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Effects of different prolamin alleles on durum wheat quality properties
Journal of Cereal Science 41 (2005) 123–131 www.elsevier.com/locate/jnlabr/yjcrs
Effects of different prolamin alleles on durum wheat quality properties Ma del Carmen Martinez, Magdalena Ruiz1, Jose M. Carrillo* Unidad de Gene´tica, Departamento de Biotecnologı´a, Escuela Te´cnica Superior de Ingenieros Agro´nomos, Ciudad Universitaria, 28040 Madrid, Spain Received 28 May 2004; revised 16 September 2004; accepted 20 October 2004
Abstract The F4 progenies of four durum wheat crosses were used to determine the effects of different prolamin alleles on quality properties evaluated by the SDS sedimentation, mixograph, micro-alveograph and vitreousness tests and by protein content. Allelic compositions of the gliadins (Gli-B1 and Gli-2 loci) and the glutenins (Glu-1, Glu-3 and Glu-B2 loci) were determined. Alleles at the Glu-B3 locus showed a strong influence on quality measured by SDSS, mixograph and alveograph tests. Significant interactions between Glu-B3 and other glutenin loci were also detected. Prolamin composition explained more than 30% of the variation in SDSS, mixograph MT and alveograph W. The mixograph parameter BDR, and alveograph P and L parameters were the most erratic with between 8 and 76% of variation explained by prolamin composition. In general, no significant associations of prolamins with vitreousness or protein content were found. A significant correlation was detected between SDSS, MT and W. These results together with those from previous studies have important implications for wheat breeders since selection based on good alleles at Glu-B3 (a, c, j) together with favourable alleles at other loci such as Glu-A1 (subunit 1), Glu-A3 (a, c, d, h), Glu-B2 (a,b) and Gli-B1 (u-35) could improve durum wheat quality. q 2004 Published by Elsevier Ltd. Keywords: Durum wheat; Prolamins; Gluten strength; Pasta quality
1. Introduction The ability of durum wheat semolina to form an ideal dough for pasta processing rests mainly on the rheological characteristics of its gluten related to gluten elasticity or strength. In fact, manufacturers in the main pasta producing countries want semolina with strong gluten to give a highquality product. In this context, the knowledge of the genetics of quality properties of wheat has important implications for the breeder. This information can assist in choosing new durum wheat lines with favourable genetic combinations for improved quality.
Abbreviations: BDR, resistance to breakdown; H3, height at 3 min after the peak of the curve; L, extensibility; LMW, low molecular weight; MH, maximum peak height; Mr, relative molecular mass; MT, mixing development time; P, tenacity; Prot, protein content; SDSS, sodium dodecyl sulphate sedimentation; V, vitreousness; W, strength. * Corresponding author. Tel.: C34 91 336 5716; fax: C34 91 543 4879. E-mail address: [email protected] (J.M. Carrillo). 1 Current address: Instituto Nacional de Investigacio´n y Tecnologı´a Agraria y Alimentaria, Centro de Recursos Fitogeneticos, 28800 Alcala de Henares, Spain. 0733-5210/$ - see front matter q 2004 Published by Elsevier Ltd. doi:10.1016/j.jcs.2004.10.005
The viscoelasticity of cooked pasta is known to correlate with the quantity and specific composition of seed storage prolamin proteins (D’Egidio et al., 1990). A highly significant positive correlation between protein quantity and pasta cooking quality has been recognised (Autran and Galterio, 1989; Dexter and Matsuo, 1980). The genetic improvement of protein content has been particularly hampered, not only by strong environmental influences, but also by the fact that a negative correlation has been frequently found between grain yield and seed protein content in segregating populations in all cereals (Cox et al., 1985). Provided there is sufficient protein, pasta quality is likely to be acceptable, however, to ensure good pasta making quality, breeders need to aim for increased protein with an appropriate prolamin composition. The specific prolamin composition depends on the allelic variation of gliadin and glutenin proteins. Gliadins are monomeric proteins and can be subdivided into four groups termed: a, b, g and u according to their decreasing electrophoretic mobility in gels at acidic pH. Glutenins contain different polypeptide subunits, connected by intermolecular disulphide bonds; subdivided into low Mr and high Mr subunits
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according to their electrophoretic mobility in polyacrylamide gels. The genes encoding gliadin components are located on the short arm of chromosomes of the groups 1 (Gli-1 loci) and 6 (Gli-2 loci) of A and B genomes (Joppa et al., 1983). The genes coding for high Mr glutenin subunits are located on the long arm of chromosomes 1A and 1B at the Glu-1 loci, whereas low Mr glutenin subunits are located on the short arm of the same chromosomes at the Glu-3, tightly linked to Gli-1 loci (Singh and Shepherd, 1988), and at the locus Glu-B2 (Liu, 1995; Ruiz and Carrillo, 1993). Some early studies (Damidaux et al., 1978; Kosmolak et al., 1980) demonstrated the usefulness of gliadins g-45 and g-42, encoded at the Gli-B1 locus (Joppa et al., 1983), as markers of good and poor quality gluten, respectively. In further studies, Payne et al. (1984), Pogna et al. (1990) and Ruiz and Carrillo (1995a) found that low Mr glutenin subunits, encoded at the Glu-B3 locus, were responsible for the differences in quality. These early studies analysed only the effect of different low Mr patterns, especially of LMW-1 and LMW-2, linked to g-42 and g-45, respectively (Payne et al., 1984; Pogna et al., 1990). The analyses, however, were not precise since low Mr patterns are composed of different subunits encoded at different loci (Glu-A3, Glu-B3 and Glu-B2). Thus, the specific effects of each allelic variant at each locus could not be analysed. However, in later studies the influence of low Mr glutenins on quality and the separate effects of allelic variants at Glu-A3, Glu-B3 and Glu-B2 loci were reported (Brites and Carrillo, 2001; Carrillo et al., 2000; Martinez et al., 2004; Ruiz and Carrillo, 1995b, 1996; Vazquez et al., 1996). Other studies have identified desirable prolamin compositions for pasta making using the SDS-sedimentation test. Also more reliable information can be obtained by determining rheological properties with mixograph and alveograph tests, used industrially to evaluate semolina quality (D’Egidio et al., 1990; Kovacs et al., 1997). The aim of this work was to determine the effect of prolamin alleles on gluten quality, including recently identified new allelic variants (Martinez et al., 2004). The main quality properties studied were protein content, vitreousness and the rheological properties of the gluten.
the 1997–1998 season. All the F4 lines were selected for homozygous Glu-B3 alleles. 2.2. Electrophoretic analysis Prolamin extraction and electrophoretic analysis were as described (Martinez et al , 2004). The alleles for high Mr and low Mr glutenin subunits were named according to Payne and Lawrence (1983) and Nieto-Taladriz et al. (1997), respectively. The a-gliadin blocks were designated according to Pogna et al. (1990). 2.3. Quality evaluation The SDS-sedimentation (SDSS) test and protein content (Prot) were performed as described (Martinez et al., 2004). To assess mixing properties, whole wheat meal was sieved to a particle size of 125–315 mm and used in the 10-g mixograph (Finney and Shogren, 1972) with modification for a constant water absorption of 6.5 ml. The mixograph parameters estimated were: mixing development time (MT), maximum peak height (MH), height at 3 min after the peak of the curve (H3), and the difference in percentage between MH and H3 (resistance to breakdown, BDR). For F4 lines with sufficient grain (61 lines in crosses 1 and 36 in cross 2) the micro-alveograph (50 g) test was performed according to D’Egidio et al. (1990) and Boggini (1991). A sample of grain (200 g) was tempered to 17.5% moisture and milled in a Chopin CD2 mill. The semolina was sieved to obtain a particle size of 125–315 mm. The saline solution added was calculated according to the formula 0.2![190.7K(semolina moisture!4.375)]. Dough was mixed for 4 min, rested for 18 min and mixed again for 4 min. Gluten strength (W), tenacity (P) and extensibility (L) were measured. These measurements were compared with those obtained with a full size alveograph with samples of 16 durum wheat varieties. The correlations between both methods were highly significant and higher than 0.9 for W and P, and higher than 0.7 for L. Vitreousness content (V) was estimated for 200 kernels by determining visual percentage of grains not showing yellowberry according to standard methods (ISO, 1994). Two replicate analyses were made for every line and test, except for the alveograph tests.
2. Experimental 2.4. Analysis of data 2.1. Plant material Seven durum wheat varieties with contrasting prolamin allelic variants were used to make the following crosses: Anto´n (A)!Blancal de Nules (BN), Senatore Capelli (S)! Fanfarron (F), Alcala la Real (AR)!Bidi-17 (B) and Bidi17 (B)!Atalaya (AT). Between 65 and 166 F2 seeds from each cross were analysed for prolamin composition. A total of 150 F2 derived F4 lines from cross 1, 70 from cross 2, 116 from cross 3 and 45 from cross 4 were sown in a randomised complete-block design with two replications in
Analysis of variance (SAS Institute, Cary, NC) was used to study the effects of the prolamin loci on mean values of technological parameters. For each cross and parameter the effects of the blocks and loci were analysed using the general lineal model (GLM) procedure. Allelic variation at each locus was considered as source of variation and lines with the same prolamin phenotype as replications. Differences between means were compared by Duncan’s test at PZ0.05. Relationships between quality tests were examined by Pearson correlation coefficients.
