Effects of Dehulling on Phytic Acid, Polyphenols, and
Enzyme Inhibitors of Dry Beans (Phaseolus vulgaris L.)
S. S. DESHPANDE, S. K. SATHE, D. K. SALUNKHE,
ABSTRACT
Effects of dehulling on phytic acid; trypsin, chymotrypsin, and
a-amylase inhibitory activities; and tannins of ten cultivars of dry
beans (PhaseolusvulgarisL.) were investigated. Phytic acid content
of whole beans ranged from 1.16-2.93%. Dehulling significantly
increased the phytic acid content of beans (range 1.63-3.67%).
Dehulling also increased trypsin, chymotrypsin, and ol-amylase in-
hibitory activities of the beans. Tannin contents of whole and
dehulled beans ranged from 33.7-282.8 and 10.0-28.7 me. catechin
equivalent~/lOOg beans, respectively. Removal of seed coats lowered
the tannin content of beans by 68-95%. Tannins were not detected
in white seeded cultivars of Sanilac, Great Northern, and Small
White. Dehulling significantly improved the in vitro digestibility of
bean proteins.
INTRODUCTION
PLANTS are the most important source of food and food
proteins for human beings. Of the total world food harvest,
plant products contribute approximately 8 1.8% of the gross
tonnage, whereas animal and marine products together
contribute only 16.8% (FAO, 1973). The average production
from plant sources of protein potentially edible by humans
was estimated to be 196.8 million tons, compared to 49.1
million tons of animal protein (Lischenko, 1979). Among
plant sources, dry legumes and legume products are the
richest source of food proteins (Pino and Martinez, 1981).
Their utilization as human foods is, however, below their
potential. Underutilization of legumes has been attributed
to factors such as the prolonged cooking times required to
prepare legume-based foods, methionine deficiency in
legume proteins, presence of several heat-stable and heat-
labile factors that interfere with digestion, and gastro-
intestinal distress and flatulence associated with legume
foods (Rockland and Nishi, 1979).
Phytic acid (myoinositol hexaphosphate) is the principal
source of phosphorus in dry beans (Lolas and Markakis,
1975). The interaction of phytate with proteins, vitamins,
and several minerals is considered to be one of the factors
that limit the nutritive value of dry beans (Chang et al.,
1977). Numerous studies suggest that phytate reduces the
biological availability of dietary copper and manganese
(Davies and Nightingale, 1975), iron (Welch et al., 1974;
Welch and van Campen, 1975), magnesium (Guenter and
Sell, 1974), and zinc (O’Dell and Savage, 1960; Oberleas,
1973). Phytate is also suggested to interfere with protein
metabolism and decreases the utilization of proteins sub-
jected to proteolytic digestion (O’Dell and Boland, 1976).
The nutritional effects of polyphenols in food legumes
are also primarily detrimental. Polyphenols (as condensed
tannins) are predominantly located in the pericarp and/or
Author Cornforth is affiliated with the Dept. of Nutrition & Food
Sciences, Utah State Univ., Logan, UT 84322. Author Deshpande,
formerly with Utah State Univ., is now affiliated with the Dept. of
Food Science, Univ. of Illinois, Urbana, IL 61801. Author Sathe,
formerly with Utah State Univ., is now with the Dept of Food
Science, Univ. of Arizona, Tucson, AZ 85721. Author Salunkhe,
formerly with Utah State Univ., is now ViceChancellor, Mahatma
Phule Agricultural Univ., Rahuri 4 13 722, Maharash tra State, India.
Address requests for reprints to Dr. Deshpande.
1846-JOURNAL OF FOOD SCIENCE-Volume 47 (1982)
and D. P. CORNFORTH
testa, particularly of pigmented cultivars of legumes and
millets. Bressani and Elias (1980) observed a higher protein
quality for white as compared to pigmented cultivars of
Phaseolus vulgaris. These authors also found tannins to be
heat stable and that they decreased protein digestibility
in animals and humans, probably by either making protein
partially unavailable or inhibiting digestive enzymes and
increasing fecal nitrogen.
Proteinaceous inhibitors of the important digestive
enzymes (trypsin, chymotrypsin, and a-amylase) occur
