Imbibition of
1.6 water is an important functional trait in foods, such as
Oil absorption capacity (ml.g -1)

1.4 sausages, custards and doughs. In these foods, proteins


1.2
imbibe water, but do not dissolve because of insufficient
water. Consequently, they swell and impart characteris-
1.0
tics, such as body thickening and viscosity. The results
0.8 suggest that MBF, JBF and BGF could be used as in-
0.6 gredients in the preparation of comminuted products
such as sausages, since these properties enable bakers to
0.4
add more water to doughs so as to improve handling
0.2 characteristics and maintain freshness in the bread.
0.0
MBF BGF JBF
3.3. Gelation properties
Fig. 2. Oil absorption capacity of flours. BGF – bambarra groundnut
flour; MBF – mucuna bean flour; JBF – jack bean flour. Error bars: Effect of concentration and pH on gelation capacity
Standard deviations. Results are means of triplicate determinations. of legume flours is presented in Table 1. Using the least
K.O. Adebowale, O.S. Lawal / Food Research International 37 (2004) 355–365 359

Table 1 Table 2
Effect of concentration and pH on gelation capacity of floursa Effect of ionic strength and concentration on gelation capacity of
floura
Sample pH 2 pH 4 pH 7 pH 8 pH 10
Sample Control Ionic strength (M)
JBF 16 12 14 16 16
BGF 16 14 16 16 16 0.1 0.2 0.4 0.6 0.8 1.0
MBF 18 14 16 16 18
JBF 14 8 8 8 12 14 16
a
Values are least gelation concentration expressed as % w/v. BGF 16 12 10 10 16 16 16
MBF 16 10 8 8 10 12 12
gelation concentration as the index of gelation capacity, a
Values are least gelation concentration expressed as % w/v.
low LGC means better gelation property. The lowest
LGC for all legume flours were obtained at pH 4, while further increase in ionic strength up to 0.6 M raised the
highest LGC values were obtained at pH 2 and 10. At LGC again to the same level as the control (16% w/v).
pH 7, among the flours, minimum LGC was recorded in However, as the ionic strength increased further, a
JBF, while MBF and BGF had the same value. Similar constant value of 16% w/v was maintained. Increase in
pH dependent gelation capacity had been reported for ionic strength of solution also reduced the LGC of JBF.
mucuna protein concentrate (Adebowale & Lawal, Although no changes were observed in LGC (8% w/v)
2003a, 2003b, 2003c), Pigeon pea and cowpea (Mwa- from 0.1 to 0.4 M, increase in ionic strength up to 0.6 M
saru, Muhammad, Bakar, & Cheman, 1999). The least raised the LGC again and it increased progressively
gelation capacity of MBF, BGF and JBF were compa- until it reached the highest value of 16% w/v at 1.0 M.
rable to those of phaseolus vulgaris L. flour (Deshpande, However, it is noteworthy that the LGC value of JBF in
Sathe, Cornforth, & Salunkhe, 1982) and black gram the control solution (14% w/v) is lower than 16% w/v
flour (Sathe, Deshpande, & Salunkhe, 1983). Variations obtained in 1.0 M. Akintayo et al. had earlier reported
in gelling properties are due to the ratio of different ionic strength dependent gelation properties for Cajanus
constituents such as proteins, lipids and carbohydrates cajan protein. In their report, the gelation capacity of
in different legume flours. flour improved at low ionic strength (0.5 M), while it
Protein gelation is vital in the preparation and ac- reduced at high ionic strength solution (1.0 M). They
ceptability of many foods, including vegetable and other attributed improvement in gelation capacity at low ionic
products. Gelation mechanism and gel appearance are strength to enhanced protein solubilisation to the salt
fundamentally controlled by the balance between at- solution, which created an effective overlapping of the
tractive hydrophobic interactions and repulsive electro- functional groups between adjacent protein molecules, a
static interactions (Egelandsal, 1980). The repulsive condition necessary for a network of gel formation.
forces are due to surface charges and the attractive Ziegler and Foegeding (1990) posited that increase in
forces are due to various functional groups exposed by ionic strength tends to reduce electrostatic repulsion
the thermal unfolding of the protein (Kojima & Na- between proteins due to the shielding of ionisable groups
kamura, 1985). The pH of protein dispersions has pro- by mobile ions. Van Camp, Messens, Clement, and
found effect on gelation reactions by influencing the Huyghebaert, 1997 also postulated that addition of so-
balance of polar and non-polar residues. At pH values dium chloride to whey protein solution provided a
in the region of isoelectric pH, protein–protein interac- shielding effect that strongly reduces the repulsive forces
tions are generally favoured because the net surface acting among proteins. However, increase in LGC par-
charge is close to zero, which significantly reduces the ticularly at 0.6 M may be a result of reverse in protein
repulsive interactions between protein molecules (Wal- unfolding with increasing ionic strength. Decrease in
stra & Jenness, 1984), while at pH far removed from protein unfolding limited access to reactive side groups
Isoelectric points, the surface charge on the protein is within the protein molecules, a condition necessary for
large and significant repulsive forces prevent protein– the formation of a three-dimensional network structure
protein interaction (Elofsson, Dejmek, Paulson, & as seen in protein gels. Similar observation had been
Burling, 1997). reported earlier (Boye, Alli, Ismail, Gibbs, & Konishi,
Effect of ionic strength and concentration on gelation 1995).
capacity of flours is presented in Table 2. Increase in Effect of concentration and carbohydrates on gela-
ionic strength of the protein solution generally reduced tion capacity of flours is presented in Table 3. Generally,
the LGC of MBF compared with the control. LGC re- addition of carbohydrates improved the gelation ca-
duced with increasing ionic strength until it reached pacity of legume flours. Least gelation capacity was
0.4 M after which further increase in ionic strength in- reduced following the addition of maltose, lactose, su-
creased the LGC. However, even at 1.0 M, LGC (12% crose and starch. Previously, we have reported reduction
w/v) was still lower than 16% w/v in the control MBF in least gelation capacity of mucuna bean protein con-
solution. In a similar pattern, increase in ionic strength centrate, following the addition of carbohydrates
of solution reduced the LGC of BGF up to 0.4 M while (Adebowale & Lawal, 2003a, 2003b, 2003c). Turgeon
360 K.O. Adebowale, O.S. Lawal / Food Research International 37 (2004) 355–365

