2001 Kluwer Academic Publishers. Printed in the Netherlands. 59. Genetic diversity of wheat storage proteins and bread wheat quality. G. Branlard, M. Dardevet, ...
Euphytica 119: 59–67, 2001. © 2001 Kluwer Academic Publishers. Printed in the Netherlands.
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Genetic diversity of wheat storage proteins and bread wheat quality G. Branlard, M. Dardevet, R. Saccomano, F. Lagoutte & J. Gourdon INRA, Station d’Am´elioration des Plantes 63039 Clermont Ferrand, France
Key words: Bread wheat, gliadins, glutenin subunits
Abstract To understand the genetic and biochemical basis of the bread making quality of wheat varieties, a large experiment was carried out with a set of 162 hexaploid bread wheat varieties registered in the French or European Wheat Catalogue. This material was used to analyse their allelic composition at the twelve main storage protein loci. A large genetic and biochemical diversity of the gluten proteins was found. Several gliadin encoding loci exhibited the highest allelic diversity whereas the lowest diversity was found for Glu-A1 and Glu-D3 loci encoding some high molecular weight glutenin subunits (HMW-GS) and LMW-GS respectively. The varieties were grown in three experimental locations in France. Quality evaluation was carried out from material harvested in each location using seven technological tests: grain protein content (Prot), grain hardness (GH), Zeleny sedimentation test (Zel), Pelshenke test (Pel), water soluble pentosans (relative viscosity: Vr ), mixograph test (giving 11 parameters) and the alveograph test (dough strength W, tenacity P , extensibility L, swelling G, ratio P/L and the elasticity index Ie). Genetic and location effects as well as broad-sense heritability of each of the 22 technological parameters were calculated. GH, corresponding to the major Ha gene, Pel, and MtxW (mixograph parameter) had the highest heritability coefficients, alveograph parameters like W, P, the relative viscosity Vr and several mixograph parameters had medium heritability coefficients whereas Prot and L had the lowest. Variance analysis (using GLM procedure) allowed the effect of the allelic diversity of the storage proteins, on the genetic variations of each quality parameters, to be estimated. Glu-1 and Glu-3 loci had significant additive effects in the genetic variations of many parameters. Gliadin alleles encoded at Gli-1 and Gli-2 were also found to play significant effect on several quality parameters. The major part of the phenotypic variation of the different quality parameters like Zel, Pel, W or mixograph peak time MPT was explained with the GH and alleles encoded at Glu-1 and Glu-3. Allelic variants encoded at Glu3 and Gli-2 had similar contribution to the phenotypic variations of quality parameters and accounted for 4% up to 21% each.
Introduction Wheat storage proteins (WSP), namely gliadins and glutenins, are the main components of gluten, which is the main contributor to the rheological and breadmaking properties of wheat flour. Gluten proteins give dough its unique viscoelastic properties. Glutenin proteins are polymeric, with disulphide bonds linking the individual glutenin polypeptides, which are known as subunits. SDS Polyacrylamide Gel Electrophoresis (SDS-PAGE) and Size Exclusion High Performance Liquid Chromatography (SE-HPLC) have identified two distinct glutenin groups: High and Low Molecular Weight Glutenin Subunit (HMW-GS and LMW-GS
respectively). The subunits of these two groups differ in terms of amino acid composition, molecular weight; ie from 23 to 68 kDa for LMW-GS and from 77 to 160kDa for HMW-GS and in their structure (See Kasarda, 1999 for a review). A higher proportion of LMW-GS (3–4 times by weight) than HMW-GS is found. The gliadins are monomeric proteins, soluble in aqueous alcohol solutions with a molecular weight of around 30–60kDa. The α-, β-, and γ -gliadins have intra molecular disulfide bonds but some γ -gliadin types may be linked with glutenin subunits (Köhler et al., 1993) Most of the ω-gliadins, also called sulphurpoor prolamins (Shewry et al, 1986), do not contain disulphide bonds. Both glutenins and gliadins are syn-