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Table 1 Allelic variants of prolamins and results of quality tests in parents Locus
Anto´n
Blancal de Nules
Senatore Capelli
Fanfarro´n
Alcala´ la Real
Bidi-17
Atalaya
Glu-A1 Glu-B1 Glu-A3 Glu-B3 Glu-B2 Gli-B1 Gli-A2 Gli-B2 Quality test SDSS (mm) MT (s) MH (mm) H3 (mm) BDR (%) W (10K4 J) P (mm H2O) L (mm) V (%) Prot (%)
Null 7C8 5/b 8C9C13C16/b 12/a u 33-35-38 g 42 a 70.5C71.5 b-64
1 6C8 6/a 1C3C13*C16/l Null/b u-39 g46 a 73 b-57
Null 20xC20y 6/a 2C4C15C19/a 12/a u-35 g-45
Null 6C8 5C20/i 8C9C13C16/b Null/b u 33-35-38 g-42
Null 6C8 6/a 2C4C15C19/a 12*/c g 45
Null 20xC20y 6/a 2C4C15C19/a 12/a u-35 g 45
Null 32C33 11/e 8C9C13C16/b Null/b u 33-35-38 g 42
30.0 110.0 92.5 72.2 21.8 94.2 73.3 51.0 98.7 17.1
37.5 87.5 94.5 65.0 30.9 82.6 69.1 49.6 99.2 18.4
37.2 97.5 98.5 80.5 18.3 156.8 97.8 64.8 99.5 17.5
27.7 61.2 78.2 49.0 37.5 44.6 46.7 30.6 99.0 16.8
52.0 101.2 92.5 72.0 22.1
35.4 116.9 102.6 78.4 24.2
25.7 61.2 78.5 49.8 36.5
99.2 18.5
99.0 19.6
99.0 15.5
3. Results and discussion The prolamin differences in F4 lines from the four crosses analysed were at the Glu-1, Glu-B2, Glu-3, Gli-B1 and Gli-2 loci. The allelic variants of prolamins and the results of the quality tests for the parents are shown in
Table 1. The inheritance of these prolamin genes has been determined in previously (Joppa et al., 1983; Martinez et al., 2004; Nieto-Taladriz et al., 1997; Ruiz and Carrillo, 1993). The high Mr and low Mr glutenin subunits and the gliadin variants studied are shown in Figs. 1 and 2, respectively. Due to subunit overlapping the effects of
Fig. 1. SDS-PAGE fractionation of high Mr and low Mr glutenin subunits in the cultivars Anto´n (A), Blancal de Nules (BN), Senatore Capelli (S), Fanfarron (F), Bidi-17 (B), Alcala la Real (AR), Bidi-17 (B) and Atalaya (A). The subunits studied are numbered.
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Fig. 2. A-PAGE fractionation of gliadins in the cultivars Anto´n (A), Blancal de Nules (BN), Bidi-17 (B) and Alcala la Real (AR). The cultivar Langdon (L) is included as reference. The gliadins studied are numbered.
some alleles (Glu-A3 in cross 1 and Glu-B2 in cross 4) could not be studied. For Glu-B3, all lines analysed were homozygous, so intrallelic interactions for this locus were avoided. 3.1. Effects of high Mr glutenin alleles on gluten quality The results of quality tests for the allelic variants of prolamins analysed in the four crosses are shown in Table 2 (SDSS and mixograph tests) and Table 3 (alveograph test). The effects of high Mr glutenins at Glu-A1 were studied in cross 1 (Table 1 and Fig. 1). Lines with the high Mr subunit 1 had significantly higher values of SDSS and mixograph parameters than lines with the Null subunit (Table 2). However, the presence or absence of subunit 1 did not result
in any significant difference in alveograph properties (Table 3). No significant interaction between Glu-A1 and other loci was found, in agreement with Brites and Carrillo (2001) and Ruiz and Carrillo (1995b). The influence of the high Mr subunit 1 on quality has not often been studied since most durum wheats possess the Null subunit at Glu-A1. Brites and Carrillo (2001), Ciaffi et al. (1991) and Turchetta et al. (1995) observed positive effects of subunit 1 on SDSS which agrees with the results obtained in the present work. Ruiz and Carrillo (1995b) showed the superiority of subunit 1 in improving MT, but not in SDSS. Conversely, Brites and Carrillo (2001) did not find any significant contribution to mixograph properties, but the L of alveograph was correlated positively with presence of subunit 1. All these results indicate a positive effect of the high Mr subunit 1 on gluten quality although the gluten parameter involved can be different depending on the material analysed. The high Mr subunits at Glu-B1 were studied in the four crosses (Table 1 and Fig. 1). All the Glu-B1 alleles compared showed significant differences in SDSS. The subunits 6C8 were associated with higher SDSS values than 7C8 (cross 1) and 20xC20y subunits (crosses 2 and 3). The 20xC20y also had lower values than 32C33 subunits (cross 4). Different effects of Glu-B1 alleles on mixograph parameters were obtained depending on the allele and the parameter considered. The subunits 6C8 had longer MT (crosses 2 and 3) and H3 and BDR (cross 3) than subunits 20xC20y which indicates stronger dough. For BDR, lower values are better. In cross 1, 7C8 subunits were associated with higher MH than 6C8. None of the Glu-B1 alleles had a significant effect on alveograph parameters either in cross 1 or 2 (Table 3). These results indicated that the differences between subunits 6C8 and 7C8 were small, whereas the 20xC20y subunits had a clear negative influence on gluten quality. Brites and Carrillo (2001) also demonstrated the inferiority of 20xC20y subunits relative to 6C8 for SDSS, mixograph properties and W of the alveograph. This last influence was not observed in the present work. The negative contribution of 20xC20y to some quality properties, mainly to SDSS has been previously observed (Kovacs et al., 1997; Ruiz and Carrillo, 1995b; Turchetta et al., 1995). Significant interactions between Glu-B1 and Glu-B3 or Glu-A3 were detected in cross 2. Thus, 6C8 subunits were associated with better values of SDSS and MT than 20xC20y when the best allele Glu-A3a was present, and with better values for SDSS in the presence of the best allele Glu-B3a. In contrast, no significant differences between subunits 6C8 and 20xC20y were found when the worst alleles Glu-A3i or Glu-B3b were present. On the other hand, Brites and Carrillo (2001) did not find interactions between Glu-B3 and Glu-B1 alleles probably because the alleles analysed were different from those studied in the present work. Although the same Glu-B1 alleles were compared in crosses 2 and 3 more significant differences were obtained in cross 3. In this cross, both parents had the same Glu-B3
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Table 2 Means values of the quality tests SDSS and mixograph values for the F4 lines grouped according to prolamin composition Locus
Cross
Prolamins/alleles alleles
Lines
SDSS (mm)
MT (s)
MH (mm)
H3 (mm)
BDR (%)
Glu-A1
1
Glu-B1
1
Null 1 7C8 6C8 20xC20y 6C8 6C8 20xC20y 20xC20y 32C33 6/a 6C5C20/aCi 6/a 11/e 8C9C13C16/b 1C3C13*C16/l 2C4C15C19/a 8C9C13C16/b 2C4C15C19/a 8C9C13C16/b 12/a Null/b 12/a Null/b 12*/c 12/a g-45 u-35 g-45 a-70.5C71.5 a-73 b-64 b-57
40 110 48 32 16 22 32 32 6 5 21 43 27 18 90 58 39 31 22 23 108 42 58 12 19 34 29 87 30 42 48 36
30.5b 35.7a 32.5b 36.9a 24.4b 37.5a 65.8a 30.9b 29.7b 50.1a 39.7aa 32.0ba 36.8a 31.7a 36.4aa 30.6ba 43.0aa 25.6ba 46.1a 23.5b 35.9a 30.0a 36.5a 29.9a 40.2ba 51.2aa 42.0ba 49.8aa 34.5a 32.0a 33.8a 32.7a
80.4b 92.1a 90.9a 87.3a 63.9b 83.5a 134.9a 105.9b 72.5a 101.7a 94.7a 75.1b 79.3a 73.6a 91.3a 85.1b 99.8a 59.5b 103.0a 53.9b 91.2a 83.2b 85.2a 66.6a 103.5b 125.5a 106.5b 122.4a 91.0a 88.1a 85.8a 88.6a
87.7b 91.1a 91.6a 89.6b 84.8a 86.5a 99.0a 101.3a 86.0a 92.0a 89.8a 85.8b 84.2a 84.2a 90.5a 89.7a 91.1a 82.8b 90.4a 78.5b 90.5a 89.3a 87.8a 85.1a 100.1a 101.3a 99.8a 100.2a 91.0a 90.9a 89.9a 90.7a
63.3b 66.9a 67.4a 65.4a 56.6a 60.5a 78.4a 72.8b 63.0a 71.7a 63.7a 60.2a 62.3a 61.0a 66.3a 65.4a 67.5a 54.5b 69.5a 55.0b 66.3a 65.0a 62.7a 56.7a 71.7b 77.3a 71.9b 76.4a 66.2a 66.3a 65.9a 65.2a
26.5b 27.9a 26.5a 27.0a 33.6a 30.2a 20.8b 28.3a 26.9a 22.1a 29.1a 30.1a 26.4a 27.4a 26.7a 27.0a 26.0b 34.1a 23.1b 29.9a 26.7a 27.1a 28.8a 33.1a 28.2a 23.7b 28.0a 23.8b 27.3a 27.0a 26.7a 28.1a
2 3 4 Glu-A3
2 4
Glu-B3
1 2 4
Glu-B2
1 2 3
Gli-B1
3
Gli-A2
1
Gli-B2
1
Means followed by different letters are significantly different at PZ0.05. a Martinez et al. (2004).
