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Volume 63, No. 2, 1998JOURNAL OF FOOD SCIENCE 229

Flow Properties of Chickpea Proteins

L.H. LIU and T.V. HUNG

ABSTRACTABSTRACTABSTRACTABSTRACTABSTRACT

Flow properties of aqueous chickpea protein dispersions were investigated. Thedispersions had Newtonian flow behavior at concentrations up to 4%. Flow be-havior became progressively less Newtonian as concentration increased above4%. The apparent viscosity of the dispersions was pH and concentration depen-dent, being higher at the proteins most soluble pHs (pH 2 and 9) and lower at theisoelectric point (pH 4-5). Within the investigated temperatures (15, 25, 35 and55C), power law constants were unchanged up to 35C but the flow behaviorbecame non-Newtonian at 55C. Denaturation by urea and sodium dodecyl sul-phate (SDS) increased the consistency index (m), casson yield stress and appar-ent viscosities, and the flow became more pseudoplastic with a decrease in theflow index (n).

Key Words: chickpea, protein dispersions, flow properties

Howell and Lawrie, 1987). Our objective was

to determine quantitative flow properties ofchickpea protein dispersions and the relevant

factors affecting their behavior.

CHEMISTRY/BIOCHEMISTRY

Authors Liu and Hung are with Food Science Australia,Private Bag 16, Werribee, Victoria, 3030, Australia.

MATERIALS & METHODS

Chickpea protein isolate

The isolate was prepared from whole seed

flour of the Kaniva cultivar, grown in Hor-

sham, Victoria. The procedure was described

previously (Liu et al., 1994) and as outlined

(Fig. 1) was applied to produce isolates at a

pilot scale plant at the Food Science Austra-

lia, Melbourne. The flour (40 kg) was extract-

ed with water (200 L), and the extract ad-

justed to pH 9 with 3M NaOH at 25C for 60

min. The slurry was separated with a com-

mercial decanter (SD230, Nilsen company)

and the residue was extracted with another

100 L of water. The combined extracts weredesludged and precipitated at pH 4.2 with 3M

HCl. The crude precipitated curd was

INTRODUCTIONCHICKPEA (CICERARIETINUML.) ISAPRO-tein rich crop, ranked as the 5th most impor-

tant grain legume produced in the world (Ue-

bersax and Ruengsakulrach, 1989). Chick-

pea seeds have been used for many traditional

foods (Pushpamma and Geervani, 1987) and

as ingredients in bakery products, imitation

milk, infant formula and meat products (Ver-

ma et al., 1985; Morcos et al., 1983; Ferman-

dez and Berry, 1989; Sosulski et al., 1978;

Hung and Nithianandan, 1993).

The nutritional value of chickpea protein

compares favorably with that of other grain

legumes (Williams and Singh, 1987; Push-

pamma and Geervani, 1987). The effectiveutilization of proteins in the food industry

depends on nutrient value and functional

properties (Kinsella, 1976). Unlike soybean

and other grain legume proteins, information

on functional properties, particularly quan-

titative flow properties, of chickpea protein

dispersions is scarce (Hulse, 1991; Chavan

and Salunkhe, 1986).

Flow properties are important in the de-

sign of unit operations such as mixing and

pumping as well as the formulation of the

most popular forms of chickpea based foods

such as paste or beverages (Hermansson,

1975; Fermandez, 1987; Rao, 1977). Flowproperties of protein dispersions are affect-

ed by environmental factors such as pH, ionic

strength, temperature and conditions under

which the protein is processed (Rha, 1978).

Such factors, influence the geometry and

behavior of a protein. Consequently, chang-

es in flow behavior of a protein dispersion

under certain conditions reflect changes in

protein molecular structure and/or protein-

protein interactions caused by environmen-

tal and processing condition (Tung, 1978;

Fig. 1 Schematic of chickpea protein isolate procedure.


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230 JOURNAL OF FOOD SCIENCEVolume 63, No. 2, 1998

washed, neutralized and pasteurized before

spray drying. The isolate contained about

89% protein, measured by a LECO combus-

tion system (Liu et al., 1994).