at relatively high amounts in several legumes (Jaffe et al.,
1973; Marshall, 1975; Liener, 1979a; Padhye and Salunkhe,
1980; Sathe and Salunkhe, 1981). The increase in nutri-
tional value of beans subjected to heat treatment has
been generally attributed to the destruction of protease
inhibitors and lectins (Liener, 1979a). The importance,
mode of action, nutritional significance, nutritional toxicity,
effects of processing, and related aspects of trypsin, chymo-
trypsin, and ar-amylase inhibitors of legumes have been
discussed in several reviews (Stein, 1976; Liener, 1975,
1979a, b; Marshall, 1975).
The seed coats of legumes are sometimes removed prior
to their processing and consumption. Kon et al. (1973)
studied the effects of seed coat removal on cooking times
of dry beans. They observed a reduction of 42, 53, and 70%
in cooking times of peeled, unsoaked California Small
White, Sanilac, and Pinto beans, compared to the corre-
sponding controls. These authors, however, did not report
data on antinutrients of dehulled beans. The present inves-
tigation was therefore undertaken to determine how much
quantitatively such seed coat removal affects certain anti-
nutritional factors (phytic acid; trypsin, chymotrypsin, and
a-amylase inhibitory activities; and tannins) of ten cultivars
of dry beans (Phaseolus vulgaris L.) commonly grown in
the United States. The effects of seed coat removal on in
vitro protein digestibility were also investigated.
MATERIALS & METHODS
MATURE DRY BEANS (PhaseolusvulgarisL.) of Sanilac, Great
Northern, and Small White (white seeded); Cranberry, Viva Pink,
Pinto, and Light Red Kidney (medium colored); and Dark Red
Kidney, Small Red, and Black Beauty (dark colored), grown and
harvested in 1980, were purchased from Roger Brothers Seed Co.,
Twin Falls, Idaho. Unless mentioned otherwise, all chemicals used
were of reagent grade.
Preparation of whole bean flour
Whole dry beans were ground to a 60 mesh flour in a UDY
Cyclone Mill (Tecator, Inc., Boulder, CO).
Preparation of dehulled bean flour
Beans were soaked in distilled water (1:s w/v, bean to water
ratio) for 12 hr at room temperature (21°C). Seed coats and germs
were then removed manually. The dehulled beans were freeze-
dehydrated along with the soaking water and ground in a UDY
Cyclone Mill to obtain a 60 mesh flour.’
Phytic acid content
Phytic acid content of whole and dehulJed beans were deter-
mined by a combination of three methods. Extraction and precipi-
tation of phytate were performed according to the method of
 Wheeler and Ferrel(l971). A 2-g sample of flour was extracted with
50 ml of 3% (w/v) trichloroacetic acid (TCA) solution for 2 hr at
21°C with mechanical shaking. The slurry obtained was centrifuged
at 5,000 X g for 15 min. Ten ml of supernatant were used for each
assay. Phytate in the supernatant was precipitated as ferric phytate.
The conversion of ferric phytate to ferric hydroxide was carried out
by Makower’s (1970) procedure. The precipitate (ferric hydroxide)
was dissolved in 0.5 ml of 0.5 N HCl in a boiling water bath for 15
mm. The solutions were then transferred quantitatively and made
to volume (50 ml) with O.lN HCl. The ferric iron (Fe*) content
was determined by the AOAC (1975) method using o-phenanthro-
line reagent. The contents of iron and phosphorus were assumedto
be in a 4:6 ratio in order to calculate phytate phosphorus content.
Phytic acid content was calculated on the assumption that it con-
tams 28.20% phosphorus, by weight.
Tannin content
Tannin content of whole and dehulled beans were determined
according to the modified vanillin-hydrochloric acid method of
Price et al. (1978) using appropriate sample blanks. All sampleswere
extracted within 6 hr of milling into flour. Catechin (+) (Sigma
Chemical Co., St. Louis, MO) was used as a reference standard
and the tannin content expressed in terms of catechin equivalents.
Trypsin and chymotrypsin inhibitors
The following were the sources of chemicals for the assays:
Trypsin enzyme and substrate, p-tosyl-L-arginine methyl ester