alleles, so the influence of Glu-B1 was probably better evaluated in this cross. Controversial results have been found with respect to influence of Glu-B1 on quality. Ciaffi et al. (1991) and Vazquez et al. (1996) no influence of Glu-B1 on quality, whereas Porceddu et al. (1998) and Tuchetta et al. (1995) found that Glu-B1 explained 8% of the variation of the SDSS test. These contrasting results could be due to the different magnitude of the influence of Glu-B1 alleles depending on which Glu-B3 alleles were present. In this work, the greatest influence of Glu-B1 was detected when the difference due to the Glu-B3 effect was removed (cross 3). 3.2. Effects of low Mr glutenin alleles on gluten quality The effects on quality of the low Mr subunits coded at Glu-A3, Glu-B3 and Glu-B2 were analysed (Table 1 and Fig. 1). The SDSS data obtained earlier (Martinez et al., 2004) for some low Mr glutenin alleles have been included in Table 2 for the comparison. The Glu-A3 alleles were studied in crosses 2 and 4 (a vs aCi and a vs e,
respectively). The Glu-A3a is frequently present in durum wheat cultivars, nevertheless alleles i and e are rare (NietoTaladriz et al., 1997; Martinez et al., 2004). Table 2 shows that allele a was associated with higher values of SDSS, MT and MH than allele i. No significant differences were observed between the two alleles in the alveograph test (Table 3). In cross 4, the presence of allele a or e did not result in any differences in the quality properties analysed (Table 2). In this cross a significant interaction was detected with the Glu-B3 alleles for SDSS. Glu-A3a was significantly better than Glu-A3e in the presence of the best allele Glu-B3a, whereas Glu-A3a and Glu-A3e were not significantly different when the Glu-B3b was present. These results indicate that the effect of the allele Glu-A3a on quality was dependent on which allele was present at Glu-B3. Ruiz and Carrillo (1995b) observed a similar interaction for Glu-A3b and d for MT and H3 mixograph parameters. Comparing Glu-A3 effects, Carrillo et al. (2000) found a superiority of allele a relative to e for SDSS and mixograph parameters. This superiority was smaller for alveograph parameters. Ruiz and Carrillo (1995b) found
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Table 3 Mean values of the alveograph test for the F4 lines grouped according to prolamin composition Locus
Cross
Prolamins/alleles
Lines
W (10K4 J)
P (mm H2O)
L (mm)
Glu-A1
1
Glu-B1
1
Null 1 7C8 6C8 20C20Y 6C8 6/a 6C5C20/aCi 8C9C13C16/b 1C3C13*C16/l 2C4C15C19/a 8C9C13C16/b 12/a Null/b 12/a Null/b a-70.5C71.5 a-73 b-64 b-57
16 45 17 15 5 2 5 12
68.8a 73.8a 76.1a 66.7a 58.5a 56.4a 82.3a 65.7a 78.0a 62.8b 98.7a 39.5b 76.6a 60.2a 78.2a 45.4a 64.5a 73.2a 66.8a 64.9a
61.0a 60.9a 62.9a 58.2a 58.6a 52.5a 68.5a 60.8a 61.7a 59.6a 74.2a 50.9b 61.7a 58.5a 66.5a 50.5a 58.6a 62.3a 61.1a 55.7a
42.5a 47.2a 49.2a 41.6a 38.0a 44.4a 45.9a 38.5a 49.4a 39.8b 48.4a 31.4b 48.5a 38.0a 42.1a 36.0a 42.7a 46.1a 41.4a 45.3a
2 Glu-A3
2
Glu-B3
1 2
Glu-B2
1 2
Gli-A2
1
Gli-B2
1
39 22 10 7 46 15 15 2 13 16 19 15
Means followed by different letters in bold are significantly different at PZ0.05.
a negative contribution of allele e to MT and H3 compared with allele b. The negative effect of Glu-A3i on quality supports a previous result for SDSS (Martinez et al., 2004), but this is the first time that its effect on mixograph and alveograph properties have been determined. These results, together with previous results (Brites and Carrillo, 2001; Carrillo et al., 2000) indicate that Glu-A3 alleles a, c, d and h are preferable to b, e, f, g, i and j (subunits 4C6*C15C19) for quality selection. For the Glu-B3, the alleles compared were b vs l in cross 1 and b vs a in crosses 2 and 4 (Table 1 and Fig. 1). The allele a should better positive effects than b for all the gluten quality properties analysed, and b was better than l for SDSS, MT, W and L (Tables 2 and 3). The high number of significant differences obtained for this locus in several quality tests confirms that Glu-B3 alleles have a much greater effect on gluten quality than alleles at other loci (Brites and Carrillo, 2001; Liu, 1995; Ruiz and Carrillo, 1995b). The smaller differential effects on gluten quality obtained in cross 1 between the parents and the alleles compared (b vs l) could be due to the higher similarity of both protein patterns and to the absence of the subunit 2 (Fig. 1) representative of the LMW-2 pattern (Nieto-Taladriz et al., 1997) and associated with high quality. This is the first time that the allele l has been analysed for mixograph and alveograph characteristics. The ranking for Glu-B3 alleles for the different quality properties, a[bOl, is in agreement with that obtained for the SDSS test (Martinez et al., 2004) and confirms the superiority of allele a, frequently present in durum wheat cultivars, in the mixograph and alveograph tests (Brites and Carrillo, 2001; Carrillo et al., 2000; Ruiz and Carrillo, 1995b). These results together with
those of Brites and Carrillo (2001) and Carrillo et al. (2000) indicate that Glu-B3 alleles a, c and j are related to the highest values for gluten quality, while the alleles b, e, i, k and l are related to the lowest. For the Glu-B2 locus, the alleles compared were a (low Mr subunit 12) vs b (Null) in crosses 1 and 2, and a vs c (low Mr subunit 12*) in cross 3 (Table 1 and Fig. 1). No significant differences were detected between alleles a and b except for MT in cross 1 (Tables 2 and 3). In the other comparison (cross 3), where most of the low Mr subunits were identical, allele a was associated with better gluten quality than allele c for almost all properties analysed (Table 2). These results confirm the small, yet significant differences in quality between alleles a and b (Brites and Carrillo, 2001; Ruiz and Carrillo, 1996) and the low SDSS values associated with allele c (Martinez et al., 2004). The influence of allele c on mixograph and alveograph tests was analysed first time and shown to have a negative effect on gluten quality. 3.3. Effects of gliadin alleles on gluten quality The influence on quality of u-35 encoded at Gli-B1 was analysed in cross 3 (Table 1 and Fig. 2). A positive effect of this gliadin on SDSS, MT, H3 and BDR was shown (Table 2). An interalelic interaction was observed with Glu-B1 for SDSS. The presence of the u-35 increased the positive effect of subunits 6C8 and the negative effect of subunits 20xC20y. Pogna et al. (1990) also detected positive effects of gliadins at Gli-B1 on gluten quality, these effects being smaller than those of Glu-B3 alleles. Autran and Galterio (1989) did not find a significant
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Table 4 Percentage of variation of the quality tests explained by the prolamins studied Cross
SDSS (mm) a
1 2 3 4
52 70a 52a 79
MT (s)
MH (mm)
H3 (mm)
BDR (%)
W (10K4 J)
P (mm H2O)
L (mm)
34 79 48 67
21 62 0 58
24 69 18 74
18 62 35 76
35 83
8 67
14 70
All the values are significant at PZ0.05, except the 8 and zero values. a Martinez et al. (2004).