60 thesised on the rough endoplasmic reticulum (RER), with a signal peptide that is removed as it directs the polypeptide into the endoplasmic reticulum (ER) lumen. The proteins are folded and disulphide bonded within the ER (Shewry, 1996). The amount of gliadins and glutenins in wheat flour (accounting for 35 to 45% dw each) is influenced by genotype and environmental growing conditions. Studies on the genetic determinism of wheat storage proteins have revealed that both gliadins and glutenins are heritated at several loci on each genome A, B and D. HMW-GS genes are located on the long arm of chromosomes 1A, 1B and 1D at loci Glu-A1, Glu-B1 and Glu-D1, respectively (Payne 1987). LMW-GS genes are located at Glu-A3, GluB3 and Glu-D3 loci on the short arms 1AS, 1BS and 1DS, respectively (Singh et al., 1988). Genes coding for ω- and many γ -gliadins are tightly clustered at three homoeologous loci named Gli-A1, Gli-B1 and Gli-D1, at the distal end of 1AS, 1BS and 1DS respectively. The Gli-1 loci are close to the LMW-GS coding Glu-3 loci (Singh et al., 1988; Pogna et al., 1990). Some ω-gliadins are also encoded by genes proximal to Gli-1 loci and named Gli-A4, Gli-A5 and Gli-B3 (Metakovsky et al., 1997a). The α-, β- and some γ gliadins are encoded by tightly clustered genes at a single locus on each of the short arms of the chromosomes of group 6, named Gli-A2, Gli-B2 and Gli-D2 respectively. For each HMW-GS and LMW-GS coding loci a high degree of polymorphism was revealed by SDS-PAGE for bread and durum wheat (Payne et al., 1983; Gupta et al., 1990a, 1990b; Branlard et al., 1989). The allelic polymorphism at each gliadin locus is higher than for glutenin loci (Metakovsky et al., 1998). Since the pioneer work of Sozinov et al. (1974) revealing the influence of some gliadin blocks on the sedimentation values of bread wheats, assessed using a modified Zeleny test, many teams have reported on the relationships between WSP and technological tests. Using the SDS sedimentation test, Payne et al. (1980) provided evidence of a strong association between the presence of alleles coding for HMW-GS and the technological value of bread wheat. Using a broad base wheat genetic collection, the influence of the diversity of HMW-GS and gliadins on the rheological properties of dough, such as strength , tenacity and extensibility was revealed (Branlard et al., 1985a, b). Many other studies have shown that allelic variations in HMWGS and LMW-GS are both associated with differences in the technological qualities of wheat flour (Payne, 1987; Autran et al., 1987; Gupta et al., 1989; Khelifi
et al., 1992; Nieto-Taladriz et al., 1994). As LMW-GS are present in a greater amount than HMW-GS, they have a pronounced effect on the viscoelastic properties of dough in both bread and durum wheat (Gupta et al., 1987, 1988, 1989; Boggini et al., 1989; Pogna et al., 1990; Metakovsky et al., 1990). It is generally accepted that glutenins are mainly responsible for viscoelastic properties. But gliadins are also important in conferring extensibility to dough. Some gliadin alleles were shown to be positively associated to dough extensibility and also to dough strength (Branlard et al., 1994b; Metakovsky et al., 1997b). The influence of the alleles encoded at the 6 gliadin loci and the 6 glutenin loci has never been simultaneously analysed from a wide genetic collection. Such an approach can allow the effects of gliadins and glutenins on technological parameters to be estimated. In this paper, we give the preliminary results on the estimated effects of both gliadin and glutenin alleles encoded at the 12 major loci on several parameters used in the quality evaluation of a large set of cultivars grown at three locations in France.
Materials and methods Plant material A wide bread wheat collection composed of 162 varieties registered in the French or European wheat Catalogues were grown in three locations in France in 1998. Each variety was tested on three lines at normal seed density, with classic nitrogen and mineral supply under full fungicide and herbicide protection. The experimental locations were at the INRA stations of Le Moulon (near Paris), Mons en Chaussée (Northern France) and Clermont Ferrand (Centre). Grain harvested in bulk, for each variety, was used for quality testing. WSP analyses Gliadin electrophoresis was performed on each cultivar by acid polyacrylamide gel electrophoresis (APAGE); their allelic composition has previously been reported (Metakovsky et al., 1998). The HMW-GS and LMW-GS were analysed using SDS-PAGE with a modified protocol based on Singh et al. (1991). The alleles found at the three HMW-GS loci and the three LMW-GS loci have been identified (Branlard et al., 2001).
