Effect of Mechanical Dough Development on the Extractability of Wheat Storage Proteins from Bread Dough

Six wheat cultivars covering a range of quality parameters were mixed to various proportions of their optimum work input using mechanical dough development (MDD) mixers. Mixing and baking characteristics were determined and each dough was subsampled. The proteins were extracted for analysis by reversed-phase HPLC. Considerable protein mobilization appeared to occur during the MDD process, but the changes appeared to be cultivar-specific and did not indicate how mixing or baking behavior could be predicted. Protein content in extracted fractions was lowest for the weakest, poorest quality wheat but failed to consistently rank the stronger samples. Acetic acid insoluble protein level decreased with mixing as did extractable high molecular weight glutenin subunits. Gliadin protein level initially decreased with mixing before rising sharply with overmixing, while low molecular weight glutenin subunits displayed the reverse pattern. The rate of change of the extractability of the protein fractions with work input was greatest for the weakest samples and least for the stronger samples. However, when the protein quantity in the extractable fractions was plotted against relative work input, the rate of change of protein extractability did not appear to vary significantly between cultivars of different strengths.     

Optimized Methods for Incorporating Glutenin Subunits into Wheat Dough for Extension and Baking Studies

In order to study the functional properties of glutenin subunits added to a dough, they must be incorporated into the glutenin polymer. This requires partial reduction to open up the polymer, followed by oxidation to incorporate the added monomer into the polymer. Existing methods for incorporating glutenin subunits were suitable only for studies on mixing properties and needed to be modified for use in studies on extension and baking. A range of concentrations and of reaction times was therefore tested for both the reductant and the oxidant. In addition, mixing time as well as relaxation time before extension were varied. Extension curves and loaf heights were used to evaluate the treatments. Optimum conditions were developed that provided extension curves of normal dimensions but with altered shape. The conditions were reduction with 0.2 mg/mL of dithiothreitol (DTT) solution for 1 min followed by oxidation with 5 mg/mL of KIO₃ solution, then mixing the dough to 70% of the peak dough development time. For microbaking, the conditions of 2 mg/mL of DTT for 1 min, 2.5 mg/mL of KIO₃ for 5 min, and mixing the dough to peak development time allowed loaf height to be retained. The size distribution of the glutenin polymer was analyzed using size‐exclusion HPLC and field‐flow fractionation methods. This showed that the monomers were incorporated into the polymer and that polymer size was restored to control levels following reduction and oxidation.     

Effect of Transglutaminase on Properties of Glutenin Macropolymer and Dough Rheology

The effect of transglutaminase (TG) on glutenin macropolymer (GMP) properties could help to understand changes in bread quality. The aim of the present study was to analyze modifications in GMP and dough properties caused by TG addition. Transglutaminase introduced cross‐links to gluten proteins, mainly high molecular weight glutenins. This effect modified the protein structure and markedly increased dough strength. These changes in the structure of glutenins increased SDS solubility and decreased GMP content and GMP storage modulus. However, TG increased GMP particle size, notably at higher doses. TG affected rheological characteristics of dough in that increasing TG doses decreased tan δ, and increased G'. In all the studies conducted, the TG increased GMP polymer size, but contrary to what was expected, this increase did not involve an increase in GMP content. These results confirmed the effect of TG on dough quality and the great differences found with different TG doses.     

Effects of Wheat Bug (Eurygaster maura) Protease on Glutenin Proteins

Proteolytic degradation of 50% 1-propanol insoluble (50PI) glutenin of six common wheat cultivars by wheat bug (Eurygaster maura) protease was investigated using reversed-phase HPLC. Wheat at the milk-ripe stage was manually infested with adult bugs. After harvest, bug-damaged kernels were blended (2:1, kernel basis) with undamaged grain of the same cultivar. Samples of ground wheat were incubated in distilled water for different times (0, 30, 60, and 120 min). The incubated whole meal samples were subsequently freeze-dried and stored until analysis. The degree of proteolytic degradation of 50PI glutenin was determined based on the quantity of total glutenin subunits (GS), high molecular weight GS (HMW-GS), and low molecular weight GS (LMW-GS). For ground wheat samples incubated for ≥30 min, 50PI glutenin was substantially degraded as evidenced by a >80% decrease on average in total GS, HMW-GS, and LMW-GS. Some cultivars showed different patterns of glutenin proteolysis as revealed by differences in the ratios of HMW-GS to LMW-GS between sound and bug-damaged samples; a significant decrease in this ratio was found for four cultivars. This evidence, combined with other observations, indicated that there were intercultivar differences in polymeric glutenin resistance to the protease of the wheat bug Eurygaster maura. While the nature of this resistance is unknown, it should be possible to select and develop wheat cultivars with improved tolerance for wheat bug damage. Propanol insoluble glutenin, which corresponds to relatively large glutenin polymers, appears to be an excellent quantitative marker for this purpose.     