Protein dispersions and flowproperties

Protein dispersions (2, 4, 8, 12, 16 and

20% by weight of dry matter) were prepared

by mixing the protein in an ultramixer (Ultra

Turrax, TS25, 20,000 rpm) for 5 min. Each

dispersion was adjusted to pH 7 with 1M

NaOH. The protein dispersions were kept at

5C for 24h before their flow properties were

examined. After being placed in the rheome-

ter, each sample was equilibrated at the des-

ignated temperature for 25 min, before four

readings were recorded at each shear rate. The

shear rate/shear stress characteristics of each

protein dispersion were measured with a

Rheometer (Rheometer 30, Germany), based

on rotational stresses at shear rates from

0.599 sec1 to 1955 sec1 at 25C. For a thin

dispersion, a coaxial cylinder type cup MS-O was used while cup A, B or C was used

for thick dispersions, based on the initial

measurement with the rheometer.

The following power law equation was

used to express the flow properties of chick-

pea protein dispersions (Ma, 1983):

mn (1)

or log nlog logm (2)

is the shear stress (mPa), is the shear rate

(sec1), n is the flow index, m is the consis-

tency coefficient.The yield values of the protein dispersions

were calculated by the Casson equation:

k0 k1 (3)

The yield stress value (y = k02) was ob-

tained by extrapolating the rheogram of

vs to zero shear rate.The apparent viscosity was calculated by:

m n1 (4)

Effect of temperature and pH

Protein dispersions at 8% concentrationwere used to investigate the effects of tem-

perature (15, 25, 35 and 55C). Similarly, pro-

tein dispersions at 8% concentration were

readjusted to pH 2, 5, 7 or 9 with 1M NaOH

or HCl and measured at 25C using the Rhe-

ometer as above.

Effect of ionic strength and proteindenaturation

Protein dispersions at 8% concentration

were prepared with 0.2, 0.5, 1 and 2M NaCl

solution and flow properties were measured

at 25C and at pH 7. The effect of protein

denaturation on flow properties was exam-ined using 8% protein dispersions in 6M urea

and in 1% sodium dodecyl sulphate (SDS)

solution. The dispersions were prepared by

mixing the protein for 1 h in urea or SDS

solution at 25C.

RESULTS & DISCUSSION

Effect of concentration

The flow curves of chickpea protein dis-

persions at different concentrations were es-

tablished (not shown) and their slopes in-

creased with increasing concentration. Up to

8%, the flow curves were linear, indicating

Newtonian or near Newtonian behavior.

Shear stress () was a function of shear rateon a logarithmic scale for these chickpea pro-

tein dispersions (Fig. 2).

Flow properties of many food protein dis-

persions have been reported to be character-

ized by the power Eq. (2) at several concen-

trations. Hermansson (1975) found that the

flow properties of soy protein isolate, casein-

ate and whey protein concentrate conformed

with the power equation at several concen-

trations. Similar observations were reported

Flow Properties of Chickpea Proteins . . .

for aqueous sunflower protein dispersions

(Lefebvre and Sherman, 1977). Mita and

Matsumoto (1980) found an excellent linear-

ity of shear stress-shear rate plots at a shear

rate range of 100-1000 sec1 for gluten dis-

persions of different concentrations. Similar

results were observed in our study for chick-

pea protein dispersions with good linearity

at shear rates of 100 to 1750 sec1. The ef-

fect of protein concentration was studied on

power law constants and apparent viscosity

of chickpea protein dispersions (Table 1). Up

to 8% concentration, the dispersions were

Newtonian (n1) or near Newtonian as theapparent viscosities were unchanged with dif-

ferent shear rates (81.4 and 950 sec1). At

higher concentrations, non-Newtonian be-

havior became more pronounced (n0.94 to0.85). The apparent viscosities were affect-

ed by the change of shear rates, particularly

at low range (100 sec1) (Fig. 3). The con-

sistency coefficient (m) increased exponen-

tially with increasing concentrations

(mAec, Fig. 4a). An exponential increase

Fig. 3Effect of protein concentration onthe apparent viscosity of chickpea proteindispersions.

Fig. 2Shear stress () as a function of shearrate (sec1) on a log scale for chickpea pro-tein dispersions at several concentrations.

Fig. 4The consistency index (m) of chickpea protein dispersions has exponential correla-tion with protein concentrat ion (a), and is a function of protein concentration on a semilogscale (b).