Table 3
MBF
Effect of concentration and carbohydrates on gelation capacity of
BGF
floursa
90
JBF
Sample Control Maltose Lactose Sucrose Starch
80
JBF 14 6 8 10 8
BGF 16 8 10 14 8 70

Emulsifying activity (%)


MBF 16 6 10 10 6
a
60
Values are least gelation concentration expressed as % w/v.
50

and Beaulieu (2001) have also reported improvement on 40

protein gel texture using carbohydrates. It has also been 30


reported that sucrose increased the gelation rate of
20
protein solutions (Bryant & Mc Clements, 2000). Im-
provement in gelation capacity following the addition of 10

carbohydrates is because of decrease in thermodynamic 0


affinity of proteins for the aqueous solution, which in- 0.0 0.1 0.2 0.4 0.6 0.8 1.0
Ionic Strength (M)
creased the interaction between proteins.
Fig. 4. Effect of ionic strength on emulsifying activity of flours. BGF –
bambarra groundnut flour; MBF – mucuna bean flour; JBF – jack
3.4. Emulsifying properties bean flour. Error bars: Standard deviations. Results are means of
triplicate determinations.

Emulsifying activity and stability of the flours were


concentration dependent as shown in Figs. 10 and 11.
Generally, emulsifying activity decreased as the con- MBF
JBF
centration of flour in solution increased. At all concen-
BGF
tration studied (2–10% w/v), BGF exhibited highest EA, 80
followed by MBF while least EA was observed in JBF.
Emulsifying stability of BGF increased progressively
as concentration increased until it began to decline with 60
Emulsion stability (%)

increasing flour concentration from 6% w/v upward.