Effects of High and Low Molecular Weight Glutenin Subunits on Rheological Dough Properties and Breadmaking Quality of Wheat

High molecular weight (HMW) or low molecular weight (LMW) subunits of different chemical state (reduced, reoxidized with KBrO₃, or KIO₃) or gliadins were added in 1% amounts to a base flour of the wheat cultivar Rektor and mixed with water. The corresponding doughs were then characterized by microscale extension tests and by microbaking tests and were compared to doughs from the base flour without additives. The maximum resistance of dough was strongly increased by HMW subunits in a reduced state and by HMW subunits reoxidized with KBrO₃. A moderate increase of resistance was caused by HMW subunits reoxidized with KIO₃ and by LMW subunits reoxidized with KBrO₃ or KIO₃. This resistance was strongly lowered by LMW subunits in a reduced state and by gliadins. The extensibility of dough was significantly increased only by gliadins and reduced HMW subunits; HMW subunits reoxidized with KBrO₃ had no effect, and all other fractions had a decreasing effect. In particular, glutenin subunits reoxidized with KIO₃ induced marked decrease of extensibility, resulting in bell‐shaped curve extensigrams, which are typical for plastic properties. The effect of reoxidized mixtures (2:1) of HMW and LMW subunits on maximum resistance depended on the oxidizing agent and on the conditions (reoxidation separated or together); extensibility was generally decreased. Bread volume was increased by addition of HMW subunits (reduced or reoxidized with KBrO₃) and decreased by LMW subunits (reoxidized with KBrO₃ or KIO₃) and by a HMW‐LMW subunit mixture (reoxidized with KBrO₃). The volume was strongly decreased by addition of reduced LMW subunits. A high bread volume was related to higher values for both resistance and extensibility.     

Synergistic and Additive Effects of Three High Molecular Weight Glutenin Subunit Loci. I. Effects on Wheat Dough Rheology

The high molecular weight glutenin subunits (HMW‐GS) play an important role in governing the functional properties of wheat dough. To understand the role of HMW‐GS in defining the basic and applied rheological parameters and end‐use quality of wheat dough, it is essential to conduct a systematic study where the effect of different HMW‐GS are determined. This study focuses on the effect of HMW‐GS on basic rheological properties. Eight wheat lines derived from cvs. Olympic and Gabo were used in this study. One line contained HMW‐GS coded by all three loci, three lines were each null at one of the loci, three lines were null at two of the loci and one line null at all three loci. The flour protein level of all samples was adjusted to a constant 9% by adding starch. In another set of experiments, in addition to the flour protein content being held at 9%, the glutenin‐to‐gliadin ratio was maintained at 0.62 by adding gliadin. Rheological properties such as elongational, dynamic, and shear viscometric properties were determined. The presence of Glu‐D1 subunits (5+10) made a significantly larger contribution to dough properties than those encoded by Glu‐B1 (17+18), while subunit 1, encoded by Glu‐A1, made the least contribution to functionality. Results also confirmed that HMW‐GS contributed to strength and stability of dough.     

Comparison of Work Input Requirement on Laboratory-Scale and Industrial-Scale Mechanical Dough Development Mixers

The use of a laboratory-scale mixer for predicting the mixing requirement of flours in an industrial-scale mixer was investigated by measuring the work input required to mix a range of flours to peak consistency on both a laboratory-scale and an industrial-scale mechanical dough development (MDD) mixer. The industrial mixer used was a Tweedy-type mixer, and the mixing optimum was determined using a probe that sensed changes in dough consistency. Work input was estimated from mixer motor power, taking into account expected motor and drive chain losses, and from dough temperature rise measurements. The laboratory mixer used twin flat-bladed rotors; mixing optimum and work input were determined from the torque measurement. Work inputs from both mixers were highly correlated (r² = 0.88) but with a large offset (the industrial mixer requiring more work to develop the dough). The two methods of measuring industrial mixer work inputs gave slightly different results leading to uncertainty as to the actual work given by the industrial mixer. Farinograph mixing properties were less well correlated with industrial-scale work input requirement than the laboratory-scale MDD mixer.     

