Gatel 1994

Animal Feed Science and Technology, 45 (1994) 317-348 317
0377-8401/94/$07.00 © 1994 - Elsevier Science B.V. All rights reserved
Protein quality of legume seeds for non-ruminant

animals: a literature review
F. Gatel
Institut Technique des C~r~ales et des Fourrages, Pouline--41 I00 Villerable, France
(Received 24 June 1992; accepted 23 July 1993 )
Abstract
Peas and field beans have been increasingly grown in Europe during the last 15 years, to improve
self-sufficiency in protein-rich feedstuffs. The protein profile of these crops is characterized by a high
lysine content (7.3% crude protein in peas) and a relative deficiency in sulphur amino acids and
tryptophan. Protein digestibility is slightly lower than in soyabean meal, especially for pigs (0.74 in
peas vs. 0.80 in soyabean meal) and for young animals, and appears variable both between and within
species. This lower digestibility can partly be explained by the presence in some species or cultivars
of antinutritionalfactors (ANF; e.g. protease inhibitors, lectins or tannins) and/or fibrous material,
leading to low accessibility of legume seed protein to digestive enzymes. More work is needed to
separate the effects of these factors and their practical importance. Because of the high variability of
ANF activity, it also appears necessary to develop reliable and quick assays which allow a check and
selection of batches by plant breeders or feed manufacturers. Owing to the high variability within
each species of these characteristics it seems possible to improve the nutritionalvalue of legume seeds
by selective breeding. In the short term, technological treatments can also lead to improved utiliza-
tion, especially in poultry, but attention has to be paid to the cost of these treatments.
Introduction
Europe has long been far from self-sufficiency in protein-rich feedstuffs for
livestock and consequently has relied heavily on soyabean meal imports. The
European Economic Community (EEC) decided in 1978 to promote the pro-
duction and use of grain legumes through guaranteed prices for producers and
financial subsidies for users. As a result of this policy, legume seeds have been
increasingly grown during the 1980s. In 1990, the EEC production reached
4 500 000 t for peas and 855 000 t for field beans.
Although still far from self-sufficiency, the EEC produced in 1991 about
39% of its protein consumption (6 250 000 t protein equivalent out of
15 800 000 t). Grain legumes contributed 18% to the EEC protein produc-
tion (i.e. 1 122 000 t protein equivalent) (UNIP, 1993). Grain legumes are,
however, not evenly consumed by all animal species, most of them being used
S S D I 0 3 7 7 - 8 4 0 1 (93)00528-4
318 F. Gatel /Animal Feed Science and Technology 45 (1994) 317-348
by non-ruminants, i.e. pigs and poultry. Hence, although accurate data are
missing, it is obvious that the contribution of grain legumes to protein con-
sumption by these species is higher than the average 7.10% value and that the
quality of this protein must be considered.
The quality of a protein source for non-ruminant feeding depends on three
major factors: the composition, mainly the essential amino acid content, the
occurrence and content ofproteic antinutritional factors (ANF) such as tryp-
sin inhibitors and lectins, and the amino acid availability. The amino acids of
a protein are made available by hydrolysis of the peptide bonds by proteolytic
enzymes. The presence of ANF or inaccessible peptide bonds will affect the
amino acids' availability. Many treatments that inactivate ANF and modify
the structure of the cells and its constituents have been reported to improve
protein availability. Protein quality can also be considered in terms of animal
health, in relation to the immune response to the dietary protein. In view of
the relative contribution of the various plant species to either production or
utilization, this review is limited mainly to peas and field beans and, to a
lesser extent, lupins.
Protein composition
The average crude protein content (Table 1 ) is about 255 g kg- 1dry matter
(DM), 300 g kg- 1 DM and 410 g kg-1 DM for smooth peas, field beans and
sweet white lupin, respectively (INRA, 1989), with important variations be-
tween and within genotypes (Matthews and Arthur, 1985; M6tayer et al.,
1992). The main protein fractions are globulins (legumin and vicilin) and
albumin (respectively 60% and 20% of total protein for peas; Gu6guen and
Baniel, 1990).
Table 1
Average protein and amino acid contents of grain legumes (g kg- t D M ) (INRA, 1989 )
Smooth peas Field beans Sweet white lupin

( Pisum sativum L. ) ( Vicia faba L. ) ( Lupinus albus L. )
Crude protein 255.8 303.4 410.3

Lysine 18.6 19.1 19.3
Methionine + cystine 6.9 6.1 9.2
Tryptophan 2.3 2.5 3.2
Threonine 10.1 10.7 14.8
Leucine 17.8 22.4 28.7
Isoleucine 11.3 13.6 18
Valine 11.7 14.4 17.2
Histidine 6.0 7.6 9.4
Arginine 24.7 28.5 43.1
Phenylalanine + tyrosine 20.1 23.2 34.5
F. Gatel / Animal Feed Science and Technology 45 (1994) 317-348 319
Amino acid content
Essential amino acid contents of smooth peas, field beans and lupins are
presented in Table 1. Compared with soyabean meal protein, legume seed
protein is rich in lysine, except for lupin. It contains a similar proportion of
threonine, but less sulphur amino acids and tryptophan. This is explained by
the amino acid composition of the main storage protein globulins, whose sul-
phur amino acid content is much lower than in soyabean meal, especially for
the vicilin fraction, whereas lysine content is higher (Gu6guen and Baniel,
1990). The amino acid content expressed relative to lysine content, when
compared with the ideal profile defined by Wang and Fuller (1989) for pigs,
reveals the deficiency of legume seeds in sulphur amino acids and tryptophan
(Sosulki and Holt, 1980; Lattanzio et al., 1983 ). On the other hand, the high
lysine content is of value, particularly as a means to reduce nitrogen content
of diets and thus nitrogen excretion (Gatel et al., 1993).
Considering the protein amino acid profile, cereals and grain legumes ap-
pear nutritionally complementary; those amino acids deficient in one (lysine
in cereals and sulphur amino acids in legumes) being adequate in the other
(Marquardt and Bell, 1988 ).The relative tryptophan deficiency in legumes is
a problem because natural sources are rather scarce and synthetic tryptophan
is still expensive compared with methionine. The relative amino acid imbal-
ance has been shown in experiments carded out on piglets and pigs, where
the introduction of peas in partial or total substitution for soyabean meal on
the basis of a constant lysine content led to poorer performance, whereas the
addition of sulphur amino acids and/or tryptophan to the experimental diets
restored performance to the levels of the control groups (Palisse Roussel et
al., 1984; Madsen and Mortensen, 1985; Gatel et al., 1989; Qu6m6r6, 1990).
Similarly, Marquardt and Campbell (1974) and Reddy et al. (1979) ob-
tained growth responses to supplemental methionine added to diets contain-
ing 87% field beans or 66% peas, fed to chickens.
Taking into account the large variation of the albumin to globulin ratio and
the vicilin to legumin ratio (Gu6guen and Barbot, 1988 ) and the difference
in amino acid profiles of these various protein fractions, it is questionable
whether this variability can be used as a means to improve genetically the
amino acid profile of grain legumes. Schroeder (1982) found in peas a nega-
tive correlation between the proportion of the albumin and the legumin frac-
tions, both of which are rich in sulphur amino acids. Similarly, attempts to
improve in this way the amino acid profile of field beans have failed (Duc
and Lacassagne, 1990). Genetic improvement of the legume protein profile
would have to rely mainly on gene manipulations to improve the content of
methionine and tryptophan (De Lumen, 1990; Gu6guen and Baniel, 1990).
Reference has been made to the high variability of legume protein content.
On a dry matter basis, and for each of the three species, i.e. peas, field beans
320 F. Gatel / Animal Feed Science and Technology 45 (1994) 317-348
Table 2
Slope a, intercept b and correlation coefficient r of regression lines representing amino acid content
(g kg-1 DM) against crude protein (NX 6.25) content (g kg-~ DM) for legume grains (Moss6, 1990)
Smooth peas Field beans Sweet white lupin
a b r a b r a b r
Lysine 0.0598 3.58 0.992 0.0494 4.65 0.880 0.0363 4.72 0.983
Methionine 0.0075 0.65 0.935 0.0053 0.55 0.693 0.0011 2.56 0.354
Cystine 0.0059 2.20 0.753 0.0133 -0.18 0.647 0.0066 3.78 0.603
Tryptophan 0.0077 0.10 0.913 0.0074 0.27 0.946 0.0037 1.24 0.900
Threonine 0.0264 2.97 0.978 0.0328 0.87 - 0.0227 5.53 0.942
Leucine 0.0672 1.08 0.990 0.0726 1.00 0 .9 2 1 0.0622 3.93 0.994
Isoleucine 0.0374 1.77 0.966 0.0395 0.31 0.889 0.0445 0.69 0.993
Valine 0.0424 1.81 0.977 0.0467 -0.43 0.879 0.0326 3.98 0.984
Histidine 0.0243 0 0.986 0.0242 0.34 0.952 0.0158 2.29 0.980
Arginine 0.1555 -14.97 0.972 0.1467 -15.38 0.937 0.1712 -24.19 0.994
Phenylalanine 0.0370 2.85 0.975 0.0395 0.73 0.914 0.0350 1.48 0.992
Tyrosine 0.0226 2.89 0.939 0.0320 -0.07 0.898 0.0510 -1.68 0.986
and lupin, the content of each amino acid is linearly correlated with the pro-
tein content (Moss6, 1990) (Table 2). Despite the assertion of Holt and So-
sulki ( 1979 ), the relationships appear independent ofgenotype, environment
or agricultural practice (Moss6 et al., 1987 ). A further interpretation of the
data of Holt and Sosulki (1979) by Moss6 et al. ( 1987 ) confirmed this con-
tention. Huet et al. (1987 ) explained the linearity of the relationship by the
fact that the extra proteins deposited when passing from a low- to a high-
protein seed consist of a mixture of the main storage protein fractions with
ratios practically remaining constant. As a consequence of such a linear rela-
tionship between grain amino acid content and protein content, amino acids
are not a fixed proportion of total protein but vary as a hyperbolic function
of protein. Proportions decrease when the protein content increases for a
number of essential amino acids, particularly lysine, sulphur amino acids,
tryptophan and threonine (Moss6, 1990). This is in agreement with the neg-
ative correlation found between protein sulphur amino acid and protein con-
tent by Evans and Boulter (1980) in peas and beans. Similarly, Reichert and
McKenzie (1982) observed with peas that varied widely in protein content
( 145-285 g kg-~ on a dry dehulled basis) a negative correlation between lys-
ine, methionine, cystine or threonine, expressed as a proportion of nitrogen
content, and pea protein content. Thus, it appears that any increase in legume
crude protein content leads to a decrease of protein quality in terms of amino
acid profile.
Proteic antinutritional factors
Grain legumes contain a number of naturally occurring antinutritional fac-
tors (ANF). The physiological effects and practical importance of legume
F. Gatel /Animal Feed Science and Technology 45 (1994) 317-348 321
ANF on protein availability will be discussed below. However, as some of

these ANF are proteins, they can be considered here. Two of the major ANF
found in legume seeds are protease inhibitors and lectins.
Protease inhibitors
Protease inhibitors are proteins with specific antitrypsin and antichymo-
trypsin activities. They are present in peas and field beans. In peas, they are
located mainly in the cotyledons, whose trypsin inhibiting activity (TIA) is
about 13 times higher than in the hulls. In field beans, the presence of inter-
fering substances in the hulls prevents an accurate study of TIA distribution
in the grains (Valdebouze et al., 1980). TIA of various cultivars of peas or
field beans are given in Tables 3 and 4. It appears that TIA of raw legume
grains is 5-20 times lower than in raw soyabean. However, to compare peas
and field beans the varieties have to be specified, as there is more variation
within than between species.
For white peas, TIA of winter varieties (6-16 trypsin inhibited units (TIU)
mg-~ DM) is generally 2-4 times higher than TIA of spring varieties (1.7-
5.5 TIU mg -1 DM) (Valdebouze and Gaborit, 1985; Leterme et al., 1990a).
According to Valdebouze et al. (1980), smooth peas contain more TIA than
wrinkled ones. However, spring marrowfat cultivars seem to have a higher
TIA than spring white pea cultivars (Griffiths, 1984; Bond and Smith, 1989;
Leterme et al., 1990a). Coloured-flowered peas generally have low TIA (Pi-
sulewski et al., 1983; Grosjean et al., 1991 ). For field beans, TIA is less vari-
able, and is similar to that of spring peas, with little systematic difference
between winter and spring cultivars (Valdebouze et al., 1980; Valdebouze and
Gaborit, 1985). Although part of the variability observed in the literature can
be associated with the analytical method itself, particularly the selectivity of
the inhibitor extraction and determination (Valdebouze et al., 1980), there
is evidence that TIA can vary within a variety according to growing condi-
tions such as climate, soil and sowing date (Valdebouze and Gaborit, 1985;
Bond and Smith, 1989; Leterme et al., 1990a; Grosjean et al., 1993). Causes
of this variability remain unknown. TIA variation in peas or field beans seems
to be independent of crude protein content (Griffiths, 1979, 1984). Consid-
ering the variability of TIA, especially for peas, and despite the existence of
accurate and reliable laboratory methods of analysis, it would be beneficial
for the feed industry to have a rapid assay to characterize batches according
to their TIA.
Owing to their proteic nature, protease inhibitors can be inactivated by heat
processing such as extrusion (Bertrand et al., 1982; Grosjean and Gatel, 1989;
Van Zuilichem and Van der Poel, 1989) infrared radiation (Van Zuilichem
and Van der Poel, 1989 ), micronizing (MeNab and Wilson, 1974 ), autoclav-
ing (Marquardt et al., 1974), steam processing (Van der Poel et al., 1990) or
flaking (Marlier et al., 1989). The extent to which TIA is reduced by heat
322 F. Gatel / Animal Feed Science and Technology 45 (1994) 317-348
Table 3
Trypsin inhibiting and haemagglutinating activities of various pea cultivars
Reference I Cultivar Seed type S / W 2 N 3 T I U m g - I D M Haemagglutinating

activity
Mean_+ SD Range (units m g - 1 D M )
a Brite, Rondo Smooth 2 - 0.58-0.84