correlation between SDSS and u-35 in a group of different durum wheat varieties. However, the separate effect of u gliadins on quality is not easy to evaluate because these prolamins are inherited together with other gliadins and low Mr glutenins encoded at Gli-B1 and Glu-B3, respectively. Thus, the effects attributed to u gliadin could be due to the presence of these associated proteins. In the present work, this problem did not exist because both parents had the gliadin g-45 at Gli-B1 (Fig. 2) and the allele Glu-B3a (Table 1 and Fig. 1). Thus, the positive effects detected seem to be specifically due to the u-35. The effects of the alleles at Gli-A2 and Gli-B2 were studied in cross 1. No significant differences were observed between Gli-A2 and Gli-B2 alleles for any of the quality tests (Tables 2 and 3). These results confirm previous
reports (Pogna et al., 1990; Ruiz and Carrillo, 1995b). However, Autran and Galterio (1989) found significant effects of Gli-A2 and Gli-B2 alleles on gluten firmness. In general, the prolamins studied showed no significant associations with vitreousness (V) or protein (Prot) contents. The F-tests of ANOVA were significant (PZ0.05) only for V between Glu-A3 alleles in cross 2. For Prot no significant correlation was detected except that reported by Martinez et al. (2004) between Glu-B3 and Gli-B1 alleles in crosses 2 and 3, respectively. Brites and Carrillo (2001) and Ruiz and Carrillo (1995b) detected no influence of prolamin composition on V or Prot values. The results of the four crosses can be grouped based on the influence of prolamin in the quality tests (Table 4). In crosses 2 and 4 a substantial proportion, 62–83 and 58–79%,
Table 5 Correlation coefficients between quality parameters in the crosses analysed
SDSS (mm)
MT (s)
MH (mm)
H3 (mm)
BDR (%)
W (10K4 J) P (mm H2O) L (mm) Prot (%)
Cross
MT (s)
MH (mm)
H3 (mm)
BDR (%)
W (10K4 J)
P (mm H2O)
1 2 3 4 1 2 3 4 1 2 3 4 1 2 3 4 1 2 3 4 1 2 1 2 1 2 1 2 3 4
0.47** 0.84** 0.66** 0.83**
0.24** 0.61** K0.07 0.78** 0.61** 0.76** 0.32** 0.88**
0.23** 0.79** 0.54** 0.84** 0.51** 0.87** 0.74** 0.94** 0.73** 0.88** 0.49** 0.95**
K0.09 K0.80** K0.65** K0.76** K0.11 K0.82** K0.67*** K0.86** K0.03 K0.67** 0.01 K0.68** K0.70** K0.94** K0.86** K0.87**
0.48** 0.87**
0.16 0.82**
0.37** 0.66**
0.56** 0.90**
0.34** 0.85**
0.42** 0.79**
0.35** 0.85**
0.18 0.91**
0.40** 0.72**
0.45** 0.95**
0.35** 0.93**
0.33** 0.87**
K0.35** K0.92**
K0.36** K0.85**
K0.11 K0.90**
0.80** 0.95**
0.64** 0.87** 0.23 0.77**
* And ** significant at the 5 and 1% level, respectively.
L (mm)
Prot (%)
V (%)
K0.00 K0.11 K0.09 K0.12 0.28** K0.13 0.12 K0.11 0.59** 0.14 0.56** 0.18 0.22** K0.02 0.14 K0.05 0.28** 0.16 0.16 0.41* 0.03 K0.24 K0.01 K0.19 0.03 K0.25
0.02 K0.10 0.10 0.17 0.17* K0.10 K0.14 0.12 K0.31** K0.11 0.06 0.09 K0.13 K0.14 K0.16 0.07 K0.14 0.15 0.22* K0.01 0.06 K0.37 0.09 K0.35 K0.02 K0.22 0.40** 0.12 0.09 0.32
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respectively, of the variation in the quality tests was explained in terms of prolamin composition. In crosses 1 and 3, this proportion was 8–52 and 0–52%, respectively. The value of zero corresponds to the parameter MH in cross 3, where no influence of prolamins on this parameter was detected. Taking into account that low Mr glutenins encoded at Glu-B3 show the most significant effects on quality, the low variation explained by prolamins in crosses 1 and 3 could be due to the similar effect on quality parameters of Glu-B3 glutenins in these two crosses. In fact, the Glu-B3 made the largest positive contribution to MH in the other two crosses, 2 and 4. With respect to the quality tests, at least 30% of the variation in the quality parameter (SDSS or W or MT) could be explained by prolamin variation. The mixograph parameter, BDR and P and L of the alveograph, were the most erratic with about 8–76% of variation explained by prolamin composition. 3.4. Quality test correlations Correlation coefficients were determined between quality parameters in the crosses analysed (Table 5). No significant correlations were found between protein and vitreousness contents in crosses 2–4. A similar result was obtained by Ruiz and Carrillo (1995b) and Autran and Galterio (1989). In cross 1 a significant correlation was detected between both parameters according to Dexter et al. (1988). In crosses 2 and 4 the influence of protein and vitreousness content on SDSS, mixograph and alveograph was low. But in crosses 1 and 3 this influence was very important mainly in MH where 37 and 43% of variation, respectively, was explained by protein content. Brites and Carrillo (2001), Kovacs et al. (1995) and Ruiz and Carrillo (1995b) also found a correlation between MH and Prot in some crosses, showing the influence of protein content on some quality characteristics. A significant correlation was detected between SDSS, MT and W in agreement with Brites and Carrillo (2001) and Kovacs et al. (1997). In this work, alleles at Glu-B3 locus made the largest contribution to gluten quality measured by SDSS, mixograph and alveograph tests. However, a very important positive influence of Glu-1, Glu-A3, Glu-B2 and Gli-B1 loci was shown, especially when the best Glu-B3 allele was present. These results together with those of Brites and Carrillo (2001) and Carrillo et al. (2000) have important implications for wheat breeders. It is should be possible to improve selection for better dough properties by selecting germplasm based on desirable alleles such as Glu-B3 (a, c, j), Glu-A1 (subunit 1), Glu-A3 (a, c, d, h), Glu-B2 (a,b) and Gli-B1 (u-35). Undesirable alleles that should be avoided are Glu-A3 (b, e, f, g, i, j), Glu-B3 (b, e,i, k, l) and Glu-B1 (subunits 20xC20y). Moreover, the quality parameters SDSS and MT were the more correlated with W of the alveograph, a parameter related to pasta quality (D’Egidio et al., 1990). Thus these tests could be very useful for screening out lines with poor
gluten strength in early generations when the amount of material available is low. The low correlation between gluten strength (SDSS and MT) and protein and vitreousness contents indicates that these parameters must be estimated separately in any breeding program for durum wheat quality.
Acknowledgements This work was supported by Grants No. AGL 2000-1280 and AGL 2003-6382 from Comision Interministerial de Ciencia y Tecnologı´a (CICYT) of Spain.
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M.C. Martinez et al. / Journal of Cereal Science 41 (2005) 123–131 Kovacs, M.I.P., Howes, N.K., Leisle, D., Zawistowski, J., 1995. Effect of two different low-molecular-weight subunits on durum wheat pastaquality parameters. Cereal Chemistry 72, 85–87. Kovacs, M.I.P., Poste, L.M., Butler, G., Woods, S.M., Leisle, D., Noll, J.S., Dahlke, G., 1997. Durum wheat quality: comparison of chemical and rheological screening tests with sensory analysis. Journal of Cereal Science 25, 65–75. Liu, C.Y., 1995. Identification of a new low Mr gluten subunit locus on chromosome 1B of durum wheat. Journal of Cereal Science 21, 209–213. Martinez, M.C., Ruiz, M., Carrillo, J.M., 2004. New B low Mr glutenin subunit alleles at the Glu-A3, Glu-B2 and Glu-B3 loci and their relationship with gluten strength in durum wheat. in press Journal of Cereal Science 40, 101–107. Nieto-Taladriz, M.T., Ruiz, M., Martinez, M.C., Vazquez, J.F., Carrillo, J.M., 1997. Variation and classification of B low-molecularweight glutenin subunit alleles in durum wheat. Theoretical and Applied Genetics 95, 1155–1160. Payne, P.I., Lawrence, C.J., 1983. Catalogue of alleles for the complex gene loci, Glu-A1, Glu-B1, Glu-D1 which code for high-molecular-weight subunits of glutenin in hexaploid wheat. Cereal Research Communications 11, 29–35. Payne, P.I., Jackson, E.A., Holt, L.M., 1984. The association between g gliadin 45 and gluten strength in durum wheat varieties: a direct causal effect of the result of genetic linkage? Journal of Cereal Science 2, 73–81. Pogna, N.E., Autran, J.C., Mellini, F., Lafiandra, D., 1990. Chromosome 1B-encoded gliadins and glutenin subunits in durum wheat: genetics
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and relationship to gluten strength. Journal of Cereal Science 11, 15–34. Porceddu, E., Turchetta, T., Masci, S., D’Ovidio, R., Lafiandra, D., Kasarda, D.D., Impiglia, A., Nachit, M.M., 1998. Variation in endosperm protein composition and technological quality properties in durum wheat. Euphytica 100, 197–205. Ruiz, M., Carrillo, J.M., 1993. Linkage relationships between prolamin genes on chromosomes 1A and 1B in durum wheat. Theoretical and Applied Genetics 87, 353–360. Ruiz, M., Carrillo, J.M., 1995a. Separate effects on gluten strength of Gli-1 and Glu-3 prolamin genes on chromosomes 1A and 1B in durum wheat. Journal of Cereal Science 21, 137–144. Ruiz, M., Carrillo, J.M., 1995b. Relationships between different prolamin proteins and some quality parameters in durum wheat. Plant Breeding 114, 40–44. Ruiz, M., Carrillo, J.M., 1996. Gli-B3/Glu-B2-encoded prolamins do not affect selected quality properties in the durum wheat cross ‘Abadia x Mexicali 75’. Plant Breeding 115, 410–412. Singh, N.K., Shepherd, K.W., 1988. Linkage mapping of the genes controlling endosperm proteins in wheat. 1. Genes on the short arms of group-1 chromosome. Theoretical and Applied Genetics 75, 628–641. Turchetta, T., Ciaffi, M., Porceddu, E., Lafiandra, D., 1995. Relationship between electrophoretic pattern of storage proteins and gluten strength in durum wheats landraces from Turkey. Plant Breeding 114, 406–412. Vazquez, J.F., Ruiz, M., Nieto-Taladriz, M.T., Albuquerque, M.M., 1996. Effects on gluten strength of low Mr glutenin subunits coded by alleles at the Glu-A3 and Glu-B3 loci in durum wheat. Journal of Cereal Science 24, 125–130.