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in the consistency coefficient with increas-

ing protein concentration has been reported

for oat protein (Ma, 1993). An index of vis-

cosity (m) is a semilogarithmic function of

concentration (ln mln A c, Fig. 4b).

The Casson Eq. (3) was fitted to the

rheological data from chickpea dispersions

(Fig. 5). From 16% a yield stress was appar-

ent, both yield stress and apparent viscosi-

ties markedly increased with increasing con-

centrations (Table 1). The consistency coef-

ficient (m) increased but the flow behavior

index (n) decreased progressively with in-

creasing concentration, reflecting a clear ten-

dency towards pseudoplastic behavior with

increasing concentrations.

A concentration dependence was found

for viscosity of chickpea protein. Similar re-

lationships were reported for soy protein

(Hermansson, 1975), faba bean protein

(Schmidt et al., 1986), oat protein (Ma,

1983), beta-lactoglobulin (Pradipasena and

Rha, 1977) and single cell protein concen-

trate (Huang and Rha, 1971). These resultssuggest a protein network was formed at high

concentrations due to protein-protein inter-

actions (Hermansson, 1975).

Effect of temperature

The effect of temperature were deter-

mined on power law constants and apparent

viscosity of 8% protein dispersions (Table 2).

Up to 35C, changes were minimal in either

power law constants or apparent viscosities.

At 55C, the flow behavior index exponen-

tially decreased, the consistency coefficient

increased greatly and a yield stress became

apparent. The flow behavior became morepseudoplastic.

Apparent viscosities of chickpea protein

dispersions markedly increased when the

temperature increased from 35 to 55 C

(Fig. 6) but the apparent viscosity at 55C

decreased at high shear rate (950 sec1), in-

dicating that the flow deviated from New-tonian behavior. Increasing viscosity of pro-

tein dispersions in blood plasma protein as-

sociated with increasing temperature had

been reported (Howell and Lawrie, 1987).

Similar results were found with whey pro-

tein (Voutsinas et al., 1983), faba bean (Sch-

wenke et al., 1990) and oat protein (Ma,

1983). The sensitivity of protein dispersion

to thermal increase depends on the type of

protein. Blood plasma protein is more ther-

mally sensitive than beta lactoglobulin (Plock

et al., 1992; Howell and Lawrie, 1987). The

viscosity of blood plasma protein increased

greatly at relatively low temperature (76C)but whey protein was only affected at higher

temperatures (80C). The increase in vis-

cosity of such protein dispersions indicated

a change in the shape of the proteins as a re-

sult of the protein unfolding due to thermal

treatment (Lee and Rha, 1979; Catsimpool-


as, 1970; Ma, 1983). In contrast to these ob-servations, Mita and Matsumoto (1980)

found that the apparent viscosities of 12%

gluten and gluten methyl ester dispersion

decreased from 20 to 50C. When thermal

effects were stronger than intermolecular in-

teractions, contributed by hydrogen bonding,

the apparent viscosity decreased. Conse-

quently, other investigations indicated that

the thermal effects on flow properties of pro-

tein, as with emulsifying properties (Voutsi-

nas et al., 1983) were not consistent. The

slight thermal effect on the apparent viscos-

ities of chickpea protein dispersions suggests

its characteristics are rather heat stable.

Effect of salts

The effects of salt concentration on the

power law constants, Casson yield stress and

apparent viscosity of 8% protein dispersion

were compared (Table 3). The flow curve was

nearly linear up to 0.2M NaCl, indicating a

Newtonian flow (not shown). The flow

curves progressively deviated from Newton-

ian, between 0.2M and 1M NaCl but a rever-

sal was observed at 2M NaCl. The flow be-

havior index (m) progressively decreased

with increasing salt concentration up to 1M

(n0.99-0.73), indicating a shear thinningeffect. In contrast no notable trend was not-

ed for the consistency coefficient, which ini-

tially dropped at 0.2M, but, then increased

up to 1M. The apparent viscosities reduced

with salt addition and varied with a change

of shear rate (81.4-950 sec1). This indicat-

ed a progressive deviation of flow curves

from Newtonian behavior. Reversal in trends

in the apparent viscosity and other power law

constants (n, m) occurred between 1 and 2M

NaCl. Ma (1983) reported a similar tenden-

cy with oat protein dispersions at 1M salt

concentration. Hermansson noted a similar

reversal in apparent viscosity of a soy pro-tein isolate between 0.5 and 1M NaCl. This

reversal in trends was attributed to a salt con-

Table 1 Effect of concentration on the power law constants and apparent viscosities ofchickpea protein dispersionsa