Multistar, Puget Wrinkled - 2 - 0.66-0.68
Progretta, Macro Wrinkled - 2 - 3.86-4.62
Minerva, Marathon 4 Smooth - 3 0.52_+0.40 0.15-1.07
Rosakrone
b Belinda Smooth S 6 2.36 _+0.56
Birte Smooth S 5 2.44_+ 0.48
Consort Smooth S 6 6.08 _+ 1.16
Miranda Smooth S 5 2.59_+0.52
Finale Smooth S 15 2.02_+ 0.40 -
Amino Smooth S 11 2.13_+ 0.40 -
Maxi Smooth S 4 1.96_+ 0.14 -
Solara Smooth S 14 2.12_+ 0.29 -

Countess Smooth S 6 3.25_+0.59 -
Progretta Wrinkled S 8 8.40_+ 1.07 -
Frijaune, Fril~ne Smooth W 6 10.25 -
Frisson
Amac, Laser Smooth W 6 7.39 -
Santon
c Various - 3 3.10_0.29 2.90-3.50
Various 4 3 4.50_+0.45 3.90-5.00
d Legio, Colmo, Smooth S - 4.20-5.50 100-400
Eryli
Frimas Smooth W - 9.4-11.70 100-400
Lincoln, Tezieride Wrinkled S - 2.70-3.70 200-400
Frogel Wrinkled W 5.70-9.40 100-400
e Amino Smooth S I1 3.50_+ 0.63 2.70-4.50
Finale Smooth S 13 3.10+_0.40 2.30-3.60
Frimas Smooth W 18 11.60_+ 1.72 8.2-14.10
Frisson Smooth W 8 12.50_+2.42 10.2-15.90
Vendevil Smooth W 8 7.90_+ 1.95 5.8-11.60
la, Grifiiths ( 1984; method of Erlanger et al. ( 1961 ) ).

b, Leterme et al. ( 1990a; method of Kakade et al. (1974) ).
c, Pisulewski et al. ( 1983; method of Kakade et al. (1974) ).
d, Valdebouze et al. (1980; method of Kakade et al. (1974) for TIA, and method adapted from Liener
( 1955 ) for haemagglutinating activity).
e, Valdebouze and Gaborit ( 1985; method of Kakade et al. (1974) ).
2S, spring; W, winter.
3Number of samples.
4Coiouredoflowered cultivars.
depends on initial level, temperature, heating time, particle size, moisture

(Liener, 1983; Griffiths, 1984), and probably species and variety. In the ex-
periment carried out by Van Zuilichem and Van der Poel (1989), trypsin
Table 4
Trypsin inhibiting and haemagglutinating activities of various field bean cultivars
Reference I Cultivar S / W 2 N3 TIU m g - i DM Haemagglutinating

activity (units mg - ~DM)
Mean + SD Range
a White flower 1.56

Marls Bead 1.55
Danas 1.47
Minden 1.47
Dacre 1.41
b Klein-Thiiringer 2.2 4.2
Diana 2.3 4.0
Hertz-Freya 2.7 3.5
Ackerperle 2.2 2.9
c Ackerperle 3.2 4.4
Bell 3.2 3.9
Blue Rock 3.2 3.6
Diana 4.3 4.4
Erfordia 2.7 5.6
Foecnevije 2.7 3.8
Herra 3.2 3.4
Klein Korninge 3.2 3.4
d Soravi, Marls Beagle W 2 3.5 25-50
Erfordia S 1 3.5 50
Kristall S 1 3.5 100
Ackerperle S 1 4.0 50
Avrissot W 1 4.0 50
Maxime, Aria S 2 4.5 25
Bianka S 1 4.5 25-50
Rovasse W 1 4.5 25-50
Survoy, Throws W 2 4.5 50
Marls Bead S 1 5.0 25
Ascott S 1 5.0 25-50
Diana S 1 5.0 50
e Talo W 7 5.4+0.71 4.4-6.3
Ascott S 6 5.0+0.73 4.1-6.1
ta, Griffiths ( 1984; method of Erlanger et al. ( 1961 ) ).

b, Marquardt et al. ( 1974; method of Rhodes et al. ( 1957, 1960) for TIA, and method adapted from
Liener ( 1955 ) for haemagglutinating activity).
c, Marquardt et al. ( 1975; method adapted from Kassel (1970) for TIA, and method adapted from
Liener ( 1955 ) for haemagglutinating activity).
d, Valdebouze et al. ( 1980; method of Kakade et al. (1974) for TIA, and method adapted from Liener
( 1955) for haemagglutinating activity).
e, Valdebouze and Gaborlt ( 1985; method of Kakade et al. (1974) ).
2S, spring; W, winter.
~Number of samples.
inhibitors ofP. sativum hortense cv. Finale were fully inactivated after extru-
sion at 105 ° C. For a batch of P. sativum arvense, however, a temperature of
125 °C was necessary to inactivate trypsin inhibitors totally. Conversely, the
324 F. Gate!/AnimalFeedScienceand Technology 45 (1994) 317-348
potential of pelleting as a means to reduce TIA seems low (Carr6 et al., 1987;
Grosjean et al., 1989); in the experiment carded out by Grosjean et al. (1989),
steam pelleting (80 °C) of a whole diet containing 30% winter or spring peas
did not change TIA. This could be explained by the findings of Griffiths
(1984) that trypsin and chymotrypsin inhibitors were stable at temperatures
below 80 ° C.
Lectins
Lectins, otherwise referred to as phytohaemagglutinins, are glycoprotein
compounds which in vitro agglutinate red blood cells. In vivo they can bind
to receptors of epithelial cells of the intestinal mucosa and disturb the diges-
tive processes. In field beans, Marquardt et al. (1975 ) reported that lectins
were located in the cotyledons. Lectin contents of various cultivars of peas
and field beans are reported in Tables 3 and 4. Peas have generally higher
contents than field beans (Valdebouze et al., 1980), but in both cases the
content is much lower than that found in raw defatted soyabean meal (about
1600-3000 units mg -~, according to Valdebouze et al. (1980)) or in other
legumes such as kidney beans (Huisman et al., 1990a). Variability exists also
between cultivars of the same species or perhaps even between samples of the
same cultivar; for instance, Marquardt et al. ( 1974, 1975 ) reported values of
2.9 and 4.4 for the Ackerpede variety.
The analytical method used to measure the lectin content in feedstuffs is a
matter of discussion: lectin analysis is generally based on the ability to bind
with sugars of the glycoproteins of red blood cells. However, erythrocytes from
various animal species agglutinate to a different extent with lectins present in
one legume sample (Marquardt et al., 1975; Huisman et al., 1990a) and it is
questionable whether this method can actually predict the binding capacity
of lectins with glycoproteins of the gut wall and thus their pathogenicity.
Moreover, different grain legumes or even a sample from one variety can con-
tain different types of lectins with different sugar specificity (Liener, 1989)
which are not pathogenic to the same extent but will react similarly in vitro.
On the other hand, some lectins do not haemagglutinate red blood cells al-
though they can react with the gut wall. These observations led Huisman et
al. (1990a) to conclude that the haemagglutination test is probably not a very
good indication of quantity and pathogenicity oflectins. A new approach based
on an ELISA technique and called FLIA (functional lectin immuno assay)
measures the ability of lectins to bind to microtitre plates coated with either
carbohydrate matrices or brush border membranes (Huisman and Jansman,
1991 ). This method allows a specific measurement of the pathogenic lectins
which react with the gut wall.
As protease inhibitors, lectins are inactivated by heat treatments, the main
factors being the duration of heating and the temperature. Steam heating also
seems more efficient than dry heating. However, steam pelleting of field beans
F. Gatel ~Animal Feed Science and Technology 45 (1994) 317-348 32 5
failed to produce any reduction in haemagglutinating activity (Marquardt et

al., 1974, 1976; Liener, 1983; Van Zuiliehem and Van der Poel, 1989; Van
der Poel et al., 1990).
Protein availability
The availability of an amino acid is defined as the proportion of the amino

acid in the diet that is absorbed in a form suitable for utilization when it is
the first limiting factor of the diet (Henry, 1985 ). As defined, availability is
an abstract concept which cannot be measured but can only be estimated.
Growth assays (slope-ratio assays) are generally considered as providing the
best estimation of availability. However, they are expensive, time consuming,
and rely on several assumptions of questionable validity (Sibbald, 1987 ). For
grain legumes, very few workers have undertaken the determination of amino
acid availability: lysine availability of peas for pigs was measured by Batter-
ham et al. (1984). In poultry, Reddy et al. (1979) measured methionine
availability in several pea varieties. Digestibility assays provide a good pre-
diction of production performance and protein quality, and offer the advan-
tage of measuring the digestibilities of protein and amino acids in a single
assay.
Faecal digestibility of crude protein

Literature on protein digestibility coefficients for legume grains is scarce
and sketchy. In most studies, a limited number of batches or varieties was
studied, and comparison of these studies is difficult owing to variations in
methods and incomplete information. However, over the last 20 years a sig-
nificant number of batches of peas or field beans has been studied on pigs,
using the same method, at the INRA Pig Research Center of St. GiUes
(France) (peas: Bourdon and Henry, 1973; Bourdon et al., 1977; Bourdon
and P6rez, 1982; Grosjean et al., 1989, 1991; field beans: Henry and Bour-
don, 1973; Pastuszewska et al., 1974; Du6e et al., 1979; Bourdon and P6rez,
1984). These data, together with some unpublished results, have been sum-
marized by P6rez and Bourdon (1992) for peas and Bourdon and P6rez
(1992) for field beans (Table 5 ). Faecal apparent crude protein digestibility
of peas appears highly variable. It is lower for coloured-flowered peas than for
white-flowered peas. Among the latter, it is higher for spring than for winter
varieties (P6rez and Bourdon, 1992). Additional data published by Lund and
H~ikansson ( 1986 ), H1/Sdverson (1987a,b) and Leterme et al. (1990a) con-
firm this observation. For field beans, it is slightly higher in white-flowered
tannin-free varieties and in coloured-flowered winter varieties than in col-
oured-flowered spring varieties (Bourdon and P6rez, 1992). For both peas
and field beans, within-variety variability is important.
Table 5
Pig faecal apparent digestibility coefficient of nitrogen for peas and field beans
N t Mean + SD Range
Coloured-floweredpeas
a 4 0.754±0.069 0.670-0.840
b 1 0.798
c 1 0.708
White-floweredsmooth-seeded
sp~ngpeas
a 8 0.862±0.023 0.822-0.888
b 2 0.795-0.867
c 2 0.832-0.899
d 1 0.860
e 1 0.910
White-flowered wrinkled-seeded
spring peas
e 1 0.818
White-flowered smooth-seeded
winter peas
a 13 0.819+0.049 0.740-0.876
Coloured-flowered winter
field beans
f 8 0.8084 + 0.041 0.719-0.856
Coloured-flowered spring
field beans
f 9 0.834 + 0.032 0.788-0.876
White-flowered field beans

f 4 0.825 + 0.056 0.758-0.888
a, Pdrez and Bourdon (1992). b, H15dversson (1987a). c, Hl/Sdversson (1987b). d, Lund and H~ik-
ansson (1986). e, Leterme et al. (1990a). f, Bourdon and Pdrez ( 1992 ).
Number of samples.
Ileal digestibility of amino acids
Numerous experiments have been conducted, especially on peas for pigs

(Table 6). Whatever the amino acid considered, results are variable between
workers.
Methodological sources of variation

The analytical method used is one major cause of variation. Owing to amino
acid fermentation in the hindgut, there is now a general agreement on the
need to rely on ileal rather than faecal digestibility. The former appears more
Table 6
Pig ileal digestibility coefficients o f selected a m i n o acids for p e a s
Reference Cultivar T/A ~ Cannula/anastomosis Lysine Methionine Cystine Threonine Tryptophan
Buraczewska et al. ( 1 9 8 9 ) Belinda T2 Cannula 0.850 0.790 0.680 0.840 0.770

