Comparative investigations of gluten proteins from different wheat species I. Qualitative and quantitative composition of gluten protein types

In contrast to the hexaploid common (bread) wheat, little information is available on the qualitative and quantitative compositions of gluten proteins from other cultivated wheat species. Therefore, representatives of hexaploid spelt, tetraploid durum wheat and emmer, and diploid einkorn were compared with three classes of common wheat (winter wheat, spring wheat, wheat rye hybrid). The flours were extracted to yield total endosperm proteins and the gluten protein fractions (gliadins and glutenin subunits). The extracts were characterised using sodium dodecyl sulfate polyacrylamide gel electrophoresis and reversed-phase HPLC; both methods revealed that gluten protein groups and types known from common wheat (ω-, α-, γ-gliadins, HMW and LMW subunits of glutenin) were present in all species. The HPLC platterns of gliadins and glutenin subunits from species with the same genome composition (common wheat/spelt or durum wheat/emmer) were related, and those of einkorn quite different. According to the quantities determined by reversed-phase HPLC, α-gliadins were predominant in most cases, followed by γ-gliadins and LMW subunits; ω-gliadins and HMW subunits were generally minor components. Common wheats were characterised by the highest proportions of total glutenins and HMW subunits, which are known to be important for breadmaking quality. Moreover, the lower ratio of gliadins to glutenins was typical. Emmer had the lowest proportions of total glutenins and of HMW and LMW subunits, together with einkorn the highest proportion of α-gliadins, and, by far, the highest ratio of gliadins to glutenins. The values for spelt and durum wheat were mostly in a medium range between common wheats, emmer, and einkorn, respectively. Amongst common wheats, spring wheat was characterised by more balanced quantities of α- and γ-gliadins, and wheat rye hybrid by the highest proportions of ω-gliadins. Received: 26 November 1999     

Chemistry of gluten proteins

Gluten proteins play a key role in determining the unique baking quality of wheat by conferring water absorption capacity, cohesivity, viscosity and elasticity on dough. Gluten proteins can be divided into two main fractions according to their solubility in aqueous alcohols: the soluble gliadins and the insoluble glutenins. Both fractions consist of numerous, partially closely related protein components characterized by high glutamine and proline contents. Gliadins are mainly monomeric proteins with molecular weights (MWs) around 28,000-55,000 and can be classified according to their different primary structures into the alpha/beta-, gamma- and omega-type. Disulphide bonds are either absent or present as intrachain crosslinks. The glutenin fraction comprises aggregated proteins linked by interchain disulphide bonds; they have a varying size ranging from about 500,000 to more than 10 million. After reduction of disulphide bonds, the resulting glutenin subunits show a solubility in aqueous alcohols similar to gliadins. Based on primary structure, glutenin subunits have been divided into the high-molecular-weight (HMW) subunits (MW=67,000-88,000) and low-molecular-weight (LMW) subunits (MW=32,000-35,000). Each gluten protein type consists or two or three different structural domains; one of them contains unique repetitive sequences rich in glutamine and proline. Native glutenins are composed of a backbone formed by HMW subunit polymers and of LMW subunit polymers branched off from HMW subunits. Non-covalent bonds such as hydrogen bonds, ionic bonds and hydrophobic bonds are important for the aggregation of gliadins and glutenins and implicate structure and physical properties of dough.     