61 Quality tests Grain hardness (GH) and grain protein content (Prot) were assessed using near infrared reflectance spectrometry (NIRS) from wholemeal grain, according to the AACC method 39–70A and with Kjeldahl calibration respectively. White flour protein content and moisture level were also measured by NIRS and used together with GH for calculating the amount of water to add for the mixograph test (Martinant at al., 1998). The Zeleny test was performed with two replicates of 3.2g of 55–60% extraction rate flour (Junior Brabender mill, screen of 200 microns). This modified Zeleny test (Branlard et al., 1991) gives a sedimentation value of higher heritability than the conventional Zeleny test (Zeleny, 1947). The Pelshenke test was carried out using 10g of wholemeal flour for determining the dough swelling time (Pelshenke, 1933). The 10 g mixograph was used to assess dough properties during mixing, according the approved method AACC 54–40A 1988. The mixograph curves were computed by Mixsmart software (Natl. Manufacturer, Lincoln, Nebraska, USA). Eleven parameters computed from the mixograph curve, as previously described (Martinant et al., 1998), were used. The Chopin alveoghraph test was used to assess dough strength (W), tenacity (P), extensibility (L) and dough swelling (G) as described by the AFNOR method V03-710. The ratio tenacity/extensibility (P/L) and the elasticity index (Ie) were also calculated from the alveograph curve. The curves and parameters were computed with Alveolink apparatus (Tripette & Renaud, 92396 Villeneuve la Garenne, France). The relative viscosity Vr of water soluble arabinoxylans was performed as described by Saulnier et al., 1995. The white flour (70% extraction rate) obtained for the alveograph test was also used for mixograph and arabinoxylans extraction. Statistical analysis The SAS statistical package was used for analysing data. The Varcomp procedure and general linear model (GLM procedure) were applied to estimate broadsense heritability H2 and the main effects attributed to protein loci, respectively. Prot and GH variates were transformed in classified variates with 5 levels each, named ProC and GHC respectively, which were used as covariates in the GLM procedure.
Results and discussion
Variation of the quality parameters The 162 varieties tested at three locations exhibited a large variation for each of the 22 quality parameters recorded. Grain Protein content (Prot) varied from 8.30% dw up to 17.6% dw. Grain hardness (GH) varied from very soft to very hard. The Zeleny (Zel) and Pelshenke (Pel) also revealed a large variation which is also confirmed by the alveograph and mixograph parameters (Table 1). For example, the average strength (W) was 176, which is a medium quality level, but the different samples varied from very bad (W = 20) to extra strong gluten wheat (W = 482). Mixograph peak time (MPT) comprised between 1.29 min up to 9.35 min and the weakening stability coefficient (WS) had values typical of very unstable wheat (WS = 14.10) up to very stable (WS = 0.10) for other varieties. All parameters except mixograph MTxW were highly significantly influenced by both varieties and locations. The width of the mixograph curve at 8 min of mixing, MTxW, was only significantly influenced by varieties. The explanatory part (R 2 ) of the variance analysis model, including locations and varieties effects, in the variation of each parameter, was generally very high and varied between R 2 = 0.662 (for ratio tenacity/extensibility) up to R 2 = 0.931 (for Pel). Using the varcomp procedure, the broad-sense heritability H2 indicated that many parameters were strongly influenced by genotypes. It was particularly the case for GH, Pel, Zel, and MtxW, but also for the relative viscosity of water extractable arabinoxylans (Vr), for dough strength W and several mixograph parameters: MPT, MRV, MRW and WS. As well as Prot, extensibility L, dough swelling G, the value of the midline curve one minute before peak and at peak time (MLV and MPV respectively), and the integrated value of the mixograph curve at 8 min (MtxI) had a low H2 coefficient, resulting from either strong location effects or interaction between genotypes and locations. The heritability coefficients reported here are not very different from those obtained with the same parameters but with other sets of cultivars, years and locations (Branlard et al., 1991; Martinant et al., 1999). As a result of the strong location effect, for 21 out of 22 parameters, the relationships between allelic variants of WSP and quality parameters were analysed separately for each location.