Belinda T2 Cannula 0.760 0.650 0.610 0.730 0.670 ~-
Kalistine T2 Cannula 0.860 0.800 0.690 0.630 0.780
Mize T2 Cannula 0.790 0.720 0.590 0.740 0.680
Opal T2 Cannula 0.760 0.590 0.440 0.690 0.570
P. a r v e n s e T2 Cannula 0.720 0.580 0.480 0.650 0.580
G r e e n (1988) Amino A Anastomosis 0.830 0.760 0.620 0.740 - ~"
G r o s j e a n et al. ( 1991 ) Solara T2 Anastomosis 0.830 0.788 0.695 0.778 0.804
P. a r v e n s e T2 Anastomosis 0.776 0.705 0.672 0.658 -
H e i n z et al. ( 1991 ) Finale A Cannula 0.834 - - 0.754
Frijaune A Cannula 0.798 - - 0.605 - '~
Finale T3 Cannula 0.904 - - 0.921 -
Frijaune Ta Cannula 0.873 - - 0.813 -
Jondreville et al. ( 1 9 9 2 ) Solara A Anastomosis 0.828 0.807 0.713 0.765 0.700
oo
H 61 A Anastomosis 0.763 0.752 0.625 0.687 0.625
Laser A Anastomosis 0.665 0.700 0.551 0.602 0.466
Frijaune A Anastomosis 0.659 0.684 0.532 0.600 0.501
L e t e r m e et al. ( 1 9 9 0 ) Solara A Cannula 0.795 0.781 0.636 0.655 0.583
A Anastomosis 0.756 0.709 0.617 0.606 0.652
M o u g h a n a n d S m i t h ( 1985 ) A Cannula 0.730 0.750 0.650 0.660
Sauer et al. ( 1 9 9 0 ) Trapper A Cannula 0.900 0.789 - 0.783
Progreta A Cannula 0.783 0.581 - 0.568
~T, true; A, apparent.

2N-Free diet.
3 ~5N technique.
sensitive in detecting differences in amino acid digestibilities between feed-

stuff samples (Sauer and Ozimek, 1986). However, the method used to col-
lect ileal digesta may vary greatly and has led to different results as shown by
K6hler et al. ( 1993 ). In the case of peas, this is illustrated by data from Let-
erme et al. (1990b), who compared on the same batch of peas ileo-rectal an-
astomosis and T cannula techniques, and observed significant differences for
some essential amino acids (methionine and tryptophan).
The expression of results as true or apparent digestibility is also a matter of
discussion. Basically, true digestibility seems a better approach. However, the
endogenous contribution to digesta is generally estimated through animals
fed a protein-free diet whose endogenous secretion may vary according to the
composition of the protein-free diet and their proteic status (De Lange et al.,
1989a,b). It is thus likely to differ from that of an animal fed a normal diet.
This inaccuracy of the estimation can be particularly high with feedstuffs such
as grain legumes where the occurrence of ANF can substantially modify diges-
tive functions and thus endogenous secretions. For instance, Heinz et al.
(1991 ) observed through digestibility experiments completed by 15N tech-
nique that the recovery of undigested endogenous protein at the end of the
ileum was 20-30% higher with peas or field beans than with toasted soyabean
protein. It can be assumed that ileal digestion of peas or field beans needed at
least 20-30% more endogenous protein (digestive enzymes). However, from
a practical point of view, if a feedstuff leads to particularly scarce or to abun-
dant endogenous secretions, it appears relevant to take this into account when
establishing its feeding value. In that respect, apparent digestibility may be a
more reliable way to express amino acid digestibility of grain legumes. Never-
theless, when considering apparent digestibility, attention must be paid to the
protein content of the experimental diets and subsequent protein intake. If
intake is too low, the endogenous secretion will amount to a large proportion
of total digesta, especially for those amino acids which occur at low levels in
the diet or at high levels in endogenous secretions. This situation will then
result in severe under-estimation of digestibility.
Age or physiological stage of animals used to measure digestibility can also
affect results, especially when comparisons are made; for instance, Christison
and Para de Solano (1982) observed a 5-10% increase in faecal apparent
crude protein digestibility of various protein-rich feedstuffs in piglets 21-42
days old. Compared with soyabean meal or barley protein concentrate, the
largest increase was observed with pea protein concentrate whose digestibility
coefficient was similar to that of soyabean meal at 42 days but was signifi-
cantly lower at 21 days. In poultry, Carr6 et al. ( 1991 ) compared digestibility
coefficients of either winter or spring peas in growing chicks or adult cocker-
els. The apparent digestibility of pea protein was significantly higher in young
birds than in adults, with a more pronounced effect observed with spring peas
and with pelleted winter peas. It appears necessary therefore for comparison
of different feedstuffs to rely on a homogeneous set of results achieved under
standard conditions.
Between- or within-variety variability

Average crude protein and amino acid ileal digestibility values of grain leg-
umes for pigs and poultry, from Rhbne Poulenc Animal Nutrition (1989),
are given in Table 7 and compared with values for wheat and soyabean meal.
Peas and field beans are characterized by a high digestibility of lysine and
threonine. In contrast, crude protein and sulphur amino acid digestibilities
appear low, especially in the case of pigs. Data from Buraczewska et al. (1989),
Saner et al. (1990), Grosjean et al. (1991 ) and Jondreville et al. (1992)
demonstrate the evidence of variability between varieties. For peas, digesti-
bility seems lower for coloured-flowered (P. arvense) than for white-flowered
(P. hortense) varieties (Buraczewska et al., 1989; Grosjean et al., 1991 ). In
white-flowered cultivars, winter varieties or wrinkled-seeded varieties such
as Progreta also seem to be characterized by a lower digestibility (Sauer et al.,
1990; Jondreville et al., 1992). Similarly, amino acid digestibility coefficients
for pigs of white-flowered tannin-free field bean cultivars are higher than those
for coloured-flowered cultivars (Maillard et al., 1990). ) Finally, even when
considering a single technique applied to the same variety, some differences
can still be found: the determination of digestibility of the cultivar Solara
with the ileo-rectal anastomosis technique by Leterme et al. (1990), Gros-
jean et al. (1991) and Jondreville et al. (1992) led to differences of up to
0.152 in the case of tryptophan. These differences can reflect differences in
method (at either the animal or the analytical level) or a within-variety var-
Table 7
Average nitrogen and amino acid ileal digestibility coefficients of various feedstuffs for pigs and poul-
try (Rh6ne Poulenc Animal Nutrition, 1989)
Apparent digestibility coefficient Nitrogen Lysine Methionine Cystine Threonine

for pigs I
Spring peas 0.743 0.815 0.767 0.621 0.710

Field beans 0.763 0.837 0.741 0.771 0.741
Lupin 0.708 0.656 0.536 0.695 0.693
Wheat 0.801 0.679 0.844 0.816 0.677
Soyabean meal 0.798 0.847 0.862 0.762 0.786
True digestibility coefficient Nitrogen Lysine Methionine Cystine Threonine

for poultry2
Spring peas 0.906 0.869 0.886 0.777 0.877

Fidd beans 0.778 0.819 0.767 0.516 0.805
Lupin 0.953 0.913 0.933 0.937 0.947
Wheat 0.869 0.816 0.885 0.820 0.791
Soyabean meal 0.892 0.885 0.906 0.818 0.870
1Excreta collected for 48 h on ileo-rectal anastomized growing pigs after a 5 day adaptation period.
2Excreta collected for 48 h on caecectomized adult cockerels, force-fed with 50 g of diet at once after
a 48 h period of food deprivation. Endogenous secretion measured on a protein-free diet.
iability (Buraczewska et al., 1989). In agreement with the latter point, the
amino acid digestibilities found for the pea cultivar Frijaune by Jondreville
et al. (1992) are particularly low and cannot be attributed to technique; on
the contrary, they could be attributed to an atypical batch of peas. From a
practical point of view, the problem is probably similar for other legumes and
for other feedstuffs where such a variability is observed (Sauer and Ozimek,
1986). Nevertheless, as no method has been developed to estimate quickly
and cheaply the actual protein or amino acid digestibility of each batch of raw
ingredient, the only way to take into account this variability is to limit the
incorporation of each ingredient in feed formulation and to take into account
a safety margin when estimating their feeding value.
Role of antinutritional factors
Many studies have been undertaken to investigate the causes of variation

of protein digestibility in legume grains. Owing to the occurrence in most spe-
cies of ANF, such studies have focused on their possible implication in diges-
tive processes and nutrient availability. However, other factors such as the
presence of fibrous compounds or protein accessibility also seem of interest
in this respect. Non-starch polysaccharides (NSP) are known to depress di-
gestibility of many nutrients including proteins. In some legume seeds (lupin,
Phaseolus bean), Chang and Sattedee ( 1981 ) and Semino et al. ( 1985 ) char-
acterized carbohydrates bound to proteins, resulting in interference with pro-
teolysis. However, all NSP do not affect digestion in the same way and to the
same extent (P6rez, 1991 ). Peas in particular contain highly soluble NSP
whose digestibility is very high compared with that of other ingredients such
as wheat or field beans (Goodlad and Mathers, 1991; Jansman et al., 1991 ).
Moreover, even the same category of NSP do not have the same effects ac-
cording to their botanical origin: a galactosides are generally known to pro-
voke flatulence (Cristofaro et al., 1974), but Saini (1989) reviewed differ-
ences in degree of response among legume species. For instance, flatulence
occurs with lupin intake whereas pea a galactosides do not lead to flatulence.
In addition to protease inhibitors and lectins, legume grains can contain
other antinutritive compounds, namely tannins (field beans and peas), vicin
and convicin (field beans) and alkaloids (lupin). Among these ANF, essen-
tially protease inhibitors, lectins and tannins are likely to have an effect on
protein digestibility. Protease inhibitors, which have mainly been studied in
soyabean fed to rats, primarily inactivate proteolytic enzymes (i.e. trypsin
and chymotrypsin) secreted by the pancreas. As a secondary effect, the neg-
ative feedback control mechanism of pancreas secretion is disturbed and pan-
creatic enzyme secretion enhanced (Liener, 1989 ), leading in certain animal
species to pancreatic enlargement (Birk, 1989). As pancreatic enzymes are
rich in sulphur amino acids, this diverts methionine and cystine from body
F. Gatel ~Animal Feed Science and Technology 45 (1994) 317-348 33 1
tissue synthesis. However, with diets based on barley and peas or lupin fed to
pigs, Buraczewska et al. ( 1991 ) did not observe any alteration of pancreatic
juice or pancreatic enzyme output compared with barley-based diets, whereas
a diet based on field beans and wheat starch led to lower pancreatic enzyme
secretion. This latter finding remains unexplained. The former is in agree-
ment with findings of Le Guen et al. (1991a) that pea ANF concentrates
added to diets based on pea protein isolate did not affect pancreas weight or
enzymatic activity of the pancreas. Most studies on lectins have been carried
out with kidney beans (Phaseolus vulgaris) and were recently reviewed by
Van der Poel (1990). Lectins have the ability to bind to specific receptor sites
on the surface of the epithelium cells lining the intestine. This results in brush
border damage and interference with absorption and transport of nutrients
across the intestinal wall (Liener, 1989; Kik et al., 1990; Huisman and Jans-
man, 1991 ). Although not fully elucidated in vivo, it is assumed that tannins
and other polyphenolic compounds form complexes with proteins or other
constituents. Protein complexation can occur with dietary protein or diges-
tive enzymes, mucosal proteins or glycoproteins from saliva. Consequently,
the digestibility of feed protein and carbohydrates are decreased and digestive
enzymes may be inactivated. The physiological effects of ANF- or ANF-con-
taining feedstuffs differ widely between animal and crop species (Huisman
et al., 1991 ). As a consequence, digestive, physiological or biological re-
sponses to ANF must be studied in the target animal. Moreover, several ANF
are generally associated in legume grains, which often makes it difficult to
isolate the actual effect of the individual ANF on protein digestibility.
Peas
Attention has been paid to protease inhibitors. In many studies where va-
rieties were compared it was found that protein or amino acid ileal digestibil-
ity in pigs yielded results in the same order as their trypsin inhibiting activity
(Leterme et al., 1990a; Heinz et al., 1991; Jondreville et al., 1992). However,
in these studies varieties differ in TIA content and also in some other botan-
ical and agronomical characteristics: Leterme et al. (1990a) compared Finale
(a smooth-seeded cultivar) and Progreta (a wrinkled-seeded cultivar),
whereas Heinz et al. ( 1991 ) and Jondreville et al. ( 1992 ) compared smooth-
seeded spring and winter cultivars. Moreover, in a study of white-flowered or
coloured-flowered peas whose TIA varied in the range of 0.77-15.94 TIU
nag- 1, Gdala et al. ( 1991 ) observed a wide variation in ileal nitrogen or amino
acid digestibility which was independent of TIA. In chickens, similarly, Carr6
and Conan (1989) failed to observe any significant correlation between ap-
parent digestibility of various cultivars of raw peas and TIA. Using a different
approach, Huisman et al. (1990b) compared in early weaned piglets the di-
gestibility of diets containing either untreated peas from Finale or Frijaune
varieties or pea protein isolates from both varieties. The Finale and Frijaune
peas, respectively, were characterized by low and high levels of ANF (trypsin
inhibitors and lectins), whereas pea protein isolates of either variety con-
tained low levels of ANF. Apparent ileal nitrogen digestibility of diets con-
taining peas was 72%, regardless of the variety, whereas it was 86% and 87%,
respectively, for the diets containing pea protein isolates from Finale and Fri-
jaune. These results led to the conclusion than factors other than pea protein
itself were responsible for the low apparent ileal protein digestibility of raw
peas. It is, however, possible that isolation of pea proteins may have modified
their physical properties and thus their accessibility to digestive enzymes. In
a subsequent experiment, Huisman and Le Guen ( 1991 ) tested the effect of
addition of isolated pea carbohydrate fraction to either a control diet or diets
whose protein source was Finale pea protein isolate or Frijaune pea protein
isolate. There was no reduction in apparent ileal protein digestibility as a re-
sult of the addition of pea carbohydrates. On the other hand, the addition of
mixed pea ANF concentrates extracted from Finale and Frijaune and con-
taining high levels of trypsin inhibitors and lectins to a diet based on pea
protein isolate from Finale resulted in a significant reduction in apparent ileal
protein digestibility. ANF seem then to be involved as a cause of the low crude
protein digestibility observed in piglets. Moreover, as Bertrand et al. ( 1988 )
did not observe any antinutritional effect of native or purified pea lectins in
young pigs, the trypsin inhibitors appear to be the more important ANF in-
volved in piglets.
However, other factors could also be involved; for instance, Ivanko et al.
( 1991 ) pointed out the structure of native pea or field bean protein as a cause
of decreased hydrolysability by digestive endopeptidases. Moreover, Nielsen
et al. ( 1988 ) and Deshpande and Damodaran ( 1989 ) reported markedly dif-
ferent in vitro susceptibility to trypsin between 7S globulins of various leg-
ume seeds. These differences are probably due to the tertiary structure of the
protein itself and protection of protease-susceptible regions (Romero and
Ryan, 1978, Reddy et al., 1988 ) and/or to the higher or lower degree of sta-
bility or flexibility of this structure (Deshpande and Damodaran, 1989). Al-
though Huisman and Le Guen ( 1991 ) did not observe any effect of isolated
pea carbohydrate fraction on crude protein digestibility, cell wall constituents
of native peas could also be related to protein and amino acid digestibility, as
observed by Gdala et al. ( 1991 ) for the NDF fraction, Hauschild and KShler
( 1991 ) for lignin, and Jondreville et al. (1992) for the ADF fraction. Simi-
larly, Grosjean et al. ( 1992 ) found a lower nitrogen digestibility for pea hulls
than for dehulled or whole peas, and a higher proportion of ADF in the NDF
fraction for the former. In poultry, Carr6 et al. ( 1991 ) inferred that a non-
specific factor affecting protein and starch, namely non-accessibility of nu-
trients to digestive enzymes owing to a strong cellular cohesion in pea cotyle-
don, rather than ANF, could act on protein digestibility. As hypothesized for
F. Gatel /Animal Feed Science and Technology45 (1994) 317-348 333
pigs, protein structure could also be a limiting factor to their digestibility in