Comparative proteome analysis of glutenin synthesis and accumulation in developing grains between superior and poor quality bread wheat cultivars

BACKGROUND: Wheat glutenins are the major determinants of wheat quality. In this study, grains at the development stage from three wheat cultivars (Jimai 20, Jin 411 and Zhoumai 16) with different bread‐making quality were harvested based on thermal times from 150 °C_d to 750 °C_d, and were used to investigate glutenin accumulation patterns and their relationships with wheat quality. RESULTS: High and low molecular weight glutenin subunits (HMW‐GSs and LMW‐GSs) were synthesised concurrently. No obvious correlations between HMW/LMW glutenin ratios and dough property were observed. Accumulation levels of HMW‐GSs and LMW‐GSs as well as 1Bx13 + 1By16 and 1Dx4 + 1Dy12 subunits were higher in superior gluten quality cultivar Jimain 20 than in poor quality cultivar Jing 411 and Zhoumai 16. According to the results of two‐dimensional gel electrophoresis, six types of accumulation patterns in LMW‐GSs were identified and classified. The possible relationships between individual LMW‐GSs and gluten quality were established. CONCLUSION: The high accumulation level of HMW‐GSs and LMW‐GSs as well as 1Bx13 + 1By16 and 1Dx4 + 1Dy12 subunits contributed to the superior gluten quality of Jimai 20. Two highly expressed and 16 specifically expressed LMW glutenin subunits in Jimain 20 had positive effects on dough quality, while 17 specifically expressed subunits in Zhoumai 16 and Jing 411 appeared to have negative effects on gluten quality. Copyright © 2011 Society of Chemical Industry     

The influence of nitrogen fertilisation on quantities and proportions of different protein types in wheat flour

The flours of 13 wheat varieties grown at different levels of nitrogen fertilisation were characterised by the quantitative determination of flour protein groups and gluten protein types using a combined extraction/HPLC procedure. The results demonstrate that the quantities of albumins and globulins were scarcely influenced by different nitrogen fertilisation, whereas those of gluten proteins (gliadins, glutenins) were strongly influenced. The effect on gliadins was more pronounced than on glutenins, as well as the effect on major protein types (α-gliadins, γ-gliadins, LMW subunits of glutenin) in comparison with minor types (ω-gliadins, HMW subunits of glutenin). The proportions of hydrophilic proteins (ω-gliadins, HMW subunits of glutenin) were increased by high levels of nitrogen and those of hydrophobic proteins (γ-gliadin, LMW subunits of glutenin) were decreased. The degree of the effects on both quantities and proportions of flour protein groups and gluten protein types was strongly dependent on the variety. © 1998 SCI.     

The influence of 1B/1R chromosome translocation on gluten protein composition and technological properties of bread wheat

The Austrian bread wheat Amadeus without and with 1BL/1RS translocation and three further translocation genotypes with known HMW subunit compositions were grown under the same environmental conditions. Their flours were characterised by the determination of crude protein content and, partly, by the determination of glutathione and cysteine. Furthermore, the qualitative and quantitative composition of gluten protein types was analysed by a combined extraction and reversed phase HPLC procedure. Dough development time, maximum resistance and extensibility of dough and gluten, and bread volume were determined by means of microscale methods. Protein, glutathione and cysteine contents of flours were only slightly influenced by translocation. The HPLC patterns of gliadins and glutenin subunits showed that translocation caused characteristic changes concerning ω‐gliadins, γ‐gliadins and LMW subunits of glutenin. The amount of ω 1,2‐gliadins was significantly increased and that of LMW subunits decreased. The effect of translocation on the rheological properties of dough and gluten was characterised by a strongly reduced dough development time, reduced maximum resistance and increased extensibility. Bread volume was decreased by about 10%. The amount of glutenin subunits was correlated with dough development time, resistance of dough and gluten, and bread volume to a higher extent (r = 0.79–0.91) than the amount of gliadins (r = 0.52–0.80). Correlation coefficients for LMW subunits were higher (r = 0.82–0.88) than those for HMW subunits (r = 0.35–0.61) when all five wheats were included. Instead, when only translocation lines were considered, HMW subunits (r = 0.89–0.98) were more important than LMW subunits (r = 0.64–0.86). Altogether, the results demonstrate that translocation causes important quantitative as well as qualitative changes in gluten protein composition which can be efficiently determined by reversed phase HPLC. © 2000 Society of Chemical Industry     