Conc (%) nb mc (mPa) Casson yield stress (mPa) Apparent Viscosity (mPa.s)81.4 sec 1 950 sec 1

2 1.00 (r2 = 0.998) 1.06 0.00 1.33 1.314 0.99 (r2 = 0.998) 1.85 0.02 1.68 1.858 0.99 (r2 = 1.000) 4.68 0.17 4.75 4.6512 0.94 (r2 = 1.000) 13.3 3.40 10.6 9.1316 0.89 (r2 = 0.999) 32.4 36.3 19.7 16.120 0.85 (r2 = 0.997) 82.4 80.2 40.4 31.6

aAverages of four determinations at pH 7 a nd 25C.bn flow behavior index.cm consistency coefficient.

Fig. 5Shear stress () as a function ofshear rate on a square root scale forchickpea protein dispersions at differentconcentrations.

Fig. 6Effect of temperatures on apparentviscosity of chickpea protein dispersions.

Table 2Effect of tem perature (C) on the power law constants and apparent viscosities of8% chickpea protein dispersionsa

Temp (C) nb mc (mPa) Casson yield stress (mPa) Apparent viscosity (mPa.s)81.4 sec1 950 sec 1

15 0.98 5.13 0.22 4.82 4.7025 0.99 4.68 0.17 4.75 4.6535 0.97 5.50 1.09 4.90 4.4355 0.68 44.7 25.4 11.2 5.02

aAverages of four determinations of 8% protein dispersions at pH 7.bn flow behavior index.cm consistency coefficient.


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232 JOURNAL OF FOOD SCIENCEVolume 63, No. 2, 1998


Table 3Effect of salt concentration (NaCl/M) on the power law constants and apparentviscosities of 8 % chickpea protein dispersionsa

NaCl conc (M) nb mc (mPa) Casson yield stress (mPa) Apparent viscosity (mPa.s)81.4 sec-1 950 sec-1

0.0 0.99 4.68 0.17 4.75 4.650.2 0.98 3.02 0.05 1.71 0.210.5 0.84 9.33 0.25 1.87 0.221.0 0.73 22.1 55.6 1.98 0.222.0 0.78 16.2 36.3 1.95 0.22

aAverages of four determinations of 8% protein dispersions at pH7 and 25C.bn flow behavior index.cm consistency coefficient.

Table 4Effect of pH on the power law constants and apparent viscosities of 8% chickpeaprotein dispersionsa

pH n(2) mc (mPa) Casson yield stress (mPa) Apparent viscosity (mPa.s)81.4 sec-1 950 sec-1

2 0.91 (r2 = 1.000) 12.9 10.9 8.70 7.145 0.84 (r2 = 0.995) 6.01 11.8 2.85 1.967 0.99 (r2 = 1.000) 4.68 0.17 4.75 4.659 0.85 (r2 = 0.999) 20.4 28.7 10.3 7.62

aAverages of four determinations of 8% protein dispersions at 25C.

bn flow behavior index.cm consistency coefficient.

Table 5 Effect of chemical modification (Urea/SDS) on the power law constants and ap-parent viscosities of 8 % chickpea protein dispersionsa

Sample nb mc (mPa) Casson yield stress (mPa) Apparent viscosity (mPa.s)81.4 sec-1 950 sec-1

Chickpea protein 0.99 4.70 0.17 4.75 4.656M urea treatedd 0.84 39.5 24.5 17.3 13.91% SDSe 0.54 326 525 36.5 14.1

aAverages of four determinations of 8% protein dispersions at pH7 and 25C.bn flow behavior index.cm consistency coefficient.d8% protein dispersion in 6M urea solutione8% protein dispersion in 1% SDS

centration critical for protein solubilization

(Megen, 1974).

Flow properties of protein dispersions

were markedly influenced by ionic strength.