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Figure 1. Contribution of protein content class (Prot), grain hardness class (GH), HMW-GS, LMW-GS and gliadins encoded at Gli-2 loci in the phenotypic variation of six quality parameters. Prot: Protein content class; GH grain hardness class; ?: unexplained part
Contribution of Prot and GH to the variation of quality parameters Linear correlation calculated between quality parameters for each location have shown that some parameters were strongly influenced by Prot and GH. The mixograph test had the parameters that varied most with protein content, particularly for the width of the curve and value at midline peak (MPW and MPV
repectively). The parameters less influenced by Prot were Pel, dough tenacity P, MTxW and of course the relative viscosity of arabinoxylans (Vr). Zel, dough extensibility L, dough strength W and the weakening stability coefficient of the mixing curve WS had, in average over the three locations, 15% of their variations explained by the protein classes ProC, whereas MPW and MPT had 34% and 30% respectively. It is well known that grain hardness GH has a strong in-
63 Table 1. Value of mean, standard deviation, minimum, maximum value and heritability coefficient calculated on the 22 quality parameters Variable
Unit
Mean
Std Dev
Prot GH PEL ZEL Vr P L G W PSL
%dw – min ml – mm H2 O mm mm 10−4 J mm H2 O mm−1 % % % min % % % % % % % × min %
12.15 41.99 69.50 28.63 1.64 73.87 76.63 19.65 176.41 1.16
1.4 25.1 45.0 7.2 0.2 30.0 27.8 3.7 82.8 0.8
41.09 36.55 20.01 3.50 39.25 16.60 35.49 11.84 32.56 8.11 267.48 3.76
16.6 5.9 7.2 1.3 6.8 4.5 5.7 4.5 5.1 4.1 44.3 2.5
IE MLV MLW MPT MPV MPW MRV MRW MTxV MTxW MTxI WS
fluence on flour granulometry, starch damage, dough hydration for a given consistency and finally rheological properties. Because the alveograph test was performed at constant hydration, GH strongly influenced dough tenacity P (R 2 = 34%) and dough strength W (R2 = 27%). Whereas all the mixograph parameters were much less influenced by GH (R 2 < 7%), as a result of the dough hydration adapted to GH for mixograph (Martinant et al., 1998). Pel and Zel were much more influenced by GH (R 2 = 28% and 26% respectively) than by Prot. Both GHC and ProC were introduced into the variance analysis model, as cofactors, in order to estimate the part played by the different WSP loci in the explanation of the quality parameters. WSP loci involved in the phenotypic variations of quality parameters The collection of 162 bread wheat varieties tested was very diverse, as confirmed by the numerous alleles found at each WSP loci. The following number
Minimum
Maximum
Heritability
8.3 2.0 15.0 13.0 1.25 23.0 19.0 9.6 20.0 0.11
17.6 99.0 273.0 51.0 2.70 187.0 219.6 35.7 482.3 6.37
0.275 0.861 0.893 0.678 0.577 0.445 0.431 0.430 0.475 0.395
0.0 12.8 7.5 1.29 17.6 6.6 14.3 4.0 11.4 1.9 103.8 0.10
67.0 52.8 46.8 9.35 59.2 34.1 53.2 28.9 46.3 20.5 393.2 14.10
0.389 0.260 0.368 0.631 0.277 0.334 0.521 0.553 0.416 0.722 0.270 0.501
of alleles was identified: for HMW-GS Glu-A1 (3), Glu-B1 (6), Glu-D1 (4); for LMW-GS Glu-A3 (4), Glu-B3 (10), Glu-D3 (4); for ω- and γ -gliadins GliA1 (8), Gli-B1 (11), Gli-D1 (9); and for α- β- and some γ -gliadins Gli-A2 (16), Gli-B2 (20), and GliD2 (16). Due to the numerous alleles found and to the near random nature of the assortment of alleles in the limited varieties collection, many possible allelic combinations were missing. The GLM procedure was appropriate to test the loci effects in such an unbalanced design. HMW-GS. At least two loci encoding the HMWGS had a significant effect on the variation of 19 parameters (Prot, HG and Vr were excluded). The part of the phenotypic variation explained by the allelic variants encoded at the Glu-1 loci, in average over the three locations, varied from 5% (for P/L) up to 34% (for MPT). Glu-B1 and Glu-D1 frequently affected the values expressed by parameters. Alveograph parameters L and G, and mixograph parameters MLV and MRV and MTxI were not influenced by Glu-D1 but varied significantly with Glu-B1 alleles. When pos-