Emulsion stability of MBF and JBF reduced as the
concentration of flour in the solution increased. Such 40
concentration dependent emulsifying properties have
been reported by Sathe et al. (1982). In their report,
emulsion capacity of winged bean protein reduced as the 20
concentration of protein in solution increased. The re-
sult is also in agreement with those of Lin, Humbert,
0
and Sosulski (1974) on emulsifying properties of sun- 0.0 0.1 0.2 0.4 0.6 0.8 1.0
flower and soybean flours and protein concentrates. Ionic Strength (M)
Concentration dependent emulsifying activity has been
Fig. 5. Effect of Ionic strength on emulsion stability of flours. BGF –
explained based on adsorption kinetics (Phillips, 1981). bambarra groundnut flour; MBF – mucuna bean flour; JBF – jack
When protein concentration is low, the rate of adsorp- bean flour. Error bars: Standard deviations. Results are means of
tion is diffusion controlled, but at high protein concen- triplicate determinations.
tration, there is an activation barrier to adsorption.
Under the later conditions, the ability of the protein
molecule to create space in the existing film and to decline in EA was observed. Minimum values of 45.5%,
penetrate and rearrange on the surface is rate deter- 73.9% and 42.0% were observed for MBF, BGF and
mining. Initial increase in emulsion stability of BGF JBF, respectively, in 1.0 M NaCl solutions. In the con-
with increasing concentration up to 6% w/v could be trol solution, highest value of 79.8% was observed in
explained based on increase in rigidity of interfacial la- BGF solution, while MBF and JBF had 48.5% and
mella (Halling, 1981). Effect of ionic strength on emul- 47.8%, respectively. In a similar way, emulsion stability
sifying activity and emulsion stability is presented in improved with initial increase in ionic strength of the
Figs. 4 and 5, respectively. Emulsifying activity of all solution and increases were observed up to 0.4 M.
flours increased progressively as the ionic strength of the Following a similar pattern with EA, emulsion stability
media increased until it reached the highest values in declined with further increase in ionic strength and
0.4 M NaCl solutions, following which a progressive minimum values in all flours were recorded in 1.0 M
K.O. Adebowale, O.S. Lawal / Food Research International 37 (2004) 355–365 361

NaCl solutions. Influence of ionic strength on emulsi- JBF


fying properties of cowpea protein had earlier been re- BGF
ported by Aluko and Yada (1995). Chavan, Mc Kenzie, MBF
and Shhidi (2001) also reported ionic strength depen-
80
dent emulsifying properties for beach pea. Wagner and
Gueguen (1995) attributed higher emulsion stability of

Emulsion stability (%)


soy protein at low ionic strength to dissociation of 60
Oligomeric structure of 11S-glycinin and subsequent
improvement of surface behaviour. Emulsifying prop-
erties of proteins depend basically on two effects: (i) A 40