(TAME) were obtained from Sigma ChemicalCo., St. Louis, MO;
a-chymotrynsin from P.L Biochemicals. Milwaukee. WI:and benzovl-
L-triosine-ethyl ester (BTEE) from Aldrich Chemical’Co., Milwau-
kee, WI.
A l-g flour sample-was blended with 15 ml of 0.05N HCl for 2
min in a Sorvall Omni mixer (Ivan Sorvall, Inc., Newtown, CT) and
extracted for 12 hr at 4°C. The slurry was then centrifuged at 5,000
X g for 15 min. Three ml of 30% TCA were added to the supernatant
and recentrifuged. The supernatant was then neutralized with sodium
hydroxide to pH 8.0 and made up to 25 ml. The enzyme inhibitory
activities were determined as described by Decker (1977). The
details of the procedures were described earlier (Sathe and Salunkhe,
1981).
o-Amylase assay
The enzyme or-amylase(Type I-A, from porcine pancreas) was
from Sigma Chemical Co., St. Louis, MO and soluble potato starch
. was from J.T. Baker Chemical Co., Phillipsburgh, NJ. All reagents
were preincubated for 15 min at 37’C in a water bath. To 0.5 ml of
1% starch solution in 0.2M sodium phosphate buffer (pH 7.0) and
0.25 ml of the buffer was added 0.25 ml of oramylase enzyme solu-
tion (30 pg/ml in 0.2M sodium phosphate buffer, pH 7.01 and con-
taining 0.006M NaCl). At the end of 3 mm. the reaction was stopped
by the addition of 2 ml of dinitrosalicyhc acid.reagent (Sumner,
1924) and heating in a boiling water bath for 10 min. The test tubes
were then cooled under running cold tap water and made to a final
volume of 13 ml using distilled water. The absorbancewas recorded
at 540 nm in a Beckman DB-G Spectrophotometer. The liberated
reducing sugars were expressed as maltose. One unit of enzyme
activity was defined as that which liberates from soluble starch one
micromole of reducing groups (calculated as maltose) per min at
37°C and pH 7.0 under the specified conditions.
cu-AmylaseInhibitor Assay
or-Amylase inhibitor acitivty was evaluated as follows. A l-g
sample was extracted with 10 ml of distilled water for 12 hr at 4°C.
centrifuged at 5,000 X g for 20 min, and the supernatants were
tested for ol-amylaseinhibitory activity. A 0.25 ml of sample solu-
tion containing the inhibitor was incubated with 0.25 ml of enzyme
solution for 15 min at 37°C. To this mixture was added 0.5 ml of
1% starch solution (preincubated at 37°C). The assaywas conducted
as described above. One unit of o-amylase activity inhibited was
defined as one ol-amylaseinhibitory unit.
In digestibility
vitro
protein digestibiltiy of whole and dehulled beans was
In vitro
determined by the multienzyme technique of Hsu et al. (1977).
The details of the procedure were described by Sathe et al. (1982).
The enzymes peptidase and trypsin were from Sigma Chemical Co.,
St. Louis, MO, and orchymotrypsin was from P.L. Biochemicals,
Milwaukee, WI.
Statistical analyses
Data were analyzed by the analysis of variance procedures of the
Statistical Analysis System (SAS, 1979). Least significant differences
were used for multiple mean comparison tests.
RESULTS
DATA on phytic acid contents of whole and dehulled beans
are summarized in Table 1. Phytic acid contents of whole
beans ranged from 11.6-29.3 mg/g beans. Comparing
cultivars, Small White beans had 40-57s less phytic acid
than the others. Black Beauty, Dark Red Kidney, and Sani-
lac beans contained significantly (p = 0.05) more phytic
acid than did any of the other cultivars investigated. Except
for Pinto beans, dehulling significantly (p = 0.05) increased
the percentage of phytic acid, compared to the content in
whole beans. The overall mean percent increase in phytic
acid content after dehulling was approximately 31%.
Tannin contents of the whole and dehulled pigmented
beans varied widely, ranging from 33.7-282.8 mg catechin
equivalents/lOOg whole beans and from 10.0-28.7 mg
catechin equivalents/lOOg dehulled beans, respectively
(Table 2). Tannins were not detected in the white seeded
cultivars (Sanilac, Great Northern, and Small White).
Among the colored seeds, Pinto and Small Red beans con-
tained more tannins than did the Kidney beans. Black