Studies on the distribution and binding of endogenous glutathione in wheat dough and gluten. II. Binding sites of endogenous glutathione in glutenins

For the identification of the binding sites of glutathione (GS) in glutenins, flour of the wheat cultivar " Canadian Western Red Spring " was mixed with water containing ³⁵S-labelled reduced GS as a tracer. The resulting dough was washed in a Glutomatic, and, in order to remove gliadins, the gluten obtained was extracted with 70% aqueous ethanol adjusted to pH 5.5 with acetic acid. The residual proteins (glutenins) were hydrolyzed with thermolysin, and the hydrolysate was separated by gel permeation chromatography on Sephadex G25 and by several steps of reversed-phase HPLC on C₁₈ silica gel. The major radioactive disulphide peptides identified by scintillation analysis were collected and analysed for their amino acid sequences. Twenty-five peptides linked to GS could be assigned to known sequences of gluten proteins. Most peptides (16) were derived from low molecular weight (LMW) subunits of glutenin. Among these, 13 peptides contained the cysteine residue C^b*, which is present in the repetitive sequence region of LMW subunits and which has been postulated to form intermolecular disulphide bonds. This peptide type represented 45% of the total radioactivity of isolated peptides. Three further peptides from LMW subunits representing 46% of radioactivity included cysteine C^x, which has also been proposed to form intermolecular disulphide bonds. Four peptides with 3.2% of radioactivity could be assigned to high molecular weight subunits (cysteines C^b, C^d, C^e, C^y) and four peptides (3.0% of radioactivity) to glutenin-bound %-gliadins (C^b*, C^w, C^z). One peptide (3.3% of radioactivity) corresponded to cysteine C^c from %-gliadins or LMW subunits. Altogether the cysteine residues in glutenins, which are usually linked by intermolecular disulphide bonds, contributed up to 95% of total radioactivity. The results obtained are in accordance with the effect of reduced GS on the rheological properties of dough, namely the weakening of dough by depolymerization of glutenin polymers via specific cleavage of intermolecular disulphide bonds.     

Relationship between gluten strength and pasta firmness in Indian durum wheats

Selected Indian durum wheats including five newly released varieties and seven landraces were studied for their grain quality, gluten strength (sodium dodecyl sulphate‐sedimentation and mixograph) and pasta making properties. Landraces were found to have good grain size, protein content, and gluten strength but they had lower test weight and semolina yield than released varieties. As protein composition affects gluten strength, landraces having combination of low molecular weight (LMW‐GS) with 5, 12, 15 and 19 linked to Gli‐B1 43.5 and high molecular weight (HMW‐GS) 2*, 14 + 15 provide a dough strength comparable with the 7 + 8 and LMW‐GS 2, 4, 6, 12, 15 and 19 (caa) allelic pattern, typically associated with good gluten strength. Landraces have rare combinations of glutenins and gliadins, which are not seen in commercial Indian durums, and in some cases, these rare alleles seem to favour good gluten strength and pasta firmness. Introduction of these alleles through breeding should improve the gluten strength and pasta making properties of Indian durum cultivars.     

Molecular Analysis of the Polymeric Glutenins with Gliadin‐Like Characteristics That Were Produced by Acid Dispersion of Wheat Gluten

We had earlier shown that the dispersion of wheat gluten in acetic acid solution conferred gliadin‐like characteristics to the polymeric glutenins. To elucidate the molecular behavior of its polymeric glutenins, the characteristics of gluten powder prepared from dispersions with various types of acid were investigated in this study. Mixograph measurements showed that the acid‐treated gluten powders, regardless of the type of acid, had dough properties markedly weakened in both resistance and elasticity properties, as though gliadin was supplemented. The polymeric glutenins extracted with 70% ethanol increased greatly in all acid‐treated gluten powders. Size exclusion HPLC and SDS‐PAGE indicated that the behavior of polymeric glutenins due to acid treatment was attributed to their subunit composition rich in high molecular weight glutenin subunit (HMW‐GS) and not their molecular size. The gluten prepared with the addition of NaCl in acid dispersion had properties similar to those of the control gluten. The results suggest that ionic repulsion induced by acid dispersion made the polymeric glutenins rich in HMW‐GS disaggregate, and therefore, act like gliadins.     