Effects of different prolamin alleles on durum wheat quality properties Ma del Carmen Martinez, Magdalena Ruiz1, Jose M. Carrillo* Unidad de Gene´tica, Departamento de Biotecnologı´a, Escuela Te´cnica Superior de Ingenieros Agro´nomos, Ciudad Universitaria, 28040 Madrid, Spain Received 28 May 2004; revised 16 September 2004; accepted 20 October 2004
Abstract The F4 progenies of four durum wheat crosses were used to determine the effects of different prolamin alleles on quality properties evaluated by the SDS sedimentation, mixograph, micro-alveograph and vitreousness tests and by protein content. Allelic compositions of the gliadins (Gli-B1 and Gli-2 loci) and the glutenins (Glu-1, Glu-3 and Glu-B2 loci) were determined. Alleles at the Glu-B3 locus showed a strong influence on quality measured by SDSS, mixograph and alveograph tests. Significant interactions between Glu-B3 and other glutenin loci were also detected. Prolamin composition explained more than 30% of the variation in SDSS, mixograph MT and alveograph W. The mixograph parameter BDR, and alveograph P and L parameters were the most erratic with between 8 and 76% of variation explained by prolamin composition. In general, no significant associations of prolamins with vitreousness or protein content were found. A significant correlation was detected between SDSS, MT and W. These results together with those from previous studies have important implications for wheat breeders since selection based on good alleles at Glu-B3 (a, c, j) together with favourable alleles at other loci such as Glu-A1 (subunit 1), Glu-A3 (a, c, d, h), Glu-B2 (a,b) and Gli-B1 (u-35) could improve durum wheat quality. q 2004 Published by Elsevier Ltd. Keywords: Durum wheat; Prolamins; Gluten strength; Pasta quality
1. Introduction The ability of durum wheat semolina to form an ideal dough for pasta processing rests mainly on the rheological characteristics of its gluten related to gluten elasticity or strength. In fact, manufacturers in the main pasta producing countries want semolina with strong gluten to give a highquality product. In this context, the knowledge of the genetics of quality properties of wheat has important implications for the breeder. This information can assist in choosing new durum wheat lines with favourable genetic combinations for improved quality.
Abbreviations: BDR, resistance to breakdown; H3, height at 3 min after the peak of the curve; L, extensibility; LMW, low molecular weight; MH, maximum peak height; Mr, relative molecular mass; MT, mixing development time; P, tenacity; Prot, protein content; SDSS, sodium dodecyl sulphate sedimentation; V, vitreousness; W, strength. * Corresponding author. Tel.: C34 91 336 5716; fax: C34 91 543 4879. E-mail address: [email protected] (J.M. Carrillo). 1 Current address: Instituto Nacional de Investigacio´n y Tecnologı´a Agraria y Alimentaria, Centro de Recursos Fitogeneticos, 28800 Alcala de Henares, Spain. 0733-5210/$ - see front matter q 2004 Published by Elsevier Ltd. doi:10.1016/j.jcs.2004.10.005
The viscoelasticity of cooked pasta is known to correlate with the quantity and specific composition of seed storage prolamin proteins (D’Egidio et al., 1990). A highly significant positive correlation between protein quantity and pasta cooking quality has been recognised (Autran and Galterio, 1989; Dexter and Matsuo, 1980). The genetic improvement of protein content has been particularly hampered, not only by strong environmental influences, but also by the fact that a negative correlation has been frequently found between grain yield and seed protein content in segregating populations in all cereals (Cox et al., 1985). Provided there is sufficient protein, pasta quality is likely to be acceptable, however, to ensure good pasta making quality, breeders need to aim for increased protein with an appropriate prolamin composition. The specific prolamin composition depends on the allelic variation of gliadin and glutenin proteins. Gliadins are monomeric proteins and can be subdivided into four groups termed: a, b, g and u according to their decreasing electrophoretic mobility in gels at acidic pH. Glutenins contain different polypeptide subunits, connected by intermolecular disulphide bonds; subdivided into low Mr and high Mr subunits
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according to their electrophoretic mobility in polyacrylamide gels. The genes encoding gliadin components are located on the short arm of chromosomes of the groups 1 (Gli-1 loci) and 6 (Gli-2 loci) of A and B genomes (Joppa et al., 1983). The genes coding for high Mr glutenin subunits are located on the long arm of chromosomes 1A and 1B at the Glu-1 loci, whereas low Mr glutenin subunits are located on the short arm of the same chromosomes at the Glu-3, tightly linked to Gli-1 loci (Singh and Shepherd, 1988), and at the locus Glu-B2 (Liu, 1995; Ruiz and Carrillo, 1993). Some early studies (Damidaux et al., 1978; Kosmolak et al., 1980) demonstrated the usefulness of gliadins g-45 and g-42, encoded at the Gli-B1 locus (Joppa et al., 1983), as markers of good and poor quality gluten, respectively. In further studies, Payne et al. (1984), Pogna et al. (1990) and Ruiz and Carrillo (1995a) found that low Mr glutenin subunits, encoded at the Glu-B3 locus, were responsible for the differences in quality. These early studies analysed only the effect of different low Mr patterns, especially of LMW-1 and LMW-2, linked to g-42 and g-45, respectively (Payne et al., 1984; Pogna et al., 1990). The analyses, however, were not precise since low Mr patterns are composed of different subunits encoded at different loci (Glu-A3, Glu-B3 and Glu-B2). Thus, the specific effects of each allelic variant at each locus could not be analysed. However, in later studies the influence of low Mr glutenins on quality and the separate effects of allelic variants at Glu-A3, Glu-B3 and Glu-B2 loci were reported (Brites and Carrillo, 2001; Carrillo et al., 2000; Martinez et al., 2004; Ruiz and Carrillo, 1995b, 1996; Vazquez et al., 1996). Other studies have identified desirable prolamin compositions for pasta making using the SDS-sedimentation test. Also more reliable information can be obtained by determining rheological properties with mixograph and alveograph tests, used industrially to evaluate semolina quality (D’Egidio et al., 1990; Kovacs et al., 1997). The aim of this work was to determine the effect of prolamin alleles on gluten quality, including recently identified new allelic variants (Martinez et al., 2004). The main quality properties studied were protein content, vitreousness and the rheological properties of the gluten.
the 1997–1998 season. All the F4 lines were selected for homozygous Glu-B3 alleles. 2.2. Electrophoretic analysis Prolamin extraction and electrophoretic analysis were as described (Martinez et al , 2004). The alleles for high Mr and low Mr glutenin subunits were named according to Payne and Lawrence (1983) and Nieto-Taladriz et al. (1997), respectively. The a-gliadin blocks were designated according to Pogna et al. (1990). 2.3. Quality evaluation The SDS-sedimentation (SDSS) test and protein content (Prot) were performed as described (Martinez et al., 2004). To assess mixing properties, whole wheat meal was sieved to a particle size of 125–315 mm and used in the 10-g mixograph (Finney and Shogren, 1972) with modification for a constant water absorption of 6.5 ml. The mixograph parameters estimated were: mixing development time (MT), maximum peak height (MH), height at 3 min after the peak of the curve (H3), and the difference in percentage between MH and H3 (resistance to breakdown, BDR). For F4 lines with sufficient grain (61 lines in crosses 1 and 36 in cross 2) the micro-alveograph (50 g) test was performed according to D’Egidio et al. (1990) and Boggini (1991). A sample of grain (200 g) was tempered to 17.5% moisture and milled in a Chopin CD2 mill. The semolina was sieved to obtain a particle size of 125–315 mm. The saline solution added was calculated according to the formula 0.2![190.7K(semolina moisture!4.375)]. Dough was mixed for 4 min, rested for 18 min and mixed again for 4 min. Gluten strength (W), tenacity (P) and extensibility (L) were measured. These measurements were compared with those obtained with a full size alveograph with samples of 16 durum wheat varieties. The correlations between both methods were highly significant and higher than 0.9 for W and P, and higher than 0.7 for L. Vitreousness content (V) was estimated for 200 kernels by determining visual percentage of grains not showing yellowberry according to standard methods (ISO, 1994). Two replicate analyses were made for every line and test, except for the alveograph tests.