poultry. This, however, needs confirmation.
Field beans
In field beans a wide variation of protein or amino acid digestibility is ob-
served, which seems to be partly linked to variety. In most experiments in-
volving a comparison of varieties, those with no tannins (white-flowered va-
rieties) exhibited a higher nitrogen or amino acid digestibility either in pigs
(Du6e et al., 1979; Liebert and Gebhardt, 1983; Bourdon and P~rez, 1984;
Jansman et al., 1989; Maillard et al., 1990; Heinz et al., 1991 ) or in poultry
(Martin-Tangny et al., 1977; Guillaume, 1978; Lacassagne et al., 1988, 1991 )
(Table 8). Even in the comparison completed by Mosenthin et al. (1991),
where no significant difference appeared between white- and dark-flowered
varieties, there was a tendency towards a higher nitrogen and amino acid di-
gestibility in the white- than in the dark-flowered variety. When statistically
significant, differences in protein digestibility ranged from 3 to 15%.
In a comparison of cultivars of field beans varying widely in tannin con-
tent, Martin-Tangny et al. (1977) observed in growing chicks a decreased
apparent nitrogen digestibility with increase in tannins. However, one low-
tannin variety had a low apparent nitrogen digestibility which suggested that
additional ANF were present or that only some fractions of tannins actually
depressed digestibility of nitrogen compounds. The latter assumption was
supported by the fact that a significant negative correlation was found be-
tween apparent nitrogen digestibility and the least highly polymerized frac-
tion of tannins. More recently, Brun et al. (1992) showed that the tanning
capacity of various genotypes of field beans was related not only to tannin
content but also to their degree of polymerization. Jansman et al. (1989)
measured ileal apparent nitrogen digestibility of four varieties of field beans
with different tannin contents in piglets. Digestibility coefficients were de-
pressed in parallel with an increase in tannin content of varieties, with a 17%
digestibility difference between the extremes. Finally, Garrido et al. ( 1989 )
measured in vitro protein digestibility (HC1 pepsin method; AOAC, 1975 )
on 24 strains of field beans including white- and coloured-flowered varieties
with different tannin contents. A significant negative correlation coefficient
( r = - 0 . 8 5 , P < 0.001 ) was found between in vitro protein digestibility and
tannin content. As tannins are mainly located in the hulls of field beans, many
studies have been carded out using different fractions of field beans or even
other sources of tannins. Jansman et al. ( 1991, 1992 ) observed that inclusion
of hulls of field beans of a high-tannin variety in pig diets decreased nitrogen
digestibility as compared with control diets with either pea hulls or hulls of
field beans from a low-tannin variety. This effect of tannin on protein diges-
tibility can be explained by a lower trypsin activity as a result of the formation
of a reversible tannin enzyme complex, as demonstrated in vitro by Griffiths
Table 8
Effect of tannin content and dehulling on field bean nitrogen and amino acid digestibility
Reference Animal Procedure Component High-tannin Low-tannin Dehulled

species variety variety high-tannin
variety
a Pig 1 Nitrogen 0.719 a 0.758 ab

0.802 b
b Pig 1 Nitrogen 0.771 a 0.851 b
c Cockerel 1 Nitrogen 0.704 0.806
d Piglet 2 Nitrogen 0.744 a 0.791 b
Lysine 0.772 a 0.804 b
Methionine + cystine 0.589 a 0.621 b
Threonine 0.723 a 0.768 b
e Pig 1 Nitrogen 0.852 0.894
f Piglet 2 Nitrogen 0.753 a 0.853 b
0.741 a
0.687 a
g Chicken 1 Nitrogen 0.669 a 0.826 b
0.694 a
h Chicken 1 Nitrogen 0.694 a 0.842 b
i Pig Nitrogen 0.792 0.835
j Pig 3 Nitrogen 0.818 a 0.846 b 0.877 b
Lysine 0.867 a 0.882 a 0.909 a
Methionine 0.781 0.773 0.818
Threonine 0.808 a 0.824 a 0.869 b
k Pig 4 Nitrogen 0.694 0.719
Lysine 0.782 0.813
Threonine 0.573 0.623
1 Pig 1 Nitrogen 0.788 0.862
a, Bourdon and P6rez (1984). b, Du6e et al. (1979). c, Guillaume (1978). d, Heinz et al. ( 1991 ). e,
Henry and Bourdon (1973). f, Jansman et al. (1989). g, Lacassagne et al. ( 1988 ). h, Lacassagne et
al. ( 1991 ). i, Liebert and Gebhardt (1983). j, Maillard et al. (1990). k, Mosenthin et al. ( 1991 ). 1,
Pastuszewska et al. (1974).
1, Apparent faecal digestibility.
2, Apparent ileal digestibility measured with post-valvular T caecum cannula.
3, True ileal digestibility measured with ileo-rectal anastomosis.
4, True ileal digestibility measured with T cannula.
(1979, 1981 ), and in vivo by Griffiths and Moseley (1980) on rats. In the
latter experiment, whereas no effect on pancreas weight was noted, pancreas
activity was enhanced, as shown by an increase in intestinal lipase activity.
The different changes in enzyme activity in the gut were explained by a dif-
ferential affinity of tannin for lipase and for trypsin or other digestive enzymes.
In an experiment on chickens, Ahmed et al. ( 1991 ) compared diets with
varying content of tannins. Increasing content of tannins resulted in a signif-
icant increase in pancreas weight and in trypsin and a amylase activities in
the pancreas of birds, with an increased inhibition of trypsin activity in the
intestinal lumen and of dipeptidase in the intestinal mucosa. At the same time,
F. Gatel / Animal Feed Science and Technology 45 (1994) 317- 348 335
nitrogen digestibility was negatively affected by the tannin content of the diet.
Longstaff and McNab ( 1991 ) fed chickens with diets containing hulls from
various cultivars of field beans. The diets with tannin-rich hulls decreased
digestion of nitrogen and other nutrients. These effects were due mainly to
the reversible inactivation of digestive enzymes, trypsin being the most ad-
versely affected. However no increased pancreatic production of digestive en-
zymes was noted nor was the enzyme activity of the jejunum mucosa affected.
Other factors can interfere with nitrogen digestibility, especially in poultry.
Longstaff and McNab ( 1991 ) observed a slight reduction in amino acid di-
gestibility subsequent to the addition of hulls from a tannin-free variety to a
control diet. This effect appeared different from a simple diluting effect of
hull non-starch polysaccharides, and seemed to be due to the inhibition of
digestive enzymes, possibly through their adsorption onto the hulls. In pigs,
however, Jansman et al. ( 1991 ) did not observe any deleterious effect of the
addition of hulls from a tannin-free variety of field beans on nitrogen diges-
tibility. Rubio and Brenes (1989), with chickens compared untreated and
autoclaved field beans or field bean cotyledons, alone or added to hulls, and
suggested the existence of a thermostable cotyledon carbohydrate fraction able
to increase intestinal transit time. Other workers dealt with the effect of de-
hulling; in most cases, dehulling a high-tannin containing variety led to a 4-
7% improvement of nitrogen digestibility (Henry and Bourdon, 1973; Pas-
tuszewska et al., 1974; Maillard et al., 1990) (Table 8). In a slightly different
approach, Lacassagne et al. ( 1991 ) found in chickens a similar nitrogen di-
gestibility for cotyledons of either a tannin-free or a tannin-containing field
bean.
Possibilities of improvement
Considering the involvement of ANF in nitrogen digestibility and the ge-
netic variation between varieties for ANF content, attempts have been made
to reduce ANF content in legumes by genetic selection. A difficulty is that
most ANF have functions in the growth and protection of the plant (Bond
and Smith, 1989). Any decrease in ANF level must preserve these functions
as well as improve nutritional quality, which makes necessary the co-opera-
tion between plant breeders and nutritionists to set up nutritional guidelines
which could be used as a target in breeding programmes. According to Bond
and Smith ( 1989 ), selection on TIA is possible but will be probably of low
priority, owing to the lack of associated characters and the effect of environ-
ment on TIA. In peas, it seems necessary, however, to take into account any
parentage with high-TIA varieties, such as Maro, Progreta or winter smooth-
seeded varieties. Selection of tannin-free field beans is possible, and is simple,
on the basis of the white flowers of low-tannin varieties (Duc and Lacassagne,
1990).
Effect of treatments
Various treatments have been tested to improve the feeding value of grain
legumes to their full potential, particularly through destruction of ANF and
possibly through increased accessibility of protein to enzymatic attack. For
instance, Van der Poel et al. (1991a) showed that reconstitution (i.e. mois-
tening and anaerobic storage of seeds for several days), extrusion or reconsti-
tution followed by extrusion resulted in a 500 decrease in field bean tannin
level, extrusion being associated with an improved in vitro protein digestibil-
ity. Germination for up to 5 days has also been proven to increase digestibility
of field beans' protein (Savelkoul et al., 1991 ). However, results observed in
vivo vary considerably with animal species, age of experimental animals, plant
species and treatment.
With growing-finishing pigs (Table 9), no effect of any of the treatments
tested (pelleting, autoclaving, flaking and extrusion) was observed by any
workers for field beans (Ivan and Bowland, 1976; Aherne et al., 1977 ) or peas
(Bertrand et al., 1982; Grosjean and Gatel, 1989; Grosjean et al., 1989; Mar-
lier et al., 1989). Similarly, with weaned piglets, S~ve et al. (1985) did not
observe any effect on protein digestibility with spring peas that had been
crumbled, dehulled and percolated with amylolytic enzymes. On the con-
trary, Bengala Freire et al. ( 1989, 1991 ) observed in early weaned piglets fed
diets containing 45% untreated or extruded spring peas a 4-5% increase in
faecal apparent digestibility of protein. Such an improvement, however, was
not observed with diets containing only 30% peas (Bengala Freire et al., 1989).
A greater increase (13%) at either the ileal or the faecal stage was observed
when using 45% winter peas (Bengala Freire et al., 1991 ), the larger response
being due probably to the inactivation of ANF by extrusion. In addition, the
workers pointed out that the beneficial effect of extrusion could be associated
with a change in pea starch structure and improvement of starch digestion in
the small intestine, which led to a reduction in the amount of endogenous
nitrogen from bacterial fermentation. Van der Poel et al. ( 199 lb) also showed
that heat treatment can modify the quality of storage protein of kidney beans.
It seemed, however, that ileal digestibility of protein was more or less temper-
ature dependent according to plant species; no study on this aspect has yet
been undertaken for field beans or peas. Finally, one should keep in mind that
overheating of protein may destroy some amino acids and depress amino acid
availability. It is thus necessary to check that any heat treatment decreases
ANF and increases in vivo protein digestibility by the same degree (Van Der
Poel, 1990).
In poultry (Table 10), treatments such as autoclaving, flaking, cold or steam
pelleting, or extrusion significantly improve digestibility of field beans (Guil-
laume, 1978; Huyghebaert et al., 1979; Lacassagne et al., 1988) or peas
(Huyghebaert et al., 1979; Carr6 et al., 1987, 1991; Conan and Carr6, 1989).
F. Gatel / Animal Feed Science and Technology 45 (1994) 317- 348 337
Table 9
Effect of treatment of legume grains on protein digestibility of diets containing legume in pigs
Reference Legume Treatment Animal Criterion Effect/