Wheat gluten: high molecular weight glutenin subunits--structure, genetics, and relation to dough elasticity

ABSTRACT:  Gluten proteins, representing the major protein fraction of the starchy endosperm, are predominantly responsible for the unique position of wheat amongst cereals. These form a continuous proteinaceous matrix in the cells of the mature dry grain and form a continuous viscoelastic network during the mixing process of dough development. These viscoelastic properties underline the utilization of wheat to prepare bread and other wheat flour based foodstuffs. One group of gluten proteins is glutenin, which consists of high molecular weight (HMW) and low molecular weight (LMW) subunits. The HMW glutenin subunits (HMW-GS) are particularly important for determining dough elasticity. The common wheat possesses 3 to 5 HMW subunits encoded at the Glu-1 loci on the long arms of group 1 chromosomes (1A, 1B, and 1D). The presence of certain HMW subunits is positively correlated with good bread-making quality. Glutamine-rich repetitive sequences that comprise the central part of the HMW subunits are actually responsible for the elastic properties due to extensive arrays of interchain hydrogen bonds. Genetic engineering can be used to manipulate the amount and composition of the HMW subunits, leading to either increased dough strength or more drastic changes in gluten structure and properties.     

Hearth bread baking quality of durum wheat varying in protein composition and physical dough properties

Thirty durum wheat genotypes from ten countries of origin were grown in field plots for two consecutive years. Three of the genotypes were γ‐gliadin 42 types and the remainder were γ‐gliadin 45 types. Among the γ‐gliadin 45 types, six high‐molecular‐weight glutenin subunit (HMW‐GS) patterns were identified: 6 + 8, 7 + 8, 7 + 16, 14 + 15, 20 and 2*, 20. All the γ‐gliadin 42 genotypes contained low amounts of unextractable polymeric protein (UPP) and exhibited low gluten index values and weak gluten properties. The γ‐gliadin 45 genotypes exhibited a wide range of UPP, gluten index and dough strength. HMW‐GS 20 genotypes were generally weak, whereas HMW‐GS 6 + 8 and 7 + 8 genotypes were generally strong. When baked by a lean formulation, long‐fermentation straight‐dough hearth bread process, the durum wheat genotypes exhibited a wide range of baking quality. Loaf volume and bread attributes were strongly correlated with UPP and gluten index. Some of the genotypes exhibited bread attributes and loaf volume equal or slightly superior to those of a high‐quality bread wheat flour. However, even the strongest durum wheat genotypes exhibited inferior fermentation tolerance to the bread wheat flour, as seen by a requirement for lower baking absorption during dough handling and more fragile dough properties when entering the oven. Among the HMW‐GS groups, HMW‐GS 7 + 8 and 6 + 8 exhibited the best and HMW‐GS 20 the poorest baking quality. Farinograph, alveograph and small‐scale extensigraph properties demonstrated that a combination of dough elasticity and extensibility was needed for superior durum wheat baking performance. Copyright © 2007 Society of Chemical Industry     

Relationship between glutenin subunit composition and gluten strength measurements in durum wheat