2. Experimental 2.4. Analysis of data 2.1. Plant material Seven durum wheat varieties with contrasting prolamin allelic variants were used to make the following crosses: Anto´n (A)!Blancal de Nules (BN), Senatore Capelli (S)! Fanfarron (F), Alcala la Real (AR)!Bidi-17 (B) and Bidi17 (B)!Atalaya (AT). Between 65 and 166 F2 seeds from each cross were analysed for prolamin composition. A total of 150 F2 derived F4 lines from cross 1, 70 from cross 2, 116 from cross 3 and 45 from cross 4 were sown in a randomised complete-block design with two replications in
Analysis of variance (SAS Institute, Cary, NC) was used to study the effects of the prolamin loci on mean values of technological parameters. For each cross and parameter the effects of the blocks and loci were analysed using the general lineal model (GLM) procedure. Allelic variation at each locus was considered as source of variation and lines with the same prolamin phenotype as replications. Differences between means were compared by Duncan’s test at PZ0.05. Relationships between quality tests were examined by Pearson correlation coefficients.
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Table 1 Allelic variants of prolamins and results of quality tests in parents Locus
Anto´n
Blancal de Nules
Senatore Capelli
Fanfarro´n
Alcala´ la Real
Bidi-17
Atalaya
Glu-A1 Glu-B1 Glu-A3 Glu-B3 Glu-B2 Gli-B1 Gli-A2 Gli-B2 Quality test SDSS (mm) MT (s) MH (mm) H3 (mm) BDR (%) W (10K4 J) P (mm H2O) L (mm) V (%) Prot (%)
Null 7C8 5/b 8C9C13C16/b 12/a u 33-35-38 g 42 a 70.5C71.5 b-64
1 6C8 6/a 1C3C13*C16/l Null/b u-39 g46 a 73 b-57
Null 20xC20y 6/a 2C4C15C19/a 12/a u-35 g-45
Null 6C8 5C20/i 8C9C13C16/b Null/b u 33-35-38 g-42
Null 6C8 6/a 2C4C15C19/a 12*/c g 45
Null 20xC20y 6/a 2C4C15C19/a 12/a u-35 g 45
Null 32C33 11/e 8C9C13C16/b Null/b u 33-35-38 g 42
30.0 110.0 92.5 72.2 21.8 94.2 73.3 51.0 98.7 17.1
37.5 87.5 94.5 65.0 30.9 82.6 69.1 49.6 99.2 18.4
37.2 97.5 98.5 80.5 18.3 156.8 97.8 64.8 99.5 17.5
27.7 61.2 78.2 49.0 37.5 44.6 46.7 30.6 99.0 16.8
52.0 101.2 92.5 72.0 22.1
35.4 116.9 102.6 78.4 24.2
25.7 61.2 78.5 49.8 36.5
99.2 18.5
99.0 19.6
99.0 15.5
3. Results and discussion The prolamin differences in F4 lines from the four crosses analysed were at the Glu-1, Glu-B2, Glu-3, Gli-B1 and Gli-2 loci. The allelic variants of prolamins and the results of the quality tests for the parents are shown in
Table 1. The inheritance of these prolamin genes has been determined in previously (Joppa et al., 1983; Martinez et al., 2004; Nieto-Taladriz et al., 1997; Ruiz and Carrillo, 1993). The high Mr and low Mr glutenin subunits and the gliadin variants studied are shown in Figs. 1 and 2, respectively. Due to subunit overlapping the effects of
Fig. 1. SDS-PAGE fractionation of high Mr and low Mr glutenin subunits in the cultivars Anto´n (A), Blancal de Nules (BN), Senatore Capelli (S), Fanfarron (F), Bidi-17 (B), Alcala la Real (AR), Bidi-17 (B) and Atalaya (A). The subunits studied are numbered.
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Fig. 2. A-PAGE fractionation of gliadins in the cultivars Anto´n (A), Blancal de Nules (BN), Bidi-17 (B) and Alcala la Real (AR). The cultivar Langdon (L) is included as reference. The gliadins studied are numbered.
some alleles (Glu-A3 in cross 1 and Glu-B2 in cross 4) could not be studied. For Glu-B3, all lines analysed were homozygous, so intrallelic interactions for this locus were avoided. 3.1. Effects of high Mr glutenin alleles on gluten quality The results of quality tests for the allelic variants of prolamins analysed in the four crosses are shown in Table 2 (SDSS and mixograph tests) and Table 3 (alveograph test). The effects of high Mr glutenins at Glu-A1 were studied in cross 1 (Table 1 and Fig. 1). Lines with the high Mr subunit 1 had significantly higher values of SDSS and mixograph parameters than lines with the Null subunit (Table 2). However, the presence or absence of subunit 1 did not result
in any significant difference in alveograph properties (Table 3). No significant interaction between Glu-A1 and other loci was found, in agreement with Brites and Carrillo (2001) and Ruiz and Carrillo (1995b). The influence of the high Mr subunit 1 on quality has not often been studied since most durum wheats possess the Null subunit at Glu-A1. Brites and Carrillo (2001), Ciaffi et al. (1991) and Turchetta et al. (1995) observed positive effects of subunit 1 on SDSS which agrees with the results obtained in the present work. Ruiz and Carrillo (1995b) showed the superiority of subunit 1 in improving MT, but not in SDSS. Conversely, Brites and Carrillo (2001) did not find any significant contribution to mixograph properties, but the L of alveograph was correlated positively with presence of subunit 1. All these results indicate a positive effect of the high Mr subunit 1 on gluten quality although the gluten parameter involved can be different depending on the material analysed. The high Mr subunits at Glu-B1 were studied in the four crosses (Table 1 and Fig. 1). All the Glu-B1 alleles compared showed significant differences in SDSS. The subunits 6C8 were associated with higher SDSS values than 7C8 (cross 1) and 20xC20y subunits (crosses 2 and 3). The 20xC20y also had lower values than 32C33 subunits (cross 4). Different effects of Glu-B1 alleles on mixograph parameters were obtained depending on the allele and the parameter considered. The subunits 6C8 had longer MT (crosses 2 and 3) and H3 and BDR (cross 3) than subunits 20xC20y which indicates stronger dough. For BDR, lower values are better. In cross 1, 7C8 subunits were associated with higher MH than 6C8. None of the Glu-B1 alleles had a significant effect on alveograph parameters either in cross 1 or 2 (Table 3). These results indicated that the differences between subunits 6C8 and 7C8 were small, whereas the 20xC20y subunits had a clear negative influence on gluten quality. Brites and Carrillo (2001) also demonstrated the inferiority of 20xC20y subunits relative to 6C8 for SDSS, mixograph properties and W of the alveograph. This last influence was not observed in the present work. The negative contribution of 20xC20y to some quality properties, mainly to SDSS has been previously observed (Kovacs et al., 1997; Ruiz and Carrillo, 1995b; Turchetta et al., 1995). Significant interactions between Glu-B1 and Glu-B3 or Glu-A3 were detected in cross 2. Thus, 6C8 subunits were associated with better values of SDSS and MT than 20xC20y when the best allele Glu-A3a was present, and with better values for SDSS in the presence of the best allele Glu-B3a. In contrast, no significant differences between subunits 6C8 and 20xC20y were found when the worst alleles Glu-A3i or Glu-B3b were present. On the other hand, Brites and Carrillo (2001) did not find interactions between Glu-B3 and Glu-B1 alleles probably because the alleles analysed were different from those studied in the present work. Although the same Glu-B1 alleles were compared in crosses 2 and 3 more significant differences were obtained in cross 3. In this cross, both parents had the same Glu-B3
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Table 2 Means values of the quality tests SDSS and mixograph values for the F4 lines grouped according to prolamin composition Locus
Cross
Prolamins/alleles alleles
Lines
SDSS (mm)
MT (s)
MH (mm)
H3 (mm)
BDR (%)
Glu-A1
1
Glu-B1
1
Null 1 7C8 6C8 20xC20y 6C8 6C8 20xC20y 20xC20y 32C33 6/a 6C5C20/aCi 6/a 11/e 8C9C13C16/b 1C3C13*C16/l 2C4C15C19/a 8C9C13C16/b 2C4C15C19/a 8C9C13C16/b 12/a Null/b 12/a Null/b 12*/c 12/a g-45 u-35 g-45 a-70.5C71.5 a-73 b-64 b-57
40 110 48 32 16 22 32 32 6 5 21 43 27 18 90 58 39 31 22 23 108 42 58 12 19 34 29 87 30 42 48 36
30.5b 35.7a 32.5b 36.9a 24.4b 37.5a 65.8a 30.9b 29.7b 50.1a 39.7aa 32.0ba 36.8a 31.7a 36.4aa 30.6ba 43.0aa 25.6ba 46.1a 23.5b 35.9a 30.0a 36.5a 29.9a 40.2ba 51.2aa 42.0ba 49.8aa 34.5a 32.0a 33.8a 32.7a
80.4b 92.1a 90.9a 87.3a 63.9b 83.5a 134.9a 105.9b 72.5a 101.7a 94.7a 75.1b 79.3a 73.6a 91.3a 85.1b 99.8a 59.5b 103.0a 53.9b 91.2a 83.2b 85.2a 66.6a 103.5b 125.5a 106.5b 122.4a 91.0a 88.1a 85.8a 88.6a