Different salt concentrations (NaCl) in-

creased or decreased the apparent viscosities

of protein isolate dispersions. At low shear

rate (10 sec1) the apparent viscosities of

11.4% canola protein increased with salt con-

centration but at a high shear rate (1,000

sec1) the apparent viscosities were de-

creased (Paulson and Tung, 1988). Hermans-

son reported that apparent viscosity of soy

protein dispersions decreased with increas-

ing salt concentration but a reversal was ob-

served with caseinate. The different response

of soy protein and caseinate to an ionic envi-

ronment was influenced by a structural dif-

ference between the two proteins. Similarly,

the flow behavior index of oat globulin dis-

persions (15%) decreased progressively with

increasing salt concentration, showing an in-

creasing pseudoplastic tendency. In our re-

sults, the addition of salt produced an insig-nificant effect on the apparent viscosity of

chickpea protein dispersions. These results

suggest that chickpea protein had a rather rig-

id structure which barely altered in a salt

medium.

Effect of pH

The effects of pH on power law constants,

Casson yield stress and apparent viscosities

of 8% protein dispersions were compared

(Table 4). At pH 7, the flow was Newtonian

with n0.98, no yield stress and apparent vis-cosities unchanged at 81.4 and 950 sec1.

The flow progressively deviated from New-tonian behavior at both alkaline and acidic

pHs with a decrease in flow behavior index

and lower viscosities at high shear rate. The

viscosity-pH curve resembled the typical sol-

ubility curve of chickpea protein. Minimum

solubility occurred at the isoelectric pH (4-

5) with much higher solubility at acidic or

alkaline pH (2 or 9). Since apparent viscosi-

ties were concentration dependent, the vis-

cosity was high at the proteins most soluble

pHs (2 or 9) and was low at the isoelectric

pH at which most protein was present as ag-

gregates (Fig. 7). Like soy and canola pro-

tein (Ishino and Okamoto, 1975; Lee andRha; 1979; Paulson and Tung, 1988) the high

viscosity of chickpea protein at pH 9 is con-

sidered to be a combined effect of alkaline

induced protein unfolding, dissociation into

subunits and an increased protein solubility.

Effect of protein denaturing agents

The effects of SDS and urea on the pow-

er law constants and apparent viscosity of

chickpea protein dispersions were compared

(Table 5). SDS has been used to improve the

solubility of rapeseed, sunflower and soy

protein (Nakai et al., 1980; Arce et al., 1991).

The pronounced effect of 6-8 M urea on theunfolding of soy protein was noted (Shiba-

saki et al., 1969). In our results, urea treat-

ment caused a decrease in n value and in-

creases in m, yield stress and apparent vis-

cosity. The effect of 1% SDS treatment onthe flow characteristic of chickpea protein

was much more pronounced. A sharp de-

crease in n value and increases in m, yield

stress and apparent viscosity were observed.

The flow behavior was much more pseudo-

plastic. A similar result was reported for oat

globulin when treated with SDS and urea

(Paulson and Tung, 1993). The marked in-

creased in apparent viscosities of oat protein

Fig. 7Effect of pH on apparent viscosity(measured at 81.4 sec 1) and solubilitycurves of chickpea protein dispersions.

was attributed to the unfolding effect of the

denaturing agents (SDS and urea). Arce et

al. (1991) reported that the dispensability ofsoy protein concentrate could be improved

by up to 65% with SDS addition. Conse-

quently, the improved solubility of chickpea

protein caused by SDS and urea probably

contributed to the change of flow behavior

through changes in conformation of the pro-

teins.

CONCLUSIONFLOWPROPERTIESOFCHICKPEAPROTEINS

were considerably influenced by several en-

vironmental factors. Chickpea protein disper-

sions exhibited Newtonian behavior at low

protein concentration or low salt concentra-tion. Viscosity and pseudoplasticity increased

with an increasing protein and/or salt con-

centration. The change in flow behavior re-

sulted from the formation of a protein net-

work, dissociation, ionic and hydrophobic

interactions and particularly the changes in

solubility of chickpea protein under differ-

ent environmental conditions.

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Ms received 3/25/97; revised 10/26/97; accepted 10/30/97.

We thank Drs. B. Imison, M. Palmer (AFISC) and U. Singh

(ICRISAT, India) for discussions and Ms. D. Womersley (AFISC)

for technical assistance. The financial support of the Australian

Grains Research & Development Corporation (GRDC) and the

collaboration of Victoria University of Technology are acknowl-

edged.

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