Durum breeders use a range of techniques in the development of new cultivars. An important selection criterion is the rheological properties of semolina dough and durum wheat breeders use this criterion in the development of new cultivars using a range of techniques. Because of the need to process large numbers of genotypes encountered in breeding programs, methods that are inexpensive, rapid, require small amounts of sample and that correlate with semolina quality are desirable. Using breeding material, this study investigated the relationship between the glutenin subunit composition and two traditional tests of gluten strength, gluten index (GI) and mixograph. Two sample sets of durum wheat breeding lines and cultivars, one grown in Canada (n = 229) and the other grown in Australia (n = 139) were analysed for GI, mixograph and both high molecular weight (HMW) and low molecular weight (LMW) glutenin subunits by SDS‐PAGE. Nine different HMW and 14 different LMW allelic combinations were found. In the Canadian set, the most frequent LMW alleles were aaa, bba, caa and cfa while in the Australian set, caa was predominant. For the HMW subunits, the most common allelic groups were Glu‐A1c/Glu‐B1d (null, 6 + 8) and Glu‐A1c/Glu‐B1b (null, 7 + 8) with fewer numbers of Glu‐A1c/Glu‐B1e (null, 20) in both sample sets. LMW subunits were more important contributors to gluten strength than HMW subunits with the rank for higher GI according to the LMW allele (Canadian set) being caa = aaa > bba and aaa > cfa while HMW subunits 6 + 8 = 7 + 8 > 20. Similarly, using the mixograph, strength ranking for the LMW alleles was aaa > cfa = bba and HMW subunit 20 gave poorer rheological properties. For some samples with a good LMW allelic group a low GI was observed and vice versa. Further characterisation of the protein composition in these samples showed the GI results could be explained by polymeric/monomeric (P/M), glutenin/gliadin (Glu/Gli) and HMW/LMW ratios or the proportion of unextractable polymeric protein. © Crown in the right of the State of New South Wales, Australia; and for the Department of Agriculture and Agri‐Food, Government of Canada, © Minister of Public Works and Government Services Canada 2005. Published for SCI by John Wiley & Sons, Ltd.     

Bread and durum wheat compared for antioxidants contents,and lipoxygenase and peroxidase activities

Potential beneficial components, including proteins, total phenolics, total flavonoids, carotenoids, tocopherols, and DPPH radical scavenging activity, were investigated in wholemeal of ten bread (T. aestivum L.) and ten durum (T. durum Desf.) novel wheat genotypes. In addition, the activity rate of lipoxygenase (LOX) and peroxidase (POD) enzymes implicated in the antioxidant metabolism was determined. The protein contnet and the antioxidant properties varied according to the two different wheat species, as well as, between the different bread and durum wheat genotypes themselves. The results indicated significant differences in proteins and antioxidant compounds between bread and durum wheat. Higher total proteins, wet gluten and antioxidants contents, combined with lower LOX and POD activities, point to a higher nutritive value of durum wheat than bread wheat.     

Disulphide bonds in wheat gluten: further cystine peptides from high molecular weight (HMW) and low molecular weight (LMW) subunits of glutenin and from γ-gliadins

Glutenin was prepared from gluten of the wheat variety Rektor by extraction of gliadin with aqueous ethanol. It was cleaved successively into soluble peptides by the enzymes trypsin and thermolysin. Separation of the peptide mixtures was performed by gel permeation chromatography (GPC) on Sephadex G25 and reversed phase high performance liquid chromatography (RP-HPLC) on ODS-Hypersil. Cystine peptides were detected by differential chromatography of the samples prior to and after reduction. After isolation by multi-step RP-HPLC, the cystine peptides were reduced. The resulting cysteine peptides were alkylated with 4-vinylpyridine, separated by RP-HPLC and sequenced by means of the Edman degradation. The isolated cystine peptides represented a considerable portion of the total cysteine in glutenin: four out of seven cysteine residues of HMW subunits, and eight out of nine cysteine residues of LMW subunits are documented by at least one cystine peptide. Most of the peptides corresponded to known sequences of gluten protein components. From the structures of some tryptic peptides, inter- and intramolecular disulphide bonds for HMW subunits of glutenin have been proven. Cystine peptides from the thermolytic digest have been assigned to LMW subunits of glutenin and toγ-gliadins. Other peptides have been closely related to partial sequences of these protein components. The results have allowed several conclusions about the arrangement of intra- and intermolecular disulphide bridges in gluten proteins.     