87.7b 91.1a 91.6a 89.6b 84.8a 86.5a 99.0a 101.3a 86.0a 92.0a 89.8a 85.8b 84.2a 84.2a 90.5a 89.7a 91.1a 82.8b 90.4a 78.5b 90.5a 89.3a 87.8a 85.1a 100.1a 101.3a 99.8a 100.2a 91.0a 90.9a 89.9a 90.7a
63.3b 66.9a 67.4a 65.4a 56.6a 60.5a 78.4a 72.8b 63.0a 71.7a 63.7a 60.2a 62.3a 61.0a 66.3a 65.4a 67.5a 54.5b 69.5a 55.0b 66.3a 65.0a 62.7a 56.7a 71.7b 77.3a 71.9b 76.4a 66.2a 66.3a 65.9a 65.2a
26.5b 27.9a 26.5a 27.0a 33.6a 30.2a 20.8b 28.3a 26.9a 22.1a 29.1a 30.1a 26.4a 27.4a 26.7a 27.0a 26.0b 34.1a 23.1b 29.9a 26.7a 27.1a 28.8a 33.1a 28.2a 23.7b 28.0a 23.8b 27.3a 27.0a 26.7a 28.1a
2 3 4 Glu-A3
2 4
Glu-B3
1 2 4
Glu-B2
1 2 3
Gli-B1
3
Gli-A2
1
Gli-B2
1
Means followed by different letters are significantly different at PZ0.05. a Martinez et al. (2004).
alleles, so the influence of Glu-B1 was probably better evaluated in this cross. Controversial results have been found with respect to influence of Glu-B1 on quality. Ciaffi et al. (1991) and Vazquez et al. (1996) no influence of Glu-B1 on quality, whereas Porceddu et al. (1998) and Tuchetta et al. (1995) found that Glu-B1 explained 8% of the variation of the SDSS test. These contrasting results could be due to the different magnitude of the influence of Glu-B1 alleles depending on which Glu-B3 alleles were present. In this work, the greatest influence of Glu-B1 was detected when the difference due to the Glu-B3 effect was removed (cross 3). 3.2. Effects of low Mr glutenin alleles on gluten quality The effects on quality of the low Mr subunits coded at Glu-A3, Glu-B3 and Glu-B2 were analysed (Table 1 and Fig. 1). The SDSS data obtained earlier (Martinez et al., 2004) for some low Mr glutenin alleles have been included in Table 2 for the comparison. The Glu-A3 alleles were studied in crosses 2 and 4 (a vs aCi and a vs e,
respectively). The Glu-A3a is frequently present in durum wheat cultivars, nevertheless alleles i and e are rare (NietoTaladriz et al., 1997; Martinez et al., 2004). Table 2 shows that allele a was associated with higher values of SDSS, MT and MH than allele i. No significant differences were observed between the two alleles in the alveograph test (Table 3). In cross 4, the presence of allele a or e did not result in any differences in the quality properties analysed (Table 2). In this cross a significant interaction was detected with the Glu-B3 alleles for SDSS. Glu-A3a was significantly better than Glu-A3e in the presence of the best allele Glu-B3a, whereas Glu-A3a and Glu-A3e were not significantly different when the Glu-B3b was present. These results indicate that the effect of the allele Glu-A3a on quality was dependent on which allele was present at Glu-B3. Ruiz and Carrillo (1995b) observed a similar interaction for Glu-A3b and d for MT and H3 mixograph parameters. Comparing Glu-A3 effects, Carrillo et al. (2000) found a superiority of allele a relative to e for SDSS and mixograph parameters. This superiority was smaller for alveograph parameters. Ruiz and Carrillo (1995b) found
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M.C. Martinez et al. / Journal of Cereal Science 41 (2005) 123–131
Table 3 Mean values of the alveograph test for the F4 lines grouped according to prolamin composition Locus
Cross
Prolamins/alleles
Lines
W (10K4 J)
P (mm H2O)
L (mm)
Glu-A1
1
Glu-B1
1
Null 1 7C8 6C8 20C20Y 6C8 6/a 6C5C20/aCi 8C9C13C16/b 1C3C13*C16/l 2C4C15C19/a 8C9C13C16/b 12/a Null/b 12/a Null/b a-70.5C71.5 a-73 b-64 b-57
16 45 17 15 5 2 5 12
68.8a 73.8a 76.1a 66.7a 58.5a 56.4a 82.3a 65.7a 78.0a 62.8b 98.7a 39.5b 76.6a 60.2a 78.2a 45.4a 64.5a 73.2a 66.8a 64.9a
61.0a 60.9a 62.9a 58.2a 58.6a 52.5a 68.5a 60.8a 61.7a 59.6a 74.2a 50.9b 61.7a 58.5a 66.5a 50.5a 58.6a 62.3a 61.1a 55.7a
42.5a 47.2a 49.2a 41.6a 38.0a 44.4a 45.9a 38.5a 49.4a 39.8b 48.4a 31.4b 48.5a 38.0a 42.1a 36.0a 42.7a 46.1a 41.4a 45.3a
2 Glu-A3
2
Glu-B3
1 2
Glu-B2
1 2
Gli-A2
1
Gli-B2
1
39 22 10 7 46 15 15 2 13 16 19 15
Means followed by different letters in bold are significantly different at PZ0.05.
a negative contribution of allele e to MT and H3 compared with allele b. The negative effect of Glu-A3i on quality supports a previous result for SDSS (Martinez et al., 2004), but this is the first time that its effect on mixograph and alveograph properties have been determined. These results, together with previous results (Brites and Carrillo, 2001; Carrillo et al., 2000) indicate that Glu-A3 alleles a, c, d and h are preferable to b, e, f, g, i and j (subunits 4C6*C15C19) for quality selection. For the Glu-B3, the alleles compared were b vs l in cross 1 and b vs a in crosses 2 and 4 (Table 1 and Fig. 1). The allele a should better positive effects than b for all the gluten quality properties analysed, and b was better than l for SDSS, MT, W and L (Tables 2 and 3). The high number of significant differences obtained for this locus in several quality tests confirms that Glu-B3 alleles have a much greater effect on gluten quality than alleles at other loci (Brites and Carrillo, 2001; Liu, 1995; Ruiz and Carrillo, 1995b). The smaller differential effects on gluten quality obtained in cross 1 between the parents and the alleles compared (b vs l) could be due to the higher similarity of both protein patterns and to the absence of the subunit 2 (Fig. 1) representative of the LMW-2 pattern (Nieto-Taladriz et al., 1997) and associated with high quality. This is the first time that the allele l has been analysed for mixograph and alveograph characteristics. The ranking for Glu-B3 alleles for the different quality properties, a[bOl, is in agreement with that obtained for the SDSS test (Martinez et al., 2004) and confirms the superiority of allele a, frequently present in durum wheat cultivars, in the mixograph and alveograph tests (Brites and Carrillo, 2001; Carrillo et al., 2000; Ruiz and Carrillo, 1995b). These results together with
those of Brites and Carrillo (2001) and Carrillo et al. (2000) indicate that Glu-B3 alleles a, c and j are related to the highest values for gluten quality, while the alleles b, e, i, k and l are related to the lowest. For the Glu-B2 locus, the alleles compared were a (low Mr subunit 12) vs b (Null) in crosses 1 and 2, and a vs c (low Mr subunit 12*) in cross 3 (Table 1 and Fig. 1). No significant differences were detected between alleles a and b except for MT in cross 1 (Tables 2 and 3). In the other comparison (cross 3), where most of the low Mr subunits were identical, allele a was associated with better gluten quality than allele c for almost all properties analysed (Table 2). These results confirm the small, yet significant differences in quality between alleles a and b (Brites and Carrillo, 2001; Ruiz and Carrillo, 1996) and the low SDSS values associated with allele c (Martinez et al., 2004). The influence of allele c on mixograph and alveograph tests was analysed first time and shown to have a negative effect on gluten quality. 3.3. Effects of gliadin alleles on gluten quality The influence on quality of u-35 encoded at Gli-B1 was analysed in cross 3 (Table 1 and Fig. 2). A positive effect of this gliadin on SDSS, MT, H3 and BDR was shown (Table 2). An interalelic interaction was observed with Glu-B1 for SDSS. The presence of the u-35 increased the positive effect of subunits 6C8 and the negative effect of subunits 20xC20y. Pogna et al. (1990) also detected positive effects of gliadins at Gli-B1 on gluten quality, these effects being smaller than those of Glu-B3 alleles. Autran and Galterio (1989) did not find a significant
M.C. Martinez et al. / Journal of Cereal Science 41 (2005) 123–131
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Table 4 Percentage of variation of the quality tests explained by the prolamins studied Cross
SDSS (mm) a
1 2 3 4
52 70a 52a 79
MT (s)
MH (mm)
H3 (mm)
BDR (%)
W (10K4 J)
P (mm H2O)
L (mm)
34 79 48 67
21 62 0 58
24 69 18 74
18 62 35 76
35 83
8 67
14 70
All the values are significant at PZ0.05, except the 8 and zero values. a Martinez et al. (2004).