substantial decrease in interfacial energy due to the ad-


sorption of the protein at the oil–water interface and (ii)
20
the electrostatic, structural and mechanical energy bar-
rier caused by the interfacial layer that opposes desta-
bilisation processes (Wagner & Gueguen, 1999). Initial 0
2 4 6 7 8 10
increase in ionic strength of the solutions up to 0.4 M
pH
enhanced the formation of charged layers around the fat
globules and this resulted in mutual repulsion among Fig. 7. Effect of pH on emulsion stability of flours. BGF – bambarra
them. Also at low ionic strength, formation of hydrated groundnut flour; MBF – mucuna bean flour; JBF – jack bean flour.
layer around the interfacial material resulted in lower Error bars: Standard deviations. Results are means of triplicate
determinations.
interfacial energy and retarded droplet coalescence. At
higher ionic strength (6.0–1.0 M), protein unfolding was
decreased. This development probably limited adsorp- all the samples while the lowest values were observed at
tion of the protein at the oil–water interface. pH 4, which corresponds to the isoelectric pH. After pH
Both emulsifying activity (Fig. 6) and stability (Fig. 7) 4, both EA and ES increased as the pH of the solution
were pH dependent. Generally, maximum EA was ob- increased. In previous studies, such pH dependent
served at pH 10, while the minimum value of 21.9%, emulsifying activity and emulsion stability has been re-
51.6% and 20.6% were recorded for MBF, BGF and ported for proteins of Cajanus cajan and Vigna unguic-
JBF, respectively, at pH 4. Among the samples at pH 7, ulata (Mwasaru et al., 1999), Phaseolus lunatus and
the highest value of 80.0% was observed in bambarra Canavalia ensiformis (Chel-Guerrero et al., 2002) and
groundnut flour while JBF had the lowest value of flours of P. angularis, P. calcaratus, D. lablab and Soy-
47.8%. Similarly, emulsion stability followed the same bean (Chau & Cheung, 1998). The pH dependent
pattern with E.A. Higher ES were recorded at pH 10 in emulsifying activity follows the same pattern with the
pH dependent solubility of the flours; hence it is rea-
sonable that protein solubility influenced the EA of the
flours. The net charge at the hydrophilic–lipophilic in-
MBF terface is dependent on pH of the solution and it may
BGF
impede or facilitate emulsifying activity of the proteins.
JBF
90
Variation in EA of the flours across the pH scale is
possibly as a result of interactions of other components
80
of the flours that influence their properties. Our obser-
Emulsifying activity (%)

70 vations agree with the general correlation between EA


60 and protein solubility as reported in previous works
50
(Abbey & Ibeh, 1988; Shanmujasundaram & Venka-
taraman, 1989). Although contrarily, Kamat, Graham,
40
and Davis (1978) reported improved emulsion stability
30 at region of isoelectric pH, the result obtained in this
20 work agrees with the observations of Sathe et al. (1982)
10
and Chau and Cheung (1998). Franzen and Kinsella
(1976) had earlier concluded that ES was near minimum
0
2 4 6 7 8 10 in isoelectric pH range due to aggregation and desta-
pH bilisation of the interfacial membrane. The relatively
high ES as observed at pH 10 and 2 may be as a result of
Fig. 6. Effect of pH on emulsifying activity of flours. BGF – bambarra
groundnut flour; MBF – mucuna bean flour; JBF – jack bean flour. higher levels of solubilised proteins, which may influence
Error bars: Standard deviations. Results are means of triplicate ES through film encapsulation and a balance of the at-
determinations. tractive van der Waals and repulsive electrostatic forces.
362 K.O. Adebowale, O.S. Lawal / Food Research International 37 (2004) 355–365

Good emulsifying properties of the flours under inves- Both foam capacity (Fig. 8) and stability (Fig. 9) were
tigation make them potentially useful in food products pH dependent. MBF had highest foam capacity of 6% in
like milk-like beverages and meat analogs. acidic medium (pH 2) while JBF and BGF recorded peak
values of 50% and 61% at pH 10. In all the samples,
3.5. Foaming properties minimum FC was observed at pH 4. Generally, FC in-
creased with increasing pH after the isoelectric point.
Effect of concentration on foam capacity is presented Also foam stability was highest at pH4 for all flours. JBF
in Table 4. Foam capacity of JBF increased from 52% in had minimum ES value of 70% at pH 2, while BGF and
2% w/v solution to 58% in 4% w/v solution, after which MBF had minimum values of 62.11% and 61.0%, re-
foam capacity reduced progressively as the concentra- spectively, at pH 10. In a previous report, Chel-Guerrero
tion of flour in solution increased and minimum value of
50.3% was recorded in 10% w/v solution. Contrarily, a
progressive increase in foam capacity was observed in
BGF and MBF as the concentration of flour in solution JBF
BGF
increased. It is noteworthy however that BGF recorded
MBF
FC value of 70% at 8% w/v and also at 10% w/v. Foam
70
stability of all flours increased with concentration of
flour in solution (Table 5) and highest FS in all the 60
samples were recorded in 10% w/v. Increase in foam