Table Z-Tannin content of whole and dehulled beansa

Table 1 -Phvtic acid content of whole and dehulled beansa
Tannin content
Phytic acid (mg/g) (mg catechin equivalents/tOOg) % Reduction
% Increase
Cultivar Whole beans Dehulled beans on dehulling Cultivar Whole beans Dehulled beans on dehulling

Sanilac 27.5 29.4 6.9 Sanilac NDb ND

Great Northern 26.4 32.6 59.8 Great Northern ND ND
Small White 11.6 16.3 40.5 Small White ND ND
Cranberry 26.3 33.9 28.9 Cranberry 76.3 10.0 86.9
Viva Pink 21.6 29.1 34.7 Viva Pink 122.1 10.4 91.5
Pinto 23.8 25.6 7.6 Pinto 264.7 14.2 94.6
Light Red Kidney 26.3 34.7 31.9 Light Red Kidney 152.2 22.2 85.4
Dark Red kidney 28.6 36.7 28.3 Dark Red Kidney 105.3 28.7 72.7
Small Red 20.7 30.5 47.3 Small Red 282.8 19.0 93.3
Black Beauty 29.3 36.1 23.2 Black Beautv 33.7 10.8 68.0

LSDb p = 0.05 1.93 30.9= LSDC p = 0.05 25.42

p = 0.01 2.53 p = 0.01 34.29
a Mean of triplicate determinations on a dry weight basis. a Mean of triplicate determinations on a dry weight basis.
’ Least significant difference. Differences of two means within/ b ND = Not detected.
between the cultivars exceeding this value are significant. ’ Least significant difference. Differences of two means within/
’ Mean percent increase on dehulling. between the cultivars exceeding this value are significant.

Volume 47 (1982)-JOURNAL OF FOOD SCIENCE-1847

 DRY BEAN ANTINUTRIENTS. ..
Table S-Enzyme inhibitory activities of whole and dehulled beansa*b

Trypsin inhibitory Chymotrypsin inhibitory o-Amylase inhibitory

activity, units/g X 10m3 activity, units/g X 10e3 activity, units/g
Whole Dehulled % Increase Whole Dehulled % Increase Whole Dehulled % Increase
Cultivar beans beans on dehulling beans beans on dehulling beans beans on dehulling
Sanilac 186 253 36.0 332 368 10.8 675 860 27.4
Great Northern 248 285 14.9 308 361 17.2 350 1011 188.9
Small White 235 262 11.5 345 369 7.0 450 671 49.1
Cranberry 233 282 21 .o 323 356 10.2 560 950 69.6
Viva Pink 257 261 1.6 217 271 24.9 531 881 65.9
Pinto 360 433 20.3 323 370 14.6 420 888 111.4
Light Red Kidney 216 257 19.0 318 364 14.5 577 990 71.6
Dark Red Kidney 240 263 9.6 335 344 2.7 633 848 34.1
Small Red 222 245 10.4 288 360 25.0 573 882 53.9
Black Beauty 270 289 7.0 331 371 12.1 330 844 155.8
LSD’ p = 0.05 14.3 15.14 17.4 13.94 66.9 82.8’
p = 0.01 18.8 22.8 87.9
z Mean of triplicate determinations on a dry weight basis.
One unit of inhibitor activity is that which reduces the activity of the corresponding enzyme by one unit under the assay conditions.
z Least significant difference. Differences of two means within/between the cultivars exceeding this value are significant.
Mean percent increase on dehulling.