untreated legume
a 25% Field beans Autoclaving Pigs 1 None

( 120 °C, 15-60 min)
b 60% Field beans Autoclaving Pigs 2 None
( 120°C, 30 or 60 rain)
c 30% Spring peas Extrusion (150°C) Piglets 1 None
45% Springpeas Extrusion (150°C) 28-56 days 1 0.821 vs. 0.784
d 45% Spring peas Extrusion (150°C) Piglets 1 0.873 vs. 0.819
28-56 days 2 None
45% Winter peas Extrusion (150°C) Piglets 1 0.858 vs. 0.726
28-56 days 2 0.784 vs. 0.657
e 33% Wrinkled-
seeded peas Extrusion (250°C) Pigs 1 None
f 40% Spring peas Steam pelleting ( 80 ° C) Pigs 1 None
40% Winter peas Steam pelleting (80°C) Pigs 1 None
g 35% Spring peas Steam flaking Pigs 1 None
25% Spring peas Extrusion Pigs 1 None
h 41% Spring peas Crumbling, Piglets 1 None
dehuUing and 12-29 days
percolating in
amylolytic
enzyme
a, Aherne et al. ( 1977 ). b, Ivan and Bowland (1976). c, Bengala Freire et al. (1989). d, Bengala Freire et
al. ( 1991 ). e, Bertrand et al. (1982). f, Grosjean et al. (1989). g, Marlier et al. ( 1989 ). h, S~ve et al. ( 1985 ).
l, Faecal apparent digestibility. 2, Ileal apparent digestibility.
As with pigs, younger animals seem more responsive to treatment than adults
(Carr6 et al., 1991 ). Moreover, the effect of treatment seems more pro-
nounced with winter than with spring pea cultivars (Conan and Cart6, 1989;
Cart6 et al., 1991 ). However, according to Cart6 et al. ( 1991 ), it is likely that
in poultry fed diets containing peas, the beneficial effect of thermo-mechani-
cal treatments such as pelleting or autoclaving is due to the breakdown of the
cell wall of pea cotyledons, which allows the accessibility of nutrients to diges-
tive enzymes, rather than to the inactivation of ANF. An increased sensitivity
of legume protein to enzyme degradation could also occur; in field beans,
grinding induced an increase in starch digestibility but did not change the
protein digestibility (Totsuka et al., 1977; Lacassagne et al., 1991 ). In peas,
fine grinding slightly improves starch and protein digestibility when the diet
is offered as mash but has no effect when the diet is offered as pellets (Conan
et al., 1992). In field beans, however, Marquardt (1989) suggested that heat
treatment can neutralize the effects of tannins and thereby prevent their in-
teraction with the protein component of the diet, leading to an increased de-
gree of digestion and absorption of protein and amino acids.
Table 10
Effect of technological treatment of legume grains on their apparent protein digestibility in poultry
Reference Legume Treatment Animal Effect/