Foam Capacity (%)


capacity and stability of mucuna protein with increase in 50
protein concentration had been reported earlier (Adeb- 40
owale & Lawal, 2003a, 2003b, 2003c). Also, improved
foaming properties with increasing concentration of 30
flour have been reported for glandless cottonseed flour
20
(Cherry & Mc Watters, 1981). Increase in protein con-
centration facilitated enhanced protein–protein interac- 10
tion at the air–water interface and this promoted
0
formation of a highly viscoelastic multiplayer film that 2 4 6 7 8 10
offers resistance to coalescence of bubbles. This devel- pH
opment enhanced foam stability. Foamability generally
Fig. 8. Effect of pH on foam capacity of flours. BGF – bambarra
reaches a maximum value at a point as the concentra- groundnut flour; MBF – mucuna bean flour; JBF – jack bean flour.
tion of protein increases. This might be responsible for Error bars: Standard deviations. Results are means of triplicate
reduction in foam capacity of JBF from 6% to 10% w/v. determinations.

Table 4
Effect of concentration on foam capacity of floursA;B
Sample Concentration (% w/v)
2 4 6 8 10
a a a a
JBF 52.0  2.4 60.0  4.2 55.0  5.5 54.6  3.0 50.3  4.2a
BGF 57.0  1.0a 58.0  1.2a 64.0  7.1b 70.0  2.9b 70.0  5.8b
MBF 41.0  2.5b 44.0  2.0b 48.0  1.6c 52.0  3.4a 61.0  2.0b
A
Each value represents the mean of three determinations  SD.
B
Samples followed by the same letter are not significantly different ðp < 0:05Þ.

Table 5
Effect of concentration on foam stabilityA;B
Sample Concentration (% w/v)
2 4 6 8 10
JBF 67.0  1.4a 68.8  2.3a 74.8  4.6a 77.6  3.0a 80.5  4.5a
BGF 70.1  5.8a 72.7  5.5a 73.2  3.2a 73.5  6.8a 74.7  2.0a
MBF 70.9  2.0a 71.5  1.4a 72.3  1.5a 76.9  2.0a 77.0  1.5a
A
Each value represents the mean of three determinations  SD.
B
Samples followed by the same letter are not significantly different ðp < 0:05Þ.
K.O. Adebowale, O.S. Lawal / Food Research International 37 (2004) 355–365 363

JBF JBF
BGF BGF
100
MBF MBF
100
90
80
80

Emulsion stability(%)
Foam stability (%)

70
60
60
50
40
40
30
20 20
10
0 0
2 4 6 7 8 10 2 4 6 8 10
pH Concentration (%)

Fig. 9. Effect of pH on foam stability of flours. BGF – bambarra Fig. 11. Effect of concentration on emulsion stability of flours. BGF –
groundnut flour; MBF – mucuna bean flour; JBF – jack bean flour. bambarra groundnut flour; MBF – mucuna bean flour; JBF – jack
Error bars: Standard deviations. Results are means of triplicate de- bean flour. Error bars: Standard deviations. Results are means of
terminations. triplicate determinations.