Emulsifying and Surface Properties of Wheat Gluten under Acidic Conditions

The solubility of wheat gluten was greatly improved at pH 4 or lower where it showed good emulsifying activity. This might be due to its high surface activity in the acidic pH range and the formation of a stable protein film surrounding the oil droplets. Among the major gluten proteins, gliadins showed higher surface activity than glutenins. The content of glutenins in the adsorbed protein film was higher than that of gliadins, and glutenins are likely to have been adsorbed more tightly than gliadins. These results suggest that gluten proteins exhibit complex behavior, such as adsorption/desorption/displacement/rearrangement during the adsorption process in a gluten‐stabilized emulsion.     

Studies on the protein composition and baking quality of einkorn lines

White flours from 23 einkorn breeding lines (assortment 1) and wholemeal flours from 24 einkorn lines (assortment 2) were investigated for their qualitative and quantitative protein compositions by means of a combined extraction/HPLC procedure. The HPLC patterns of the gliadin fractions enabled the differentiation of most einkorn samples. The absence of a group of γ-gliadins at the beginning of the γ-gliadin elution region was unique for einkorn compared to all other wheat species. Differences in the patterns of γ-gliadins allowed the classification of einkorns into four groups; a further subdivision of these groups was possible by the number of ω5-gliadins and the different patterns of α-gliadins and low-molecular-weight glutenin subunits. The total gluten protein (gliadins + glutenins) contents of einkorn flours were similar to or even higher than those of common wheat and spelt. Typical for einkorn flours was the extreme excess of gliadins over glutenins with ω5-gliadins being most abundant and high-molecular-weight glutenin subunits being extremely rare. Micro-tests on the mixing properties and baking performance of assortment 2 flours revealed remarkable differences. Dough development time was negatively correlated with the ratio of gliadins to glutenins and positively with the content of glutenins; bread volume was mainly dependent on the content of glutenins. In conclusion, the determination of the quantitative gluten protein compositions offers a reliable indication of the expected baking quality during the early stages of breeding.     

Sulfur in wheat gluten: In situ analysis by X-ray absorption near edge structure (XANES) spectroscopy

The sulfur containing gluten proteins largely determine the baking quality of wheat. In order to probe the speciation of sulfur, gluten proteins [gliadin, high molecular weight (HMW) and low molecular weight (LMW) subunits of glutenin], stored glutenin subunits as well as flour were investigated in situ by S K-edge X-ray near edge absorption structure (XANES) spectroscopy. The spectra confirmed the existence of disulfide bonds in oxidised (oxygen stream) glutenin subunits, supporting their significance for the formation of gluten networks. Additionally, glutenin subunits, which were stored under ambient air and temperature conditions, predominantly contained sulfur of higher oxidation states (sulfoxide, sulfonic acid). The disulfide state and also sulfoxide and sulfonic acid states were detected after reoxidation of glutenin subunits with potassium bromate.     

High‐molecular‐weight glutenin subunit composition of Pakistani hard white spring wheats grown at three locations for 2 years and its relationship with end‐use quality characteristics

Eleven Pakistani hard white spring wheat cultivars, along with one durum wheat and two hard white American‐grown wheat cultivars, were evaluated for their high‐molecular‐weight (HMW) glutenin subunit composition via sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS‐PAGE). The relationships among different quality characteristics and between these characteristics and HMW glutenin subunits were computed. Three to six HMW glutenin subunits were observed in Pakistani bread wheat cultivars. The presence of HMW glutenin subunits was not affected by growth locations or crop years. However, variations in intensities were observed. Correlations were noticed between certain HMW glutenin subunits and some quality attributes, such as protein, farinograph dough development time, farinograph water absorption, loaf volume and mixograph peak height. The presence of HMW glutenin subunit 20 in the older wheat cultivars C591 and C273, known for excellent chapati quality, indicated a possible relationship between this band and chapati quality. This observation will need to be confirmed by testing a larger number of wheat samples known to have characteristics for both good and poor chapati quality. © 2000 Society of Chemical Industry     