Table 4-in vitro digestibility of whole and dehulled beansa may be attributed to at least two factors. First, these anti-
nutritional factors may be characteristically present in the
% In vitro digestibility cotyledon fractions of the beans. Second, the seed coat
% Increase
Cultivar Whole beans Dehulled beans on dehulling contributes a substantial portion of the whole seed weight.
Removing the seed coat may lead to an increase in the con-
Sanilac 70.0 72.8 4.0
Great Northern 69.0 71.3 3.3
centrations of these antinutrients on a unit weight basis.
Small White 68.7 70.3 2.3 Hull contents of the dry bean cultivars investigated were in
Cranberry 69.5 72.2 3.9 the range of 6.9-9.8% of the dry weight of the seed (Desh-
Viva Pink 70.9 73.1 3.1 pande et al., 1982). Removal of the seed coats, however,
b
Pinto 69.6 72.3 3.9 did not cause an increase in the relative contents of these
Light Red Kidney 66.9 69.4 3.7 antinutrients by an average factor of 10. The mean percent
Dark Red Kidney 68.6 71.1 3.6 increases after dehulling were as follows: phytic acid 30.9%,
Small Red 69.0 72.0 4.3 trypsin inhibitor 15.1%, chymotrypsin inhibitor 13.9%,
Black Beauty 69.4 71.5 3.0
and cr-amylase inhibitor 82.8%. The more than the average
LSDb p = 0.05 0.37 53 increase in phytic acid content suggests that dehulling may
p = 0.01 0.50 improve the extraction efficiency of phytic acid from the
a Mean of duplicate determinations on isonitrogenous basis. beans. Phytic acid reportedly forms complexes with the
b Least significant difference. Differences of two means within/ seed coat fractions (Cummings, 1976). The formation of
between the cultivars exceeding this value are significant. such complexes during extraction may lead to a lower
’ Mean percent increase on dehulling.
estimation of phytic acid in whole beans since these com-
plexes will be retained in the residue fraction after centri-
Beauty beans had the lowest tannin content of the colored fugation.
beans (Table 2). Dehulling removed most of the tannins Phytic acid is also a strong inhibitor of a-amylases derived
from the colored beans. Thus, the dehulled beans of all the from a variety of sources (Sharma et al., 1978; Cawley and
pigmented cultivars investigated did not differ significantly Mitchell, 1968). In the absence of seed coat fractions in
(p = 0.05) in their tannin contents. Total elimination of dehulled beans, more phytic acid is free to suppress (II-
tannins after dehulling, however, was not observed. amylase activity. The significant increase in cu-amylase
Data on trypsin, chymotrypsin, and a-amylase inhibitory inhibitor activity after dehulling of beans may be due to a
activities of the whole and dehulled beans are presented in combined inhibitory activity exerted by the natural inhibi-
Table 3. Removal of the seed coat significantly (p = 0.05) tor and phytic acid.
Phytic acid contents (1.16-2.93%) of the dry bean
increased the activities of all three enzyme inhibitors in the
cultivars investigated were within and/or higher than the
dry bean cultivars investigated. The exceptions were found
range of reported values for several legumes (Reddy et al.,
in Viva Pink (trypsin inhibitor) and Dark Red Kidney
1978; .Lolas et al., 1976; Lolas and Markakis, 1975; Iyer
(chymotrypsin inhibitor).
et al., 1980; Dieckert et al., 1962). In many cases, phytic
Dehulled beans were significantly higher in in vitro
acid content is not considered to be absolute and may vary
protein digestibility, compared to whole beans (Table 4).
depending upon the variety and/or cultivar, climatic condi-
The in vitro protein digestibility on an isonitrogenous basis
tions, location, irrigation conditions, type of soil, and year
ranged from 66.9-70.9% and from 69.4-73.1% for the
during which they are grown (Bassiri and Nahapetian, 1977;
whole and dehulled beans, respectively. Viva Pink bean
Singh and Sedeh, 1979; Miller et al., 1980a, b). The high
proteins were significantly more digestible than those of the
other cultivars investigated, whereas Light Red Kidney phytic acid content of certain cultivars in the present study
(Black Beauty, Sanilac, Cranberry, and Kidney beans) may
bean proteins were the least digestible (Table 4).
largely be due to these factors.
Increased phytic acid content of black gram cotyledons
DISCUSSION
(1.70%) compared to whole black gram seeds ( 1.46%) has
THE INCREASE in relative contents of phytic acid and been previously reported (Reddy and Salunkhe, 1980).
the activities of trypsin, chymotrypsin, and a-amylase Literature data also suggest that milling lowers the phytic
inhibitors after dehulling of all ten cultivars investigated acid content of rice (de Boland et al., 1975; Reddy and