Changes in SDS Solubility of Glutenin Polymers During Dough Mixing and Resting

An online coupling of high‐performance size‐exclusion chromatography (HPSEC) combined with multiangle laser‐light scattering (MALLS) and a reverse‐phase HPLC procedure were used to characterize and reveal the polydispersity of the glutenin polymers of doughs during mixing and resting. Experiments involved doughs prepared from several samples of a common French wheat cultivar (Soissons) differing in total amount of SDS‐unextractable glutenin polymers. During dough mixing, the amounts, size distribution of protein, and glutenin subunit composition within the SDS‐unextractable polymers changed. However, the major changes in SDS‐unextractable glutenin content and size distribution occurred before the peak mixing time (MT) was reached, whereas detectable changes in subunit composition also occurred after the peak MT. Even if sonication, which was used to solubilize the total wheat glutenin, can narrow the glutenin size distribution, HPSEC‐MALLS revealed a close relationship between the SDS solubility of the glutenin polymers and size distribution, confirming a depolymerization and repolymerization hypothesis. During the depolymerization of the SDS‐unextractable polymers, glutenin subunits were released in nonrandom order, which indicated that the polymers have a hierarchical structure. Some HMW glutenin subunits (HMW‐GS), especially 1D×5, were particularly resistant to the depolymerization mechanism. This suggested that the subunit plays a major role in forming the backbone of the SDS‐unextractable polymers, consistent with the potential to form branched structure. These studies suggest that the SDS‐unextrac‐table polymers in flours have a well‐ordered structure that can be modified by dough mixing and resting.     

Effects of Mixing Conditions on Pasta Dough Development and Biochemical Changes

Mixing of commercial durum wheat semolina with water was performed under different conditions in a Brabender micromixer equipped with pastamaking shafts. Semolina filling of the mixing chamber was 30.4–42.9% (v/v), shaft speed was 10–110 rpm, temperature was 10–40°C, and hydration level was 47–52.5% (db). The blend of water and semolina evolved from individualized hydrated particles (HP) to a dough product (DP) as a function of these conditions. Torque values (T) and the specific mechanical energies (SME) were recorded during mixing as a function of time. Terms from these curves were defined to characterize the mixing process: t_o (starting time of dough development), t_d (time to reach the maximum dough consistency), T_m (mean torque value after dough development), and SME_f (total energy applied to the dough during mixing). Transformation of HP into DP and the mixing temperature were the main parameters affecting t_o, t_d, T_m, and SME_f. Protein aggregate distribution was measured by size-exclusion HPLC, protein solubility in 0.01N acetic acid, free -SH content, soluble arabinoxylans, reducing sugars, ferulic acid, carotenoid content, and oxidase activities to characterize the biochemical changes that occurred during pasta dough formation. DP was characterized by lower amounts of insoluble glutenin aggregates, lower protein solubility in dilute acetic acid, lower free -SH content, ferulic acid, carotenoid content, and lower oxidoreductase activities as compared to HP. Once the dough was developed, the effects of mixing speed, temperature, or hydration level on the biochemical composition of the blend were null or low compared to the modifications that were observed when the blends changed from HP to DP. The t_o and SME_f were the most significant parameters in characterizing the pasta dough mixing process in relation to biochemical changes.     