correlation between SDSS and u-35 in a group of different durum wheat varieties. However, the separate effect of u gliadins on quality is not easy to evaluate because these prolamins are inherited together with other gliadins and low Mr glutenins encoded at Gli-B1 and Glu-B3, respectively. Thus, the effects attributed to u gliadin could be due to the presence of these associated proteins. In the present work, this problem did not exist because both parents had the gliadin g-45 at Gli-B1 (Fig. 2) and the allele Glu-B3a (Table 1 and Fig. 1). Thus, the positive effects detected seem to be specifically due to the u-35. The effects of the alleles at Gli-A2 and Gli-B2 were studied in cross 1. No significant differences were observed between Gli-A2 and Gli-B2 alleles for any of the quality tests (Tables 2 and 3). These results confirm previous
reports (Pogna et al., 1990; Ruiz and Carrillo, 1995b). However, Autran and Galterio (1989) found significant effects of Gli-A2 and Gli-B2 alleles on gluten firmness. In general, the prolamins studied showed no significant associations with vitreousness (V) or protein (Prot) contents. The F-tests of ANOVA were significant (PZ0.05) only for V between Glu-A3 alleles in cross 2. For Prot no significant correlation was detected except that reported by Martinez et al. (2004) between Glu-B3 and Gli-B1 alleles in crosses 2 and 3, respectively. Brites and Carrillo (2001) and Ruiz and Carrillo (1995b) detected no influence of prolamin composition on V or Prot values. The results of the four crosses can be grouped based on the influence of prolamin in the quality tests (Table 4). In crosses 2 and 4 a substantial proportion, 62–83 and 58–79%,
Table 5 Correlation coefficients between quality parameters in the crosses analysed
SDSS (mm)
MT (s)
MH (mm)
H3 (mm)
BDR (%)
W (10K4 J) P (mm H2O) L (mm) Prot (%)
Cross
MT (s)
MH (mm)
H3 (mm)
BDR (%)
W (10K4 J)
P (mm H2O)
1 2 3 4 1 2 3 4 1 2 3 4 1 2 3 4 1 2 3 4 1 2 1 2 1 2 1 2 3 4
0.47** 0.84** 0.66** 0.83**
0.24** 0.61** K0.07 0.78** 0.61** 0.76** 0.32** 0.88**
0.23** 0.79** 0.54** 0.84** 0.51** 0.87** 0.74** 0.94** 0.73** 0.88** 0.49** 0.95**
K0.09 K0.80** K0.65** K0.76** K0.11 K0.82** K0.67*** K0.86** K0.03 K0.67** 0.01 K0.68** K0.70** K0.94** K0.86** K0.87**
0.48** 0.87**
0.16 0.82**
0.37** 0.66**
0.56** 0.90**
0.34** 0.85**
0.42** 0.79**
0.35** 0.85**
0.18 0.91**
0.40** 0.72**
0.45** 0.95**
0.35** 0.93**
0.33** 0.87**
K0.35** K0.92**
K0.36** K0.85**
K0.11 K0.90**
0.80** 0.95**
0.64** 0.87** 0.23 0.77**
* And ** significant at the 5 and 1% level, respectively.
L (mm)
Prot (%)
V (%)
K0.00 K0.11 K0.09 K0.12 0.28** K0.13 0.12 K0.11 0.59** 0.14 0.56** 0.18 0.22** K0.02 0.14 K0.05 0.28** 0.16 0.16 0.41* 0.03 K0.24 K0.01 K0.19 0.03 K0.25
0.02 K0.10 0.10 0.17 0.17* K0.10 K0.14 0.12 K0.31** K0.11 0.06 0.09 K0.13 K0.14 K0.16 0.07 K0.14 0.15 0.22* K0.01 0.06 K0.37 0.09 K0.35 K0.02 K0.22 0.40** 0.12 0.09 0.32
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M.C. Martinez et al. / Journal of Cereal Science 41 (2005) 123–131
respectively, of the variation in the quality tests was explained in terms of prolamin composition. In crosses 1 and 3, this proportion was 8–52 and 0–52%, respectively. The value of zero corresponds to the parameter MH in cross 3, where no influence of prolamins on this parameter was detected. Taking into account that low Mr glutenins encoded at Glu-B3 show the most significant effects on quality, the low variation explained by prolamins in crosses 1 and 3 could be due to the similar effect on quality parameters of Glu-B3 glutenins in these two crosses. In fact, the Glu-B3 made the largest positive contribution to MH in the other two crosses, 2 and 4. With respect to the quality tests, at least 30% of the variation in the quality parameter (SDSS or W or MT) could be explained by prolamin variation. The mixograph parameter, BDR and P and L of the alveograph, were the most erratic with about 8–76% of variation explained by prolamin composition. 3.4. Quality test correlations Correlation coefficients were determined between quality parameters in the crosses analysed (Table 5). No significant correlations were found between protein and vitreousness contents in crosses 2–4. A similar result was obtained by Ruiz and Carrillo (1995b) and Autran and Galterio (1989). In cross 1 a significant correlation was detected between both parameters according to Dexter et al. (1988). In crosses 2 and 4 the influence of protein and vitreousness content on SDSS, mixograph and alveograph was low. But in crosses 1 and 3 this influence was very important mainly in MH where 37 and 43% of variation, respectively, was explained by protein content. Brites and Carrillo (2001), Kovacs et al. (1995) and Ruiz and Carrillo (1995b) also found a correlation between MH and Prot in some crosses, showing the influence of protein content on some quality characteristics. A significant correlation was detected between SDSS, MT and W in agreement with Brites and Carrillo (2001) and Kovacs et al. (1997). In this work, alleles at Glu-B3 locus made the largest contribution to gluten quality measured by SDSS, mixograph and alveograph tests. However, a very important positive influence of Glu-1, Glu-A3, Glu-B2 and Gli-B1 loci was shown, especially when the best Glu-B3 allele was present. These results together with those of Brites and Carrillo (2001) and Carrillo et al. (2000) have important implications for wheat breeders. It is should be possible to improve selection for better dough properties by selecting germplasm based on desirable alleles such as Glu-B3 (a, c, j), Glu-A1 (subunit 1), Glu-A3 (a, c, d, h), Glu-B2 (a,b) and Gli-B1 (u-35). Undesirable alleles that should be avoided are Glu-A3 (b, e, f, g, i, j), Glu-B3 (b, e,i, k, l) and Glu-B1 (subunits 20xC20y). Moreover, the quality parameters SDSS and MT were the more correlated with W of the alveograph, a parameter related to pasta quality (D’Egidio et al., 1990). Thus these tests could be very useful for screening out lines with poor
gluten strength in early generations when the amount of material available is low. The low correlation between gluten strength (SDSS and MT) and protein and vitreousness contents indicates that these parameters must be estimated separately in any breeding program for durum wheat quality.
Acknowledgements This work was supported by Grants No. AGL 2000-1280 and AGL 2003-6382 from Comision Interministerial de Ciencia y Tecnologı´a (CICYT) of Spain.
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