1848-JOURNAL OF FOOD SCIENCE-Volume 47 (1982)

Salunkhe, 1980). The latter may be attributed to phytic generally destroys these heat-labile antinutritional factors
acid accumulating in aleurone particles or as grains in the (Liener, 1979a).
aleurone layer and globoids (Lott and Buttrose, 1978; Dehulling slightly but significantly improved the in vitro
Sobolev, 1966), which are removed during the polishing of protein digestibility (on an isonitrogenous basis) of the dry
rice. The same sites have been indicated for phytic acid in bean cultivars investigated. This may be attributed to the
legumes (Sobolev, 1966). The increase in phytic acid con- removal of seed coat fractions and the polyphenols therein.
tent of the dehulled beans observed in the present investi- Dietary fiber constituents have been known to affect pro-
gation may be attributed to the dehulling process employed. tein digestibility in humans (Kelsay et al., 1978; Walker,
Since the seed coats were removed manually in the present 1975; Southgate and Durin, 1970). Recently, Acton et al.
study, few changes were expected in the composition of the (1982) reported that the dietary fiber constituents from
aleurone layers of the beans. Consequently, loss of phytic several sources significantly reduced the in vitro digestibility
acid through the removal of hulls would be minimal. If of casein. These authors proposed that the dietary fiber
dry beans were to be mechanically milled, substantial constituents may reduce protein digestibility and increase
changes may be expected in phytic acid content through nitrogen excretion through ionic interaction and matrix
the removal of aleurone layers. Losses as great as 15-25% formation.
of the dry seed weight have been reported during the me- The in vitro digestibility of bean proteins observed in the
chanical milling of dry beans (NAS, 1978). present study was much less than that reported for casein
Two of the three white seeded cultivars included in the (90.1%) (Acton et al., 1982). The low in vitro digestibility
present study (Small White and Great Northern) had signifi- of bean proteins may be due to their structural characteris-
cantly lower phytic acid contents than did the others. In tics. Major storage proteins of dry beans are known to be
general, the colored beans contained more phytic acid. The resistant to proteolysis (Liener and Thompson, 1980;
wide variation in phytic acid contents observed among the Chang and Satterlee, 198 1) and are implicated as one of the
cultivars Investigated suggest that genetic selection for causes for the poor nutritive value of unheated Phaseolus
beans with low phytic acid content should be effective. vulgaris. Numerous studies have indicated that the globulin
Selective removal of heat-stable antinutritional factors fraction of these legumes, which represents the major storage
(such as phytic acid) may aid in increasing the utilization of protein and comprises 50-75% of the total protein of the
legumes. dry seed (Romero et al., 1975) is quite resistant to attack
Tannin contents of the dry bean cultivars investigated by proteolytic enzymes in vitro (Romero and Ryan, 1978;
were within the range reported for several legumes (Ma and Seidl et al., 1969; Vaintraub et al., 1976; Liener and
Bliss, 1978; Price et al., 1980; Davis, 1981). Tannins in Thompson, 1980; Chang and Satterlee, 1981). Our results
beans are located in the seed coat (Ma and Bliss, 1978) and also indicate the inherent resistance of bean proteins to
thus its removal may be expected to reduce the tannin proteolytic digestion.
content of beans. Similarly significant reduction in tannin
content on removal of seed coats of sorghum (Jambunathan REFERENCES
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be a practical problem. Cooking or heat treatment of beans Quick-cooking beans (Phaseolus vulgaris L.): 2. Phytates, oligo-

Volume 47 (1982)-JOURNAL OF FOOD SCIENCE-1849

DRY BEAN ANTINUTRIENTS. ..
saccharides, and antienzymes. Qual. Plant. Pl. Fds. Hum. Nutr. Price, M.L., Hagerman, A.E., and Butler, L.G. 1980. Tannin content
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1850-JOURNAL OF FOOD SCIENCE-Volume 47 (7982)