untreated legume
a 33 or 66% Autoclaving Chickens 0.760 vs. 0.704

Field beans ( 120 ° C, 30 rain) (3 weeks)
b 50% Peas Flaking ( 160 ° C) Adult cockerels 0.880 vs. 0.850
Extrusion (140°C) 0.870 vs. 0.850
Cold pelleting (45°C) 0.860 vs. 0.850
Steam pelleting (60°C) 0.870 vs. 0.850
50% Field beans Flaking (160°C) Adult cockerels 0.820 vs. 0.780
Extrusion (140°C) 0.830 vs. 0.780
Cold pelleting (45 °C) 0.820 vs. 0.780
Steam pelleting (60 ° C) 0.810 vs. 0.780
c 50% Winter peas Single steam pelleting Adult cockerels 0.802 vs. 0.772
(85°C)
Double steam pelleting 0.796 vs. 0.772
(85°C then 70°C)
d 48% Field beans Steam pelleting Chickens 0.706 vs. 0.669
(70°C) (3 weeks)
48% White-flowered Steam pelleting Chickens 0.872 vs. 0.826
field beans (70 ° C) (3 weeks)
e 40% Spring peas Autoclaving Chickens 0.829 vs. 0.786
( 130°C, 3 min) (3 weeks)
40% Winter peas Autoclaving Chickens 0.851 vs. 0.678
(130°C, 3 min) (3 weeks)
f 47% Winter peas Steam pelleting (80°C) Chickens 0.808 vs. 0.759
(3 weeks)
47% Spring peas Steam pelleting (75 ° C) Chickens 0.839 vs. 0.803
( 3 weeks)
g 48% Field beans Fine grinding Chickens None
(hammer mill; 1 mm (3 weeks)
round hole screens)
48% White-flowered Fine grinding Chickens None
field beans ( hammer mill; 1 mm ( 3 weeks)
round hole screens)
h 40% Spring peas Pelleting after normal Adult cockerels 0.829 vs. 0.759
grinding (hammer mill;
4 mm round hole screens)
Pelleting after fine Adult cockerels 0.811 vs. 0.794
grinding (hammer mill;
0.8 mm round hole screens)
a, GuiUaume (1978). b, Huyghebaert et at. ( 1979 ). c, Cart6 et al. (1987). d, Lacassagne et al. ( 1988 ). e,
Conan and Carr6 (1989). f, Cart6 et al. ( 1991 ). g, Lacassagne et al. ( 1991 ). h, Conan et al. ( 1992 ).
Antigenicity of grain legume proteins
Although this aspect has not so far been fully investigated in farm animals
there is evidence that legume seeds contain proteins with antigenic proper-
ties, i.e. able to induce in certain categories of animals local (gut) or systemic
immune responses. Most of the studies in this area have been carried out with
soyabean, the main globulins of which (glycinin and p conglycinin) can alter
digesta movements, digestion and nutrient absorption, gut wall architecture,
and gut motility in the dairy calf. These disturbances are explained by a tran-
sient hypersensitivity to dietary antigens. The changes of active and passive
transfers of molecules across the gut epithelium can also lead to the produc-
tion, in sensitive animals, of specific antibodies, mainly of the immunoglob-
ulin G (IgG) class (Lall~s, 1991 ). In grain legumes, antigenic properties have
been found for lectins, legumin and vicilin.
Pusztai (1989) reviewed the effects of kidney bean lectins on both local
(gut) and systemic immune systems. In rats, Greer and Pusztai (1985) ob-
served a loss of serum protein in the gut, as a result of an increased vascular
permeability mediated by an immediate hypersensitivity mechanism. The re-
sults were more emphasized in rats which had already been fed a diet contain-
ing kidney beans. Moreover, a long-term experiment did not provide evi-
dence of any sign of adaptation to the kidney bean diet, which suggested an
insufficient level of local IgA to eliminate the toxic effect of kidney beans.
One of the systemic effects of lectins in all animal species studied was a pow-
erful and rapid humoral response through the development of antilectin an-
tibodies of the IgG class (Pusztai, 1989 ).
Pea legumin and vicilin antigenic properties have been studied in preru-
minant calves and piglets. Preruminant calves fed a diet containing raw pea
flour exhibited a transient rise of gut permeability to macromolecules, which
could have been due to the low digestibility of pea protein. Concomitantly,
immunoreactive legumin was temporarily found in blood plasma whereas the
antibody titre of anti pea protein, anti legumin and anti vicilin gradually in-
creased (Nunes do Prado et al., 1988, 1989, 1990; Bush et al., 1991 ). In young
piglets (4 or 5 weeks old) a pea-based diet similarly resulted in the produc-
tion of serum antibodies against pea legumin and vicilin, the maximum level
of antibodies being reached at 3 weeks (Le Guen et al., 199 lb). Although this
was not investigated, these results seem to indicate an enhancement of anti-
gen uptake owing to a change in the gut permeability to macromolecules, which
could be explained by toxic agents such as lectins, local hypersensitivity re-
actions in the gut or increased concentration of macromolecules in the intes-
tinal lumen owing to the low digestibility of raw pea protein in the digestive
tract (Van Dijk et al., 1988). However, in this experiment, the observed im-
mune response was not associated with gastrointestinal or general disorders
such as diarrhoea, weight loss or poor growth, and it could therefore be hy-
pothesized that piglets had established a local immune tolerance.
There are differences between species or individuals in their susceptibility
to immunologically induced digestive disorders and the severity and type of
reaction (Lalles, 1991 ). For instance, dietary allergy seems to involve young
rather than adult animals. Previous nutritional history, i.e. exposure to small
amounts of an immunogenic diet, will predispose to subsequent digestive dis-
orders. Finally, the development of an immune response to legume feeding
does not always result in digestive disorders or depressed growth. This is il-
lustrated by the results ofLe Guen et al. (1991b) and Toullec et al. (1992).
More work is obviously required to elucidate the antigenic properties of grain
legume proteins and their effects in non-ruminants. As the only risk reported
concerns very young animals, one practical piece of advice would be to avoid
high levels of legume in their diets.
Acknowledgements
Thanks are due to A. Aumaitre (INRA, St. Gilles), M.P. le Guen (EURE-
TEC, Rennes) and R. Toullec (INRA, Rennes) for their help and critical
review of the manuscript.
References
Aherne, F.X., Lewis, A.J. and Hardin, R.T., 1977. An evaluation of faba beans (Viciafaba) as
a protein supplement for swine. Can. J. Anita. Sci., 57: 321-328.
Ahmed, A.E., Smithard, R. and Ellis, M., 1991. Activities of enzymes of the pancreas, and the
lumen and mucosa of the small intestine in growing broiler cockerels fed on tannin-contain-
ing diets. Br. J. Nutr., 65: 189-197.
Batterham, E.S., Murisson, R.D. and Andersen, L.M., 1984. Availability of lysine in vegetable
protein concentrates as determined by the slope-ratio assay with growing pigs and rats and
by chemical techniques. Br. J. Nutr., 51: 85-99.
Bengala Freire, J., Hulin, J.C., Peiniau, J. and Aumaitre, A., 1989. Effet de la cuisson extrusion
du pois de printemps sur la digestibilit6 des aliments de sevrage pr6coce du porcelet et con-
s6quences sur les performances jusqu'~t l'abattage. Journ. Rech. Porc. Fr., 21: 75-82.
Bengala Freire, J., Aumaitre, A. and Peiniau, J., 1991. Effects of feeding raw and extruded peas
on ileal digestibility, pancreatic enzymes and plasma glucose and insulin in early weaned
pigs. J. Anim. Physiol. Anim. Nutr., 65:154-164.
Bertrand, D., Delort-Laval, J., Melcion, J.P. and Valdebouze, P., 1982. Influence de l'extrusion
et de l'infranisation sur les facteurs antinutritionnels et la valeur alimentaire du pois (Pisum
sativum L. ). Sci. Aliments, 2 (HS II ): 197-202.
Bertrand, G., S~ve, B., Gallant, D.J. and Tome, R., 1988. Absence d'effets antinutritionnels des
lectines de pois sous forme native ou purifi6e, chez le porcelet. Comparaison avec les lectines
natives de soja. Sci. Aliments, 8: 187-212.
Birk, Y., 1989. Protein protease inhibitors of plant origin and their significance in nutrition. In:
J. Huisman, A.F.B. van der Poel and I.E. Liener (Editors), Proc. 1st Int. Workshop on An-
tinutritional Factors in Legume Seeds, Wageningen, Netherlands, 23-25 November 1988.
PUDOC, Wageningen, pp. 83-94.
Bond, D.A. and Smith, D.B., 1989. Possibilities for the reduction of antinutritional factors in
grain legumes by breeding. In: J. Huisman, A.F.B. van der Poel and I.E. Liener (Editors),
Proc. 1st Int. Workshop on Antinutritional Factors in Legume Seeds, Wageningen, Nether-
lands, 23-25 November 1988. PUDOC, Wageningen, pp. 285-296.
Bourdon, D. and Henry, Y, 1973. Valeur ~nerg~tique du pois fourrager et utilisation par le porc
en finition. Journ. Reeh. Pore. Ft., 5:115-121.
Bourdon, D. and P~rez, J.M., 1982. Premiers r~sultats sur la valeur ~nerg~tique et azot~e des
pois prot~agineux de printemps. Journ. Rech. Porc. Fr., 14:261-266.
Bourdon, D. and P~rez, J.M., 1984. Valeur ~nerg~tique et azot~e pour le porc de diffdrents types
de f~veroles pauvre ou fiche en tanins. Journ. Rech. Porc. Fr., 16: 401-408.
Bourdon, D. and P~rez, J.M., 1992. Energy and protein values of faba beans ( Viciafaba minor
L. ) for pigs: synthesis of French results. In: Proc. 1st Eur. Conf. on Grain Legumes, Angers,
France, 1-3 June, pp. 521-522.
Bourdon, D., Jung, J. and P~rez, J.M., 1977. Valeur ~nerg~tique et azot6e de diff~rentes vari6t6s
de pois (Pisum sativum L. ) pour le pore. Journ. Rech. Porc. Fr., 9: 265-269.
Brun, N., Jay, M. and Merghem, R., 1992. A proposition for the study of phenolic and of leg-
umes. In: Proc. 1 st Eur. Conf. on Grain Legumes, Angers, France, 1-3 June, pp. 393-394.
Buraczewska, L., Gdala, J. and Grala, W., 1989. Ileal digestibility of protein in pigs fed diets
with peas of variable content of protein and tannins. In: J. Huisman, A.F.B. van der Pod
and I.E. Liener (Editors), Proc. 1st Int. Workshop on Antinutritional Factors in Legume
Seeds, Wageningen, Netherlands, 23-25 November 1988. PUDOC, Wageningen.
Buraczewska, L., Pohland, U., Gdala, J., Grala, W., Jandwska, G. and Souffrant, W.B., 1991.
Exocrine pancreatic secretion of enzymes in growing pigs given diets based on barley, pea,
lupin or field bean. In: M.W.A. Verstegen, J. Huisman and L.A. den Hartog (Editors), Proc.
5th Int. Symp. on Digestive Physiology in Pigs, Wageningen, Netherlands, 24-26 April. PU-
DOC, Wageningen, pp. 167-172.
Bush, R.S., Toullec, R., Caugant, L. and GuiUoteau, P., 1991. Intolerance to pea protein in the
preruminant calf. In: J.H.M. Metz and C.M. Groenestein (Editors), Proc. Int. Symp. on
Veal Calf Production, Wageningen, Netherlands, 14-16 March, pp. 253-256.
Carr6, B. and Conan, L., 1989. Relationship between trypsin-inhibitor content of pea seeds and
pea protein digestibility in poultry. In: J. Huisman, A.F.B. van der Poel and I.E. Liener (Ed-
itors), Proc. I st Int. Workshop on Antinutritional Factors in Legume Seeds, Wageningen,
Netherlands, 23-25 November 1988. PUDOC, Wageningen, pp. 103-106.
Carr6, B., Escartin, R., Melcion, J.P., Champ, M., Roux, G. and Leclercq, B., 1987. Effect of
pelleting and associations with maize or wheat on the nutritive value of smooth pea (Pisum
sativum) seeds in adult cockerels. Br. Poult. Sci., 28:219-229.
Carr6, B., Beaufils, E. and Melcion, J.P., 1991. Evaluation of protein and starch digestibility
and energy value of peUeted or unpelleted pea seeds from winter or spring cultivars in adult
and young chickens. J. Agric. Food Chem., 39: 468-472.
Chang, K.C. and Satterlee, L.D., 1981. Isolation and characterization of the major protein from
Great Northern beans (Phaseolus vulgaris). J. Food Sci., 46:1368-1373.
Christison, G.I. and Parra de Solano, N.M., 1982. Utilization of protein from peas, harley, hut-
termilk powder and soyabean meal by early weaned pigs. Can. J. Anim. Sci., 62: 899-905.
Conan, L. and CarrY, B., 1989. Effect of autoclaving on metabolizable energy value of smooth
pea seed (Pisum sativum) in growing chicks. Anim. Feed Sci. Technol., 26: 337-345.
Conan, L., Barrier-Guillot, B., Widiez, J.L. and Lucbert, J., 1992. Effect ofgfinding and pellet-
ing on the nutritional value of smooth pea seed (Pisum sativum) in adult cockerel. In: Proc.
1st Eur. Conf. on Grain Legumes, Angers, France, 1-3 June, pp. 479-480.
Cristofaro, E., Mottu, F. and Wuhrmann, J.J., 1974. Involvement of the raffinose family of
oligosaccharides in flatulence. In: H.E. Sipple and K.W. McNutt (Editors), Sugars in Nutri-
tion. Academic Press, New York, pp. 313-336.
De Lange, C.F.M., Sauer, W.C., Mosenthin, R. and Souffrant, W.B., 1989a. The effect of feed-
342 F. Gatel/AnimalFeedScienceand Technology45 (1994)317-348
ing different protein-free diets on the recovery and amino acid composition of endogenous
protein collected from the distal ileum and feces in pigs. J. Anim. Sci., 67: 746-754.
De Lange, C.F.M., Sauer, W.C. and Souffrant, W., 1989b. The effect of protein status of the pig
on the recovery and amino acid composition of endogenous protein in digesta collected from
the distal ileum. J. Anim. Sci., 67: 755-762.
De Lumen, B.O., 1990. Molecular approaches to improving the nutritional and functional prop-
erties of plant seeds as food sources: developments and comments. J. Agric. Food Chem., 38:
1779-1788.
Deshpande, S.S. and Damodaran, S., 1989. Structure-digestibility relationship of legume 7S
proteins. J. Food Sci., 54:108-113.
Duc, G. and Lacassagne, L., 1990. S61ection pour la qualit6 chez la f6verole ( Viciafaba L.). In:
Symposium Qualit6 des C6r6ales, des Ol6agineux et des Prot6agineux Fran~ais pour l'Ali-
mentation Animale, Toulouse, 6 July, AGPM, CETIOM, ITCF, ONIDOL, UNIP, Paris, pp.
93-95.
Du6e, P.H., Bourdon, D., Guibault, L., Calmes, R. and Martin-Tanguy, J., 1979. Utilisation de
la feverole contenant ou non des tanins par le porc en croissance. Journ. Rech. Porc. Fr., 11:
277-283.
Evans, I.M. and Boulter, D., 1980. Crude protein and sulphur amino acid contents of some
commercial varieties of peas and beans. J. Sci. Food Agric., 31: 238-242.
Garrido, A., Cahrera, A., Gomez, A. and Guerrero, J.E., 1989. Relationship between tannin
content and "in vitro" nutritive value in seeds of 24 strains of Viciafaba L. In: J. Huisman,
A.F.B. van der Poel and I.E. Liener (Editors), Proc. 1st Int. Workshop on Antinutritional
Factors in Legume Seeds, Wageningen, Netherlands, 23-25 November 1988. PUDOC, Wag-
eningen, pp. 160-163.
Gatel, F., Fekete, J. and Grosjean, F., 1989. A note on the use of spring pea (Pisum sativum
hortense) in diets for weaned pigs. Anim. Prod., 49: 330-332.
Gatel, F., Jondreville, C., Buron, G., Peyronnet, C. and Grosjean, F., 1993. Effet de l'introduc-
tion de pois darts le r6gime sur les rejets azot6s du porc charcutier. Journ. Rech. Porc. Fr.,
25: 301-306.
Gdala, J., Buraczewska, L. and Grala, W., 1991. Factors influencing ileal and total digestibility
of pea protein and amino acids in pigs. In: Proc. 6th Int. Symp. on Protein Metabolism and
Nutrition, Vol. 2, Herning, Denmark, 9-14 June, pp. 240-242.
Goodlad, J.S. and Mathers, J.C., 1991. Digestion by pigs of non-starch polysaccharides in wheat
and raw peas (Pisum sativurn) fed in mixed diets. Br. J. Nutr., 65: 259-270.
Green, S., 1988. A note on amino acid digestibility measured in pigs with pre- or post-valve
ileo-rectal anastomoses, fed soya-bean, pea and meat meals. Anim. Prod., 47:317-320.
Greet, F. and Pusztai, A., 1985. Toxicity of kidney bean (Phaseolus vulgaris) in rats: changes
in intestinal permeability. Digestion, 32: 42-46.
Griftiths, D.W., 1979. The inhibition of digestive enzymes by extracts of field bean (Viciafaba).
J. Sci. Food Agric., 30: 458-462.
Griffiths, D.W., 1981. The polyphenolic content and enzyme inhibitory activity of testas from
bean (Viciafaba) and peas (Pisum spp.) varieties. J. Sci. Food Agric., 32: 797-804.
Griffiths, D.W., 1984. The trypsin and chymotrypsin inhibitor activities of various pea (Pisum
spp.) and field bean (Viciafaba) cultivars. J. Sci. Food Agric., 35:481-486.
Griffiths, D.W. and Moseley, G., 1980. The effect of diets containing field beans of high or low
polyphenolic content on the activity of digestive enzymes in the intestine of rats. J. Sci. Food
Agric., 31: 255-259.
Grosjean, F. and Gatel, F., 1989. Feeding value ofPisum sativum for pigs: influence of technol-
ogy, influence of genotype (trypsin inhibitor activity). In: J. Huisman, A.F.B. van der Poel
F. Gatel / Animal Feed Science and Technology45 (1994) 317-348 343
and I.E. Liener (Editors), Proc. 1st Int. Workshop on Antinutritional Factors in Legume
Seeds, Wageningen, Netherlands, 23-25 November 1988. PUDOC, Wageningen, pp. 239-
242.
Grosjean, F., Bourdon, D., Theillaud-Ricca, V., Castaing, J. and Beague, E., 1989. Comparaison
des pois d'hiver et de printemps clans des aliments pour pore charcutier pr~sent~s en farine
ou en granules. Journ. Rech. Pore. Fr., 21: 59-68.
Grosjean, F., Bourdon, D., Kiener, T., Castaing, J. and Gatel, F., 1991. Valeur alimentaire pour
les porcs des pois francais et import~s. Journ. Rech. Porc. Fr., 23: 53-60.
Grosjean, F., Bourdon, D., Isambert, P., Peyronnet, C. and Jondreville, C., 1992. Valeur ali-
mentaire pour le porc charcutier de produits de d~corticage du pois. Journ. Rech. Porc. Fr.,
24: 173-178.
Grosjean, F., M~tayer, J.P., Peyronnet, C. and Carrou~e, B., 1993. Variability of trypsin inhib-
iting activity of peas grown in France. Proc. 2nd Int. ANF Workshop, Wageningen, Nether-
lands, 1-3 December, in press.
Gu~guen, J. and Baniel, A., 1990. Perspectives d'am~lioration de la fraction proteique du pois
(Pisum sativum L. ). In: Symp. Qualit6 des CO'rales, des Olragineux et des Prot~agineux
Fran~ais pour l'Alimentation Animale, AGPM, CETIOM, ITCF, ONIDOL, UNIP, 6 July,
pp. 87-92.
Gurguen, J. and Barbot, J., 1988. Quantitative and qualitative variability of pea (Pisum sati-
rum L.) protein composition. J. Sci. Food Agric., 42: 209-224.
Guillaume, J., 1978. Digestibilit6 des protrines, de l'amidon et des lipides de deux types de
frveroles ( Viciafaba L. ) crue ou autoclavre chez le poussin. Arch. Gefliigelk., 42:179-182.
Hauschild, A. and K/Shier, R., 1991. Influence of dietary fibre on digestibility of protein and
organic matter of different pea genotypes in growing pigs. In: Proc. 6th Int. Symp. on Protein
Metabolism and Nutrition, Herning, Denmark, 9-14 June, pp. 21-23.
Heinz, T., Souffrant, W.B., Huisman, J. and Jansman, A.J.M., 1991. Apparent and true protein
digestibility of ANF-containing legume seeds measured by ~SN-technique. In: Proc. 42nd
Annual Meeting of the EAAP, Berlin, 8-12 September. Vol. 2, pp. 402-403.
Henry, Y., 1985. Principles of protein evaluation in pig feeding. World Rev. Anim. Prod., 21:
47-59.
Henry, Y. and Bourdon, D., 1973. Utilisation digestive de l'rnergie et des mati~res azotres de
la frverole sous forme enti~re ou drcortiqure en comparison avec le tourteau de soja. Journ.
Rech. Porc. Fr., 5: 105-114.
Hff$dversson, R., 1987a. Comparison of the nutritional value of dark and white flowered culti-
vars of pea for growing-finishing pigs. Swed. J. Agric. Res., 17:97-101.