64 sible the allelic effects were compared and results are briefly reported in Table 2. LMW-GS. Glu-A3 and Glu-B3 had the more pronounced effect on the 19 quality parameters. Glu-D3 alleles had a significant effect (p = 0.95) for GH variation. Many other parameters did not vary with the four alleles of Glu-D3. The proportion of quality variation explained by Glu-A3 and Glu-B3 was generally lower than that of the HMW-GS loci except for L, G, P/L and Ie. The effects of LMW-GS loci were generally additive to those attributed to HMW-GS loci. The significant interactions observed between loci will not be detailed in the present report. The proportions attributed to the three HMW-GS loci and to the two LMW-GS loci in the phenotypic variation of six important quality parameters is given on Figure 1. Gliadins. The general linear model revealed significant effects of the Gli-1 loci. Among these Gli-B1 was generally the more important. The Gli-A1 loci had significant effects for Zel, P/L, and MTxI. Only two mixograph parameters, MPV and MPW, revealed the influences of the Gli-D1 alleles. Part of the variation explained by the Gli-1 loci was similar to that attributed to Glu-3 loci and consequently the effects respectively attributable to each of the two protein groups (ω-gliadins and LMW-GS) were not distinguished in this first approach. Several mixograph parameters, MLW, MPV, MPW and MRV, however, appeared better explained by the Gli-1 alleles than by those encoded at Glu-3. A more detailed comparison of the allelic effects attributable to the Gli-1 and Glu3 linked loci will be carried out on the genetic values calculated for each parameter. The Gli-2 loci were involved in the phenotypic values obtained using Pelshenke, alveograph and mixograph. The Gli-A2 was frequently associated to variations in parameters L, G and P/L and also the Gli-D2 to some mixograph parameters: MPT, MPV, MTxW and MtxI. For most of the parameters, the proportion of the quality variation explained by the gliadin alleles encoded at Gli-2 loci, was always lower than the part played by the alleles of the Gli-1 loci. The three Gli-2 loci had the lowest effect (R 2 = 8%) with Zel and the highest with MTxW (R2 = 21%), (Figure 1). The total contribution of the alleles encoded at Glu-1, Glu-3 and Gli-2 loci amounted to 33% (for dough tenacity) up to 60% for MPT. These amounts correspond to allelic effects, which are independent from the protein content and from the grain hardness. The total contribution obtained using a model involving ProC, GHC and Glu-1, Glu-3 and Gli-2 loci
was 56% for P/L up to 82% and 83% for Zel and Pel respectively. The respective influence played by GHC and ProC together with the glutenins and Gli-2 encoded gliadins in the total contribution can be very different from one parameter to another (Figure 1) The comparison of allelic effects is reported in Table 2 for dough strength W, dough extensibility L and the Zeleny test. The effects attributed to alleles encoding the HMW-GS have been reported many times. The favorable effect of the subunits 13–16 on L has already been reported (Branlard et al., 1985b). Because dough extensibility L is a component of W, it follows that subunits 13–16 are associated with dough strength. But most of the alleles having a positive effect on tenacity P are in fact positively associated to W, which is not the case for subunits 13–16. Gupta et al. (1990c, 1991, 1994) and Metakovsky et al. (1990) have ranked several alleles at the Glu-3 loci with respect to their effect on dough resistance and extensibility as measured by the Brabender extensograph. Although our plant material was different from Australian cultivars and the alveograph or mixograph were used instead of the extensograph, some alleles were ranked similarly. For Glu-A3 we confirmed that d>e. For Glu-B3 allele b was better than allele f and for tenacity P, a parameter which is close to Rmax of the extensograph, we also observed b>h = f = g. For Rmax the Australian group reported the allele i as better than allele b, here we had i>b for extensibility but not for P or W. Our comparison involved many alleles that were absent from those already reported for bread wheat. Because the SDS-PAGE was performed at constant acrylamide concentration alleles b’ and c’ have been identified at Glu-B3. Allele b’ appeared better than b for W, L and the Zeleny test. Allele l characterising the 1BL/1RL translocation had, as expected, a very bad effect. Because only a few parameters were significantly influenced by Glu-D3, the ranking e > b > a > c > d proposed by Australian groups was not confirmed in our experiment, where we had d ≥ b = a ≥ c. Several alleles encoding α-, β- and γ gliadins had similar ranking for W or L and the Zeleny test particularly for Gli-A2 t and p, Gli-B2 m and l and Gli-D2 m and n. The allele Gli-A2t was previously associated to dough strength (Metakovsky et al., 1997). The α-, β- and γ -gliadins are known to contain only intramolecular disulphide bonds, consequently the effects on W of the alleles encoding the α-, βand γ -gliadins could come either from quantitative effect-ie: the difference between alleles with respect