Synergistic and Additive Effects of Three High Molecular Weight Glutenin Subunit Loci. II. Effects on Wheat Dough Functionality and End‐Use Quality

Understanding the relationship between basic and applied rheological parameters and the contribution of wheat flour protein content and composition in defining these parameters requires information on the roles of individual flour protein components. The high molecular weight glutenin subunit (HMW‐GS) proteins are major contributors to dough strength and stability. This study focused on eight homozygous wheat lines derived from the bread wheat cvs. Olympic and Gabo with systematic deletions at each of three HMW‐GS encoding gene loci, Glu‐A1, Glu‐B1, and Glu‐D1. Flour protein levels were adjusted to a constant 9% by adding starch. Functionality of the flours was characterized by small‐scale methods (2‐g mixograph, microextension tester). End‐use quality was evaluated by 2‐g microbaking and 10‐g noodle‐making procedures. In this sample set, the Glu‐D1 HMW‐GS (5+10) made a significantly larger contribution to dough properties than HMW‐GS coded by Glu‐B1 (17+18), while subunit 1 coded by Glu‐A1 made the smallest contribution to functionality. These differences remained after removing variations in glutenin‐to‐gliadin ratio. Correlations showed that both basic rheological characteristics and protein size distributions of these flours were good predictors of several applied rheological and end‐use quality tests.     

Effects of Temperature and Mechanical Input on Semisweet Biscuit (Cookie) Quality and Dough Characteristics

The effects of specific mechanical energy (SME) and dough temperature at the end of mixing (T_f) on semisweet biscuit dough characteristics and biscuit quality were studied using an experimental mixer fitted with monitoring devices. The fluid circulating in the double jacket of the mixing bowl was regulated at variable temperatures and mixed dough samples were prepared at T_f of 23, 30, and 37°C for three levels of SME input (20, 60 and 120 kJ/kg). Correlation analysis showed that semisweet biscuit length and thickness were independent quality parameters, influenced respectively by the T_f of dough and SME. Biscuit thickness and volume increased with SME input, but SME had no significant influence on the physicochemical characteristics of the dough. Biscuit length was related to the density and stickiness of the dough and to rheological behavior as assessed by fundamental and empirical measurements. A rise in dough temperature >35°C induced a dramatic increase in viscoelastic properties, leading to biscuit shrinkage. The increase of dough density with T_f seemed to be related to the melting of solid fat in the dough recipe. Melting of fat during mixing could also be a source of viscoelastic changes in the dough at T_f.     

Composition of HMW and LMW Glutenin Subunits and Their Effects on Dough Properties,Pan Bread,and Noodle Quality of Chinese Bread Wheats

Knowledge of composition of high molecular weight glutenin subunits (HMW‐GS) and low molecular weight glutenin subunits (LMW‐GS) and their associations with pan bread and noodle quality will contribute to genetically improving processing quality of Chinese bread wheats. Two trials including a total of 158 winter and facultative cultivars and advanced lines were conducted to detect the allelic variation at Glu‐1 and Glu‐3 loci by SDS‐PAGE electrophoresis and to understand their effects on dough properties, pan bread, and dry white Chinese noodle (DWCN) quality. Results indicate that subunits/alleles 1 and null at Glu‐A1, 7+8 and 7+9 at Glu‐B1, 2+12 and 5+10 at Glu‐D1, alleles a and d at Glu‐A3, and alleles j and d at Glu‐B3 predominate in Chinese germplasm, and that 34.9% of the tested genotypes carry the 1B/1R translocation (allelic variation at Glu‐D3 was not determined because no significant effects were reported previously). Both variations at HMW‐GS and LMW‐GS/alleles and loci interactions contribute to dough properties and processing quality. For dough strength related traits such as farinograph stability and extensigraph maximum resistance and loaf volume, subunits/alleles 1, 7+8, 5+10, and Glu‐A3d are significantly better than those of their counterpart allelic variation, however, no significant difference was observed for the effects of d, b, and f at Glu‐B3 on these traits. For extensigraph extensibility, only subunits 1 and 7+8 are significantly better than their counterpart alleles, and alleles d and b at Glu‐B3 are slightly better than others. For DWCN quality, no significant difference is observed for HMW‐GS at Glu‐1, and Glu‐A3d and Glu‐B3d are slightly better than other alleles. Glu‐B3j, associated the 1B/1R translocation, has a strong negative effect on all quality traits except protein content. It is recommended that selection for subunits/alleles 1, 7+8, 5+10, and Glu‐A3d could contribute to improving gluten quality and pan bread quality. Reducing the frequency of the 1B/1R translocation will be crucial to wheat quality improvement in China.     