and Yada, 1995). Previous studies have indicated that


JBF protein stabilised foams are more stable in the neigh-
BGF bourhood of the isoelectric pH of the protein than at any
MBF
other pH (Buckingham, 1970; Sathe et al. (1982)). High
60 foam stability at pH 4 is due to formation of stable mo-
lecular layers in the air–water interface of the foams. In
50
Emulsifying activity (%)

addition, the protein has low net charge near isoelectric


pH; this might have contributed to the formation of
40
stable molecular layers in the air–water interface, which
30
imparted stability to the foam.
Effect of ionic strength on foam capacity is presented
20 in Table 6. Initial increase in ionic strength from 0.0 to
0.2 M improved the FC of JBF from 52% to 62%.
10 However, further increase in ionic strength from 0.4–1.0
M put the foam capacity of the flour on a decline and
0
2 4 6 8 10
minimum value of 39% was recorded in 1.0 M NaCl
Concentration (%w/v) solutions. Foam capacity of BGF over ionic strength
range of 0.0–1.0 M ranged from 57% to 80% and foam
Fig. 10. Effect of concentration of sample on emulsifying activity of
capacity of the flour increased as the ionic strength in-
flours. BGF – bambarra groundnut flour; MBF – mucuna bean flour;
JBF – jack bean flour. Error bars: Standard deviations. Results are creased. FC of MBF increased from 41% in control
means of triplicate determinations. solution to maximal value of 54% in 0.4 M NaCl solu-
tions. Further increase in ionic strength of the solution
reduced the foaming capacity progressively and minimal
et al. (2002) reported a pH dependent foam properties for value of 36% was observed in 1.0 M NaCl solutions.
Phaseouls lunatus and Canavalia ensiformis flours. Our Effect of ionic strength on foam stability is presented
observations on minimum FC at pH 4 agree with the in Table 7. Increase in ionic strength improved the foam
findings of Chau and Cheung (1998), in which minimum stability of JBF up to 0.2 M. Progressive reduction in ES
foam capacity of 80.8%, 64.4%, 76.4% and 110% were was however observed with further increase in ionic
recorded for P. angularis, P. calcaratus and D. lablab and strength and minimal value of 31.9% was observed
soybean flours, respectively, at isoelectric point. The in 1.0 M NaCl solutions. Also increases were observed in
higher FC at the two extreme pHs has been attributed to FS of BGF as the ionic strength of the protein solution
the increased flexibility of the proteins in the flours, which increased and maximal value of 79.44% was observed in
diffused more rapidly to the air–water interface to en- 1.0 M NaCl solutions. FS of MBF reached peak value
capsulate air particles and then enhance foaming (Aluko of80.3% at 0.4 M solutions, followed by progressive
364 K.O. Adebowale, O.S. Lawal / Food Research International 37 (2004) 355–365

Table 6
Effect of ionic strength on foam capacity of flours (%)A;B
Sample Control Ionic strength (M)
0.1 0.2 0.4 0.6 0.8 1.0
a a a a a a
JBF 52.0  1.0 58.0  2.0 62.0  2.2 50.2  2.1 48.0  3.2 47.0  3.2 39.0  4.0a
BGF 57.1  1.5a 58.0  3.4a 62.0  2.9a 71.1  3.0b 73.4  2.4b 74.0  2.0b 80.5  2.0b
MBF 41.0  2.4a 43.0  2.0b 52.0  3.5b 54.0  2.3a 39.0  3.7a 37.8  2.5b 36.4  2.5a
A
Each value represents the mean of three determinations  SD.
B
Samples followed by the same letter are not significantly different ðp < 0:05Þ.

Table 7
Effect of ionic strength on foam stability of flours (%)A;B
Sample Control Ionic strength (M)
0.1 0.2 0.4 0.6 0.8 1.0
JBF 67.1  3.1a 72.8  4.0a 72.8  2.3a 66.6  3.6a 57.56  2.0a 48.0  3.5a 31.9  2.5a
BGF 70.1  2.0a 70.8  2.5a 71.0  1.0a 72.1  1.0ab 72.8  2.6b 73.5  2.5b 79.6  2.0b
MBF 70.9  3.0a 76.9  3.6a 78.9  1.7a 80.5  1.2b 77.6  4.0b 76.2  3.0b 75.0  2.8b
A
Each value represents the mean of three determinations  SD.
B
Samples followed by the same letter are not significantly different ðp < 0:05Þ.

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