Prediction of durum-wheat quality from gliadin-protein composition

Cros, DL du; Wrigley, C. W.; Hare, RA

doi:10.1071/ar9820429

Cited by 51 publications

(12 citation statements)

References 15 publications

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“…However, the first order is more reliable since it has been obtained using random lines instead of cultivars. Differences in gluten strength between LMW -1 and LMW -2 patterns have been shown in several studies (du Cros 1987, Pogna et al 1990, Carrillo et al 1990a, b, Ciaffi et al 1991. Desirable mixing properties associated with }'-45 were obtained by Kosmolak et al (1980), Taha andSagi (1987) anddu Cros (1987).…”

Section: Discussionmentioning

confidence: 84%

“…This information is used to help choose parental lines that will produce progenies with favourable genetic combinations and to enable selection in early generations by rapid biochemical tests. Prolamin proteins (gliadins and glutenins) have been shown to have a cause-and-effect relationships with durum quality: varieties with the y-gliadin type 45 generally produce cooked pasta with high firmness and visco-elasticity, while the opposite occurs when the y-ghadin type 42 is present (Damidaux et al 1978, Kosmolak et al 1980, du Cros et al 1982). Gliadins 7-42 and 7-45, coded by alleles at the Gli-B\ locus, are closely linked to two different low-molecular-weight (LMW) glutenin patterns (LMW-1 and LMW-2, respectively), coded by alleles at the Glu-Bl) locus (Payne et al 1984).…”

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confidence: 99%

“…It seems that these patterns, composed of several LMW glutenin subunits, are functionally responsible for gluten strength in durum wheat, while y-gliadins coded at Gli-Bl are only genetic markers (Payne et al 1984, Pogna et al 1988. Some researchers have studied the association of LMW-1 and LMW-2 patterns with gluten quality (du Cros, 1987, Pogna et al 1990, Ciaffi et al 1991. However, there are other LMW patterns coded at Glu-Bl) besides LMW-1 and LMW-2 which show different relationships with gluten strength (Carrillo et al 1990a, b).…”

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confidence: 99%

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Relationships between different prolamin proteins and some quality properties in durum wheat

Ruíz

Carrillo

1995

Plant Breeding

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The objective of this paper was to study the differences between some prolamin variants coded at the loci Glu-3/Gli-l, Glu-\ and Gli-A2 and their relative roles in durum-wheat quality. F, lines from four durum wheat crosses ("Abadia" x 'Mexicali". "Oscar" x "Ardente", 'Oscar X Mexicali' and 'Alaga' x "C. of Balazote") were analysed for ghadin and glutenin composition by electrophoresis. Whole-grain-derived samples were analysed for SDS sedimentation (SDSS) value, mixing properties, and contents of protein and vitreousness. The glutenin patterns LMW-2. LMW-2-and LMW-2 (CB) at Ghi-B3/Gli-B\ were associated with better gluten quality than were LMW-1 and LMW-2*. The glutenin subunits LMW4 and LMW3 -h 15 at Glu-A3/Gli-A] and HMW-1 showed better mixing properties than LMW7 + 12. LMW5 and the null phenotype. respectively. The HMW glutenin subunits 20 + 8 at Glu-B\ showed a negative association with gluten quahty. but the rest of the HMW glutenin subunits and a-gliadins did not show any influence on gluten quality.Correlations between the results of the SDSS test and the mixograph were highly significant, but no correlation was found between these results and protein and vitreousness contents. The results are discussed in relation to the development of durum wheat varieties with improved qualities.

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Section: Discussionmentioning

confidence: 84%

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confidence: 99%

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confidence: 99%

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Relationships between different prolamin proteins and some quality properties in durum wheat

Ruíz

Carrillo

1995

Plant Breeding

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“…Autran and Galterio (1989) observed negative relationship of ω-gliadins with pasta quality. Du Cros et al (1982) observed close association between dough strength and a group of gliadin proteins (including band 45), and between dough weakness and a different group of gliadins (including band 42). All breeding lines with weak dough had band 42 and its associated bands, while 90% of the strong-dough lines had gliadin 45 band.…”

Section: Pasta Qualitymentioning

confidence: 95%

Biochemical and Functional Properties of Wheat Gliadins: A Review

Barak

Mudgil

Khatkar

2014

Critical Reviews in Food Science and Nutrition

132

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Gliadins account for 40-50% of the total storage proteins of wheat and are classified into four subcategories, α-, β-, γ-, and ω-gliadins. They have also been classified as ω5-, ω1, 2-, α/β-, and γ-gliadins on the basis of their primary structure and molecular weight. Cysteine residues of gliadins mainly form intramolecular disulfide bonds, although α-gliadins with odd numbers of cysteine residues have also been reported. Gliadins are generally regarded to possess globular protein structure, though recent studies report that the α/β-gliadins have compact globular structures and γ- and ω-gliadins have extended rod-like structures. Newer techniques such as Mass Spectrometry with the development of matrix-assisted laser desorption/ionization (MALDI) in combination with time-of-flight mass spectrometry (TOFMS) have been employed to determine the molecular weight of purified ω- gliadins and to carry out the direct analysis of bread and durum wheat gliadins. Few gliadin alleles and components, such as Gli-B1b, Gli-B2c and Gli-A2b in bread wheat cultivars, γ-45 in pasta, γ-gliadins in cookies, lower gliadin content for chapatti and alteration in Gli 2 loci in tortillas have been reported to improve the product quality, respectively. Further studies are needed in order to elucidate the precise role of gliadin subgroups in dough strength and product quality.

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“…1 and Table II). Most of the samples had g-45 but five of the accessions had g-42, known to be associated with lower dough strength in durum wheat (du Cros et al 1982). Thirteen different HMW-GS patterns were found with the majority null at Glu-A1 but with two other variants found expressing subunits 1, 2*, or 2**.…”

Section: Protein Qualitymentioning

confidence: 98%

Protein and Starch Properties of Some Tetraploid Wheats

Sissons

Batey

2003

Cereal Chem

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The tetraploid relatives (subspecies) of commercial durum wheat (Triticum turgidum L. subsp. turgidum conv. durum (Desf.) MacKey) offer a source of economically useful genes for the genetic improvement of durum cultivars. Thirty‐two accessions, representing five different subspecies: var. durum (13 accessions), polonicum (7), persicum (3), turanicum (5), and turgidum (4) were grown at Tamworth, Australia, in 1997 and 1999. These accessions were compared with three durum cultivars: Wollaroi and Kamilaroi (in both years) and Yallaroi (in 1998 only). In this study, the glutenin subunit composition and molecular weight distribution, together with starch properties of these accessions, were studied. A much wider range in both the glutenin subunit composition and the starch RVA paste viscosities and gelatinization profiles were found in the accessions compared with the cultivated durum wheats. Most of the accessions had lower gluten strength and the presence of poor quality LMW alleles, and low proportions of unextractable polymeric protein could explain this. For starch, RVA peak viscosity correlated strongly with cooking loss of pasta, the only significant correlation between starch properties and measured aspects of pasta quality.

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Prediction of durum-wheat quality from gliadin-protein composition

Cited by 51 publications

References 15 publications

Relationships between different prolamin proteins and some quality properties in durum wheat

Relationships between different prolamin proteins and some quality properties in durum wheat

Biochemical and Functional Properties of Wheat Gliadins: A Review

Protein and Starch Properties of Some Tetraploid Wheats

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