H18dversson, R., 1987b. The nutritive value of white and dark flowered cultivars of pea for
growing-finishing pigs. Anim. Feed Sci. Technol., 17: 245-255.
Holt, N.W. and Sosulki, F.W., 1979. Amino acid composition and protein quality of field peas.
Can. J. Plant Sci., 59: 653-660.
Huet, J.C., Baudet, J. and Mossr, J., 1987. Constancy of composition of storage proteins depos-
ited in Pisum sativum seeds. Phytochemistry, 26: 47-50.
Huisman, J. and Jansman, A.J.M., 1991. Dietary effects and some analytical aspects of antinu-
tritional factors in peas (Pisum sativum ), common bean (Phaseolus vulgaris) and soyabeans
(Glycine max L. ) in monogastric farm animals. A literature review. Nutr. Abstr. Rev., Ser.
B., 61: 901-921.
Huisman, J. and le Guen, M.P., 1991. Effects of pea ANFs and pea carbohydrates on ileal pro-
tein digestibility of piglets. In: M.W.A. Verstegen, J. Huisman and L.A. den Hartog (Edi-
tors), Proc. 5th Int. Symp. on Digestive Physiology in Pigs, Wageningen, Netherlands, 24-
26 April. PUDOC, Wageningen, pp. 60-66.
Huisman, J., van der Poel, A.F.B., Verstegen, M.W.A. and van Weerden, E.J., 1990a. Antinu-
tritional factors (ANF) in pig production. World Rev. Anita. Prod., 25: 77-82.
Huisman, J., le Guen, M.P., Gueguen, J., Beelen, J.M. and van der Poel, A.F.B., 1990b. Diges-
344 F. Gatel/ AnimalFeedScienceand Technology45 (1994)317-348
tive response of piglets to isolated fractions from peas. 1. Apparent fecal and ileal digestibil-
ity of pea proteins in early weaned piglets: comparison of raw peas and protein isolate. Ph.D.
Thesis, Agricultural University of Wageningen, Netherlands, pp. 81-97.
Huisman, J., van der Poel, A.F.B. and Beynen, A.C., 1991. Animal species difference in anti-
nutritional effects of raw Phaseolus vulgaris beans and Pisum sativum: comparison of piglets,
rats, chickens and mice. In: M.W.A. Verstegen, J. Huisman and L.A. den Hartog (Editors),
Proc. 5th Int. Symp. on Digestive Physiology in Pigs, Wageningen, Netherlands, 24-26 April.
Huyghebaert, G., Fontaine, G. and de Groote, G., 1979. D6termination de la valeur alimentaire
des pois (Pisum sativum) et des f6veroles (Vicia faba) au moyen d'essais de digestibilit6
avec des coqs adultes. Rev. Agric., 32: 759-777.
INRA, 1989. L'Alimentation des Animaux monogastriques: Porc, Lapin, Volailles, 2nd revised
ed. INRA, Paris, 282 pp.
Ivan, M. and Bowland, J.P., 1976. Digestion of nutrients in the small intestine of pigs fed diets
containing raw and autoclaved faba beans. Can. J. Anim. Sci., 56:451-456.
Ivanko, S., Slesarova, L., Bystricky, P. and Chudy, D., 1991. Digestion of legume seed proteins
by enzymes of the gastrointestinal tract. In: Proc. 6th Int. Symp. on Protein Metabolism and
Nutrition, Herning, Denmark, 9-14 June, pp. 213-233.
Jansman, A.J.M., Huisman, J. and van der Poel, A.F.B., 1989. Faba beans with different tannin
contents: ileal and fecal digestibility in piglets and growth in chicks. In: J. Huisman, A.F.B.
van der Poel and I.E. Liener (Editors), Proc. 1st Int. Workshop on Antinutritional Factors
in Legume Seeds, Wageningen, Netherlands, 23-25 November 1988. PUDOC, Wageningen,
pp. 176-180.
Jansman, A.J.M., Huisman, J. and Verstegen, M.W.A., 1991. The effect of hulls of field beans
(Viciafaba L.) with different tannin contents on nutrient digestibility, growth and N bal-
ance of piglets. In: Proc. 6th Symp. on Protein Metabolism and Nutrition, Herning, Den-
mark, 9-14 June, pp. 216-221.
Jansman, A.J.M., Huisman, J. and Verstegen, M.W.A., 1992. The effect of condensed tannins
in faba bean hulls ( Viciafaba L. ) on the ileal digestibility in piglets of diets containing dif-
ferent protein sources. In: Proc. 1st Eur. Conf. on Grain Legumes, Angers, France, 1-3 June,
pp. 523-524.
Jondreville, C., Grosjean, F., Buron, G., Peyronnet, C. and Beneytout, J.L., 1992. Comparison
of four pea varieties in pig feeding through digestibility and growth performance results. J.
Anim. Physiol. Anim. Nutr., 68:113-122.
Kik, M.J.M., Huisman, J., van der Poel, A.F.B. and Mouwen, J.M.V.M., 1990. Pathologic changes
of the small intestinal mucosa of piglets after feeding of Phaseolus vulgaris beans. Vet. Pa-
thol., 27: 329-334.
K6hler, T., den Hartog, L.A., Huisman, J., Mosenthin, R. and Verstegen, M.W.A., 1993. Diges-
tibility measurements in pigs by using post-valve T-caecum cannulation or end-to-side ileo-
rectal anastomosis. J. Anim. Physiol. Anim. Nutr., 66:305-315.
Lacassagne, L., Francesch, M., Carr6, B. and Melcion, J.P., 1988. Utilization of tannin-contain-
ing and tannin-flee faba beans (Vicia faba) by young chicks: effects of pelleting feeds on
energy, protein and starch digestibility. Anim. Feed Sci. Technol., 20: 59-68.
Lacassagne, L., Melcion, J.P., de Monredon, F. and Carr6, B., 1991. The nutritional value of
faba bean flours varying in their mean particle size. Anim. Feed Sci. Technol., 34:11-19.
Lall6s, J.P., 1991. Nutritional and anti-nutritional aspects of soyabean and field pea protein
used in veal calf production: a review. Livest. Prod. Sci., 34:181-202.
Lattanzio, V., Bianco, V.V., Crivelli, G. and Miccolis, V., 1983. Variability of amino acids,
protein, vicine and convicine in Viciafaba (L.) cultivars. J. Food Sci., 48: 992-993.
Le Guen, M.P., Huisman, J. and Makkink, C.A., 1991 a. Effect of peas and pea isolates on pro-
tease activities in pancreatic tissue of piglets. In: M.W.A. Verstegen, J. Huisman and L.A.
F. Gatel/Animal FeedScienceand Technology45 (1994) 317-348 345
den Hartog (Editors), Proc. 5th Int. Symp. on Digestive Physiology in Pigs, Wageningen,
Netherlands, 24-26 April. PUDOC, Wageningen, pp. 207-210.
Le Guen, M.P., Tolman, G.H. and Huisman, J., 1991b. Antibodies formation against pea pro-
teins in piglets. In: M.W.A. Vcrstcgen, J. Huisman and L.A. den Hartog (Editors), Proc. 5th
Int. Symp. on Digestive Physiology in Pigs, Wagcningen, Netherlands, 24-26 April. PU-
DOC, Wageningcn, pp. 99-103.
Leterme, P., Bcckers, Y. and Thcwis, A., 1990a. Trypsin inhibitors in peas: varietal effect and
influence on digestibility of crude protein by growing pigs. Anim. Feed Sci. Tcchnol., 29: 45-
55.
Leterme, P., Beckcrs, Y., Thewis, A. and Baudart, E., 1990b. Apparent and ileal digestibility of
amino acids and nitrogen balance measured in pigs with ilco-rcctal anastomosis or T-can-
nulas, given a diet containing peas. J. Sci. Food Agric., 52: 485-497.
Liebcrt, F. and Gcbhardt, G., 1983. Results of a comparative nutritive test of horse beans of
various origins with fattening pigs in particular consideration of a white flowering new vari-
ety (in German). Arch. Tiercrnaehr., 33: 47-56.
Liencr, I.E., 1983. Removal by processing of naturally occurring toxicants and antinutrients.
In: L.W. Shemit (Editor), Chemistry and World Food Supplies: the New Frontiers. Perga-
mon, New York, pp. 453-463.
Liencr, I.E., 1989. Antinutritional factors. In: R.H. Matthews (Editor), Legumes: Chemistry,
Technology and Human Nutrition. Marcel Dekker, New York, pp. 339-382.
Longstaff, M. and McNab, J.M., 1991. The inhibitory effects of hull polysaccharides and tan-
nins of field beans ( Vicia faba L. ) on the digestion of amino acids, starch and lipid and on
digestive enzyme activities in young chicks. Br. J. Nutr., 65:199-216.
Lund, S., H[ikansson, J., 1986. Nutritional and growth studies with pea-crop meals and peas for
growing-finishing pigs. Anim. Feed. Sci. Tcchnol., 16:119-128.
Madsen, A. and Mortensen, H.P., 1985. Peas for bacon pigs (in Danish). Beret. Statens Hus-
dyrbrugsforseg, 581, 45 pp.
Maillard, R., Kiener, T. and Bertrand, S., 1990. Digestibilit~ r~elle, mesur~e au niveau ileal des
acides amines de la f~verole et du lupin. Journ. Rech. Pore. Fr., 22: 223-228.
Marlier, L., Focant, M., Allart, B. and Vanbelle, M., 1989. Effets du floconnage et de l'extrusion
sur la valeur alimentaire du pois prot~agineux pour le porc charcutier. Ann. Zootech., 38:
237-245.
Marquardt, R.R., 1989. Dietary effects of tannins, vicine and convicine. In: J. Huisman, A.F.B.
van der Poel and I.E. Liener (Editors), Proc. 1st Int. Workshop on Antinutritional Factors
in Legume Seeds, Wageningen, Netherlands, 23-25 November 1988. PUDOC, Wageningen,
pp. 141-155.
Marquardt, R.R. and Bell, J.M., 1988. Future potential of pulses for use in animal feeds. In:
R.J. Summerfield (Editor), World Crops: Cool Season Food Legumes. Kluwer Academic,
Dordrecht, pp. 421-444.
Marquardt, R.R. and Campbell, L.D., 1974. Deficiency of methionine in raw and autoclaved
faba beans in chick diets. Can. J. Anim. Sci., 54: 437-442.
Marquardt, R.R., Campbell, L.D., Stothers, S.C. and McKirdy, J.A., 1974. Growth responses
of chicks and rats fed diets containing four cultivars of raw or autoclaved faba beans. Can. J.
Anim. Sci., 54: 177-182.
Marquardt, R.R., McKirdy, J.A., Ward, T. and Campbell, L.D., 1975. Amino acid, hemagglu-
tinin and trypsin inhibitor levels, and proximate analyses of faba beans ( Vicia faba) and
faba bean fractions. Can. J. Anim. Sci., 55:421-429.
Marquardt, R.R., Campbell, L.D. and Ward, T., 1976. Studies with chicks on the growth de-
pressing factor(s) in faha beans ( Viciafaba L. var. minor). J. Nutr., 106: 275-284.
Martin-Tanguy, J., Guillaume, J. and Kossa, A., 1977. Condensed tannins in horse bean seeds:
chemical structure and apparent effects on poultry. J. Sci. Food Agric., 28: 757-765.
Matthews, P. and Arthur, E., 1985. Genetic and environmental components of variation in
346 F. Gatel/ Animal FeedScienceand Technology45 (1994) 317-348
protein content of peas. In: P.D. Hebblethwaite, M.C. Heath and T.C.K. Dawkins (Editors),
The Pea Crop. Butterworths, London, pp. 369-381.
McNab, J.M. and Wilson, B.J., 1974. Effects of micronizing on the utilization of field beans
( Viciafaba L. ) by the young chick. J. Sci. Food Agric., 25: 395-400.
M6tayer, J.P., Grosjean, F., Peyronnet, C. and Carrou6e, B., 1992. Composition of peas grown
in France for animal feeding: results of surveys. In: Proc. 1st Eur. Conf. on Grain Legumes,
Angers, France, 1-3 June, pp.447-448.
Moscnthin, R., Saner, W.C., Lien, K., de Lange, C.F.M. and Ahrens, F., 1991. Apparent and
real ileal amino acid digestibilities in white and dark coloured faha beans (Viciafaba). In:
Proc. 6th Int. Syrup. on Protein Metabolism and Nutrition, Herning, Denmark, 9-14 June,
pp. 219-221.
Mossd, J., 1990. Acides amin6s de 16 c6r6ales et proteagineux: variations et cl6s du calcul de la
composition en fonction du taux d'azote des grain (e)s. Cons6quences nutritionnelles. INRA
Prod. Anim., 3:103-119.
Moss6, J., Huet, J.C. and Baudet, J., 1987. Changement de la composition en acides aminds des
graines de pois en fonction de leur taux d'azote. Sci. Aliments, 7: 301-324.
Moughan, P.J. and Smith, W.C., 1985. Determination and assessment of apparent ileal amino
acid digestibility coefficients for the growing pig. NZ J. Agric. Res., 28: 365-370.
Nielsen, S.S., Deshpande, S.S., Hermodson, M.A. and Scott, M.P., 1988. Comparative digesti-
bility of legume storage proteins. J. Agric. Food Chem., 36: 896-902.
Nunes do Prado, I., Toullec, R., Lall~s, J.P., Hingand, L. and Gueguen, J., 1988. Anticorps
contre les protdines alimentaires et permdabilit6 intestinale aux macromol6cules chez le veau
pr6ruminant recevant de la farine de pois. Reprod. Nutr. Dev., 28 (Suppl. 1 ): 157-158.
Nunes do Prado, I., Toullec, R., Lall~s, J.P., Hingand, L., Gueguen, J. and Guilloteau, P., 1989.
Digestion des protdines de pois chez le veau pr6ruminant. 1. Taux circulants de nutriments,
formation d'anticorps et perm6ahilit6 intestinale aux macromoldcules. Reprod. Nutr. Dev.,
29: 413-424.
Nunes do Prado, I., Toullec, R., Guilloteau, P. and Gueguen, J., 1990. Digestion des prot6ines
de pois dans la caillette et l'intestin gr~le du veau pr6ruminant: rdsultats pr61iminaires. Re-
prod. Nutr. Dee., 30(Suppl. 2): 195s-196s.
Palisse-Roussel, M., Jacquot, L. and Maury, Y., 1984. Int~r~t de l'association pois de printemps
et tryptophane de synth~sc pour remplacer la totalit6 du tourteau de soja dans une formule
porc engraissement. Journ. Rech. Pore. Ft., 16: 383-392.
Pastuszewska, B., Dude, P.H., Henry, Y., Bourdon, D. and Jung, J., 1974. Utilisation de la
f6verole enti~re et d6cortiqu6e par le porc en croissance: digestibilit6 et disponibilit6 des
acides amines. Ann. Zootech., 23: 537-554.
P6rez, J.M., 1991. Int6r~t et limites des model,s de pr6vision de la valeur 6nerg6tique des ali-
ments destin6s au pore. Th~se de Doctorat, Universit6 des Sciences et Techniques du
Languedoc.
P6rez, J.M. and Bourdon, D., 1992. Energy and protein value of peas for pigs: synthesis of
French results. In: Proc. 1st Eur. Conf. on Grain Legumes, Angers, France, 1-3 June, pp.
489-490.
Pisulewski, P., Pisulewska, E., Hanczakowski, P. and Ernest, T., 1983. The chemical composi-
tion and nutritive value of pea (Pisum sativum L. ) and field pea (Pisum arvense L.) seeds.
Roez. Nauk Roln., Ser. B, 10: I l 1-116.
Pusztai, A., 1989. Biological effects of dietary lectins. In: J. Huisman, A.F.B. van der P o d and
I.E. Liener (Editors), Proc. 1st Int. Workshop on Antinutritional Factors in Legume Seeds,
Wageningen, Netherlands, 23-25 November 1988. PUDOC, Wageningen, pp. 17-29.
Qu6m6r6, P., 1990. Synth~se des essais franqais et 6trangers sur l'utilisation du pois prot6agi-
neux par les porcins (porcelets, pores charcutiers, truies). Journ. Rech. Pore. Fr., 22:133-
150.
F. Gatel/AnimalFeedScienceand Technology45 (1994)317-348 347
Reddy, I.M., KeUa, N.K.D. and Kinsella, J.E., 1988. Structural and conformational basis of the
resistance of b bactoglobulin to peptic and chymotryptic digestion. J. Agric. Food Chem.,
36: 737-741.
Reddy, S.J., McGinnis, J., Muehlbauer, F. and Campbell, A., 1979. Methionine content and
availability in varieties and breeding lines of peas for chicks. Poult. Sci., 58: 376-381.
Reichert, R.D. and McKenzie, S.L., 1982. Composition of peas (Pisum sativum) varying widely
in protein content. J. Agric. Food Chem., 30: 312-317.
Rh6ne Poulenc Animal Nutrition, 1989. Nutrition Guide, 1st edn. Rh6ne Poulenc, Commen-
try, 34 pp.
Romero, J. and Ryan, D.S., 1978. Susceptibility oftbe major storage protein of the bean, Phas-
eolus vulgaris L., to in vitro enzymatic hydrolysis. J. Agric. Food Chem., 26: 784-788.
Rubio, L.A. and Brenes, A., 1989. Effects of raw and autoclaved faba beans ( Viciafaba L.) and
faba beans fractions on the intestinal physiology and histological structure in chicks. In: J.
Huisman, A.F.B. van der Poel and I.E. Liener (Editors), Proc. 1st Int. Workshop on Anti-
nutritional Factors in Legume Seeds, Wageningen, Netherlands, 23-25 November 1988.
Saini, H.S., 1989. Legume seed oligosaccharides. In: J. Huisman, A.F.B. van tier Poel and I.E.
Liener (Editors), Proc. I st Int. Workshop on Antinutritional Factors in Legume Seeds, Wag-
eningen, Netherlands, 23-25 November 1988. PUDOC, Wageningen, pp. 329-341.
Sauer, W.C. and Ozimek, L., 1986. Digestibility of amino-acids in swine: results and their prac-
tical applications. A review. Livest. Prod. Sci., 15: 367-388.
Sauer, W.C., Jaikaran, S. and Lien, K., 1990. The nutritive value of peas for swine. In: Proc.
11th Western Nutrition Conf., Calgary, 13-14 September, pp. 19-25.
Savelkoul, F.H.M.G., Scbepers, J., Boer, H. and Tamminga, S., 1991. The in vitro protein di-
gestibility of germinated legumes. In: Proc. 41 st Annual Meeting of the EAAP, Toulouse, 9-
12 July. Vol. l, pp. 334-335.
Schroeder, H.E., 1982. Quantitative studies on the cotyledonary proteins in the genus Pisum. J.
Sci. Food Agric., 33: 623-633.
Semino, G.A., Restans, P. and Cerletti, P., 1985. Effect of bound carbohydrate on the action of
trypsin on lupin seed glycoproteins. J. Agric. Food Chem., 33: 196-199.
S~ve, B., Aumaitre, A. and Bouchez, P., 1985. Effet d'un traitement technologique sur la valeur
nutritionnelle du pois pour le jeune porcelet. Sci. Aliments, 5:119-126.
Sibbald, I.R., 1987. Estimation ofbioavailable amino acids in feedingstuffs for poultry and pigs:
a review with emphasis on balance experiments. Can. J. Anim. Sci., 67:221-301.
Sosulki, F.W. and Holt, N.W., 1980. Amino acid composition and nitrogen-to-protein factors
for grain legumes. Can. J. Plant Sci., 60:1327-1331.
Totsuka, K., Tajima, M., Saito, T. and Shoji, K., 1977. Studies on the energy and protein values
of faba beans for poultry rations. Jpn. Poult. Sci., 14:109-114.
Toullec, R., Lall~s, J.P. and Guilloteau, P., 1992. Influence du floconnage sur l'utilisation de la
farine de pois dans l'alimentation du veau de boucherie. In: Proc. 1st Eur. Conf. on Grain
Legumes, Angers, France, 1-3 June.
UNIP, 1993. Plantes riches en prot6ines---chiffres cl6s, 1991-1992, UNIP, 4 pp.
Valdebouze, P. and Gaborit, T., 1985. Activit6 antitrypsique des graines de 16gumineuses. Rev.
Alim. Anim., 392: 45-47.
Valdebouze, P., Bergeron, E., Gaborit, T. and Delort-Laval, J., 1980. Content and distribution
of trypsin inhibitors and hemagglutinins in some legume seeds. Can. J. Plant Sci., 60: 695-
701.
Van der Poel, A.F.B., 1990. Effect of processing on antinutritional factors and protein nutri-
tional value of dry beans (Phaseolus vulgaris L. ). A review. Anim. Feed Sci. Technol., 29:
179-208.
Van der Poel, A.F.B., Blonk, J., van Zuilicbem, D.J. and van Oort, M.G., 1990. Thermal inac-
348 F. Gatel / Animal FeedScienceand Technology45 (1994) 317-348
tivation of lectins and trypsin inhibitor activity during steam processing of dry beans (Phas-
eolus vulgaris) and effects on protein quality. J. Sci. Food Agric., 53:215-228.
Van der Poel, A.F.B., Gravendeel, S. and Boer, H., 1991a. Effect of different processing meth-
ods on tannin content and in vitro protein digestibility of faba bean ( V i c a f a b a L. ). Anim.
Feed Sci. Technol., 33: 49-58.
Van der Poel, A.F.B., Kemp, B., Wahle, E.R. and van Zuilichem, D.J., 199 lb. Pig ileal digesti-
bility associated with antinutritional factors and protein quality in Phaseolus beans and soy-
abeans. In: M.W.A. Verstegen, J. Huisman and L.A. den Hartog (Editors), Proc. 5th Int.
Symp. on Digestive Physiology in Pigs, Wageningen, Netherlands, 24-26 April. PUDOC,
Wageningen, pp. 50-54.
Van Dijk, J.E., Fledderus, A., Mouwen, J.M.V.M. and Holzhauer, C., 1988. Gastro-intestinal
food allergy and its role in large domestic animals. Vet. Res. Com., 12: 47-59.
Van Zuilichem, D.J. and van der Poel, A.F.B., 1989. Effect of HTST treatment o f P i s u m sati-
vum on the inactivation of antinutritional factors. In: J. Huisman, A.F.B. van der Poel and
I.E. Liener (Editors), Proc. 1st Int. Workshop on Antinutritional Factors in Legume Seeds,
Wageningen, Netherlands, 23-25 November 1988. PUDOC, Wageningen, pp. 263-267.
Wang, T.C. and Fuller, M.F., 1989. The optimal dietary amino acid pattern for growing pigs. 1.
Experiments by amino acid deletion. Br. J. Nutr., 62: 77-89.