THE MOLECULAR STRUCTURE OF GELPROTEIN FROM BARLEY,ITS BEHAVIOUR IN WORT-FILTRATION AND ANALYSIS

Gelproteins from barley and malt play a major role in the lauter tun filtration. These proteins (called glutenin in wheat) are partly broken down during malting and then aggregate during mashing. These aggregates form a part of the upper layer of the spent grains (the ‘oberteig’). To obtain more insight into this mechanism the composition of gelproteins of different cultivars of barley were analysed using various electrophoretic techniques. From this work a model can be proposed in which the protein, like its counterpart in wheat consists of high molecular weight (HMW) subunits as a backbone and low molecular weight (LMW) subunits as side chains, joined by inter-and intra-molecular disulphide bonds. During malting the disulphide bonds are reduced and subunits are broken down by proteolysis. During mashing a complex is formed between residual gelprotein in the malt and the glutelins, which gives rise to an impenetrable layer on the spent grains. The quantity of gelprotein as analysed by high pressure liquid chromatography (HPLC) or densitometry of Sodium dodecyl sulphate polyacrylamide electrophoresis (SDS—PAGE) patterns of HMW subunits showed a negative relationship to the lauter tun filtration rate.     

Relationship between gluten degradation by Aelia spp and Eurygaster spp and protein structure

Gluten from wheat damaged by heteropterous insects loses its functionality after a short period of resting. In this study the properties of the gluten from damaged wheat are compared with that from sound wheat in order to understand the changes produced during incubation at 37 °C. The amounts of free thiol and amino groups were quantified, obtaining a marked increase of those groups during incubation of the damaged wheat. The thermal characterization of the damaged gluten showed a decrease in the denaturation temperature and a pronounced increase in the protein denaturation enthalpy after a short incubation, although the value of that enthalpy greatly dropped with a longer incubation period. The high‐molecular‐weight glutenin subunits (HMW‐GS) were rapidly hydrolysed while the low‐molecular‐weight glutenin subunits (LMW‐GS) showed a slower degradation. It seems that the HMW‐GS backbone was first hydrolysed, leading to a protein structure with higher thermal stability but, as the hydrolysis proceeded, a deeper degradation of the structure yielded a protein structure with lower denaturation enthalpy. The loss of gluten functionality results from complex changes in the gluten structure at the first and second level of the protein organization structure. Copyright © 2005 Society of Chemical Industry     

Role of gluten and its components in influencing durum wheat dough properties and spaghetti cooking quality

Protein is an important component of grain which affects the technological properties of durum wheat. It is known that the amount and composition of protein can influence dough rheology and pasta quality but the influence of the major classes of protein is not well documented. The influence of the various gluten components on dough and pasta properties was investigated. The protein composition of durum semolina was altered by either adding gluten fractions to a base semolina or preparing reconstituted flours with varying protein composition. The effects on semolina dough rheology and spaghetti texture were measured. Published methods to isolate relatively pure quantities (gram amounts) of glutenin, gliadin, high molecular and low molecular weight glutenin subunits were evaluated and modified procedures were adopted. Reconstituted flours with additional glutenin increased dough strength while additional gliadin and LMW‐GS decreased strength. These changes did not impact on spaghetti texture. Results from using the addition of protein fractions to a base semolina showed that gluten and glutenin addition increased the dough strength of a weak base semolina while gliadin addition weakened the base dough further. Addition of HMW‐GS greatly increased dough strength of the base while addition of LMW‐GS greatly reduced dough strength. Again, these affects were not translated into firmer pasta. Copyright © 2007 Society of Chemical Industry