65 Table 2. Comparison of alleles effects for phenotypic values of dough strength, dough extensibility and Zeleny test (nsd: not significantly different) Locus
Strength
Extensibility
Zeleny
GluA1 GluB1
2∗ = 1 > null 17–18 ≥ 13–16 ≥ 7–9 = 7–8 ≥ 7 = 6–8 5–10 ≥ 3–12 = 2–12 ≥ 4–12 a=d=f≥e b’ ≥ d = c = c’ = b = g >i>f≥j a≥b=d=c t≥k=r=f=g=j≥l =b=p m >b ≥ r ≥ h = o = g ≥ ae = l = ac m=e≥a=h=v=gn =n
nsd 13-16 ≥ 7–8 = 7–9 = 17–18 ≥ 7 ≥ 6–8 nsd
2∗ = 1 > null 13–16 ≥ 17–18 ≥ 7–9 = 7–8 = 7 = 6–8 5–10 > 3–12 = 2–12 > 4–12
d=a=f≥e i ≥ b’ ≥ c = c’ = g > b =f=d>j nsd b=t≥k=g=l≥p= r=f=j ae ≥ m ≥ g = o = h = ac ≥ b = r = l nsd
d≥a≥f>e b’ = c’ = d = b = i = g = c > f>j nsd f≥t≥g=b=r=j=k≥l≥p p m ≥ b ≥ ae = h = g ≥ r = o = l = ac m>e=h=v=a=g=n
GluD1 GluA3 GluB3 GluD3 GliA2 GliB2 GliD2
to protein quantity, or from their own composition in allowing the whole gluten network to aggregate to a greater or lesser extent. The fact that several Gli-2 alleles had similar rankings for the Zeleny test and dough strength is in favour of the quantitative effect. But some structural differences may exist between gliadins encoded at Gli-2 loci and their possible role, as proteins linked more or less with glutenins through hydrogen bonding, is not opposed to the quantitative effect and should not be rejected out of hand as a hypothesis. The quality variation of dough strength is largely influenced by the molecular weight distribution of gluten polymers (Popineau et al., 1994; Mac Ritchie, 1999; Ewart, 1987). The gliadins are not independent from gluten polymers. They are completely integrated in the complex network forming the protein matrix overlapping more or less the starch granules. Proteins with sequences characteristic of gliadins have been detected in gluten polymers (Masci et al., 1993; Sreeramulu et al., 1997). Gliadin-type genes with an odd number of cyteine residues have been identified (D’Ovidio et al., 1995; Anderson et al., 1997) and some γ -gliadin types were reported linked through disulphide bonds to glutenin polymers (Keck et al., 1995). At least two Gli-D1 alleles were positively associated to dough strength (data not shown). The first (Gli-D1 null) was previously reported (Lafiandra et al., 1993; Branlard et al., 1994) and the second Gli-D1j could be related to D type low molecular weight glut-
enin subunits (Masci et al., 1993, 1999) but with a very positive effect as reported for Glu-B3 encoded glutenin related to ω-gliadins (Nieto-Taladriz et al., 1998). Many research programmes have been devoted to HMW-GS and LMW-GS and have demonstrated that the polymerisation of glutenins has a key role in the properties of gluten. Gliadins are also important in providing viscosity and gluten extensibility which is a component of dough strength. Although further research will be carried out, particularly on the genetic variance of each parameter used, our results have shown that gliadins may make a significant contribution to the quality variation of many parameters and that the genetic variability of gluten composition accounts for a proportion of the variation in quality tests. Protein content and grain hardness had a strong influence on many parameters and to a lesser extent the relative viscosity of pentosans (data not shown). As a consequence, improving wheat quality cannot be achieved without considering protein content, grain hardness and several glutenin and gliadin alleles. Taking into account all the different alleles and the numerous genetic combinations represents a considerable burden for geneticists. In the future, we should devote research to obtaining DNA chips containing the major wheat storage protein alleles, making breeding for quality improvement easier.
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