Gatel 1994

Uploaded by

Copyright:

Available Formats

Gatel 1994

Uploaded by

Document Information

Original Title

Copyright

Available Formats

Share this document

Share or Embed Document

Sharing Options

Did you find this document useful?

Is this content inappropriate?

Copyright:

Available Formats

Gatel 1994

Uploaded by

Copyright:

Available Formats

Animal Feed Science and Technology, 45 (1994) 317-348 317

0377-8401/94/$07.00 © 1994 - Elsevier Science B.V. All rights reserved

Protein quality of legume seeds for non-ruminant

Smooth peas Field beans Sweet white lupin

Crude protein 255.8 303.4 410.3

Amino acid content

Smooth peas Field beans Sweet white lupin

ANF on protein availability will be discussed below. However, as some of

Reference I Cultivar Seed type S / W 2 N 3 T I U m g - I D M Haemagglutinating

a Brite, Rondo Smooth 2 - 0.58-0.84

Solara Smooth S 14 2.12_+ 0.29 -

la, Grifiiths ( 1984; method of Erlanger et al. ( 1961 ) ).

depends on initial level, temperature, heating time, particle size, moisture

Reference I Cultivar S / W 2 N3 TIU m g - i DM Haemagglutinating

a White flower 1.56

ta, Griffiths ( 1984; method of Erlanger et al. ( 1961 ) ).

failed to produce any reduction in haemagglutinating activity (Marquardt et

The availability of an amino acid is defined as the proportion of the amino

Faecal digestibility of crude protein

White-flowered field beans

Ileal digestibility of amino acids

Numerous experiments have been conducted, especially on peas for pigs

Methodological sources of variation

Reference Cultivar T/A ~ Cannula/anastomosis Lysine Methionine Cystine Threonine Tryptophan

Buraczewska et al. ( 1 9 8 9 ) Belinda T2 Cannula 0.850 0.790 0.680 0.840 0.770

~T, true; A, apparent.

sensitive in detecting differences in amino acid digestibilities between feed-

Between- or within-variety variability

Apparent digestibility coefficient Nitrogen Lysine Methionine Cystine Threonine

Spring peas 0.743 0.815 0.767 0.621 0.710

True digestibility coefficient Nitrogen Lysine Methionine Cystine Threonine

Spring peas 0.906 0.869 0.886 0.777 0.877

Role of antinutritional factors

Many studies have been undertaken to investigate the causes of variation

pigs, protein structure could also be a limiting factor to their digestibility in

Reference Animal Procedure Component High-tannin Low-tannin Dehulled

a Pig 1 Nitrogen 0.719 a 0.758 ab

Reference Legume Treatment Animal Criterion Effect/

a 25% Field beans Autoclaving Pigs 1 None

Reference Legume Treatment Animal Effect/

a 33 or 66% Autoclaving Chickens 0.760 vs. 0.704

Antigenicity of grain legume proteins

You might also like