Effect of Amaranthus and Buckwheat Proteins on Wheat Dough Properties and Noodle Quality

Isoelectric protein concentrates (IPC) were prepared from one buckwheat (Fagopyrum esculentum) and five Amaranthus genotypes. Their effect on the mixing properties of a wheat flour was studied. Mixograph and dynamic oscillatory measurements showed significant increases in dough strength with the addition of 2 and 4% IPC, correlated to the water-insoluble fraction level of the IPC. The same IPCs were used at 2% level to supplement a wheat flour in making Chinese dry noodles. Measurable changes in both the raw and cooked noodle color were observed, and the change caused by addition of buckwheat IPC was substantial. Some of the IPCs caused an increase in cooking loss and only one caused an increase in weight, while increase in volume of the cooked noodles was not significantly affected. The changes in the rheological properties of cooked noodles due to addition of IPCs were measured. Overall, their effects were favorable, but the changes were statistically significant in only a few cases. The substantial dough-strengthening effect of the IPCs was hence not effectively translated into improved cooked noodle quality, and possible reasons for this are discussed.     

Immunocytochemical Localization of Gluten Proteins Uncovers Structural Organization of Glutenin Macropolymer

The content and composition of the disulfide‐bonded glutenin macropolymer has been shown to influence dough properties, although its structural organization is poorly characterized. The structure of the glutenin macropolymer in dough was studied using an immunolocalization transmission electron microscopy (TEM) technique by localizing gliadins, low molecular weight glutenin subunits (LMW‐GS), and high molecular weight glutenin subunits (HMW‐GS) in sections of dough using antibody probes selective for each of the three classes of gluten polypeptides. Distinct differences in the distribution patterns of gliadins, LMW‐GS, and HMW‐GS were observed, which suggests that proteins have different roles in the structural organization of the gluten matrix. On the basis of the observed distribution of the proteins in dough, it is speculated that gliadins, which are randomly distributed as individual particles, fill space within the glutenin macropolymer; LMW‐GS, which are present as clusters, are speculated to form aggregated branch structures; and HMW‐GS, which are present as chains, are speculated to form a network from which the LMW‐GS branches are formed. Changes in the distribution of gliadins, LMW‐GS, and HMW‐GS in dough during mixing were also noted. Such an arrangement supports previous biochemical evidence which has established that gliadins, LMW‐GS, and HMW‐GS have specific roles in the structural organization of the glutenin macropolymer in doughs.     

Association of Glutenin Subunit Composition and Dough Rheological Characteristics with Cookie Baking Properties of Soft Wheat Cultivars

The effect of flour type and dough rheology on cookie development during baking was investigated using seven different soft winter wheat cultivars. Electrophoresis was used to determine the hydrolyzing effects of a commercial protease enzyme on gluten protein and to evaluate the relationships between protein composition and baking characteristics. The SDS‐PAGE technique differentiated flour cultivars based on the glutenin subunits pattern. Electrophoresis result showed that the protease degraded the glutenin subunits of flour gluten. Extensional viscosities of cookie dough at all three crosshead speeds were able to discriminate flour cultivar and correlated strongly and negatively to baking performance (P < 0.0001). The cookie doughs exhibited extensional strain hardening behavior and those values significantly correlated to baking characteristics. Of all rheological measurements calculated, dough consistency index exhibited the strongest correlation coefficient with baking parameters. The degradation effects of the protease enzyme resulted in more pronounced improvements on baking characteristics compared with dough rheological properties. Stepwise multiple regression showed that the dough consistency index, the presence or absence of the fourth (44 kDa) subunit in LMW‐GS and the fifth subunit (71 kDa) subunit in HMW‐GS were predominant parameters in predicting cookie baking properties.     

The Combination of Rhizopus chinensis Lipase and Transglutaminase Affects the Rheology and Glutenin Macropolymer Properties of Frozen Dough

The combination of Rhizopus chinensis lipase (RCL) and transglutaminase (TG) was previously reported to improve the quality of frozen dough bread. In this study, the effects of RCL, TG, and their combination on the modification of glutenin macropolymer (GMP) and rheological properties of dough during frozen storage were investigated. Frozen storage changed both GMP and rheology properties of dough. TG treatment significantly decreased the ratio of high‐molecular‐weight glutenin subunits to low‐molecular‐weight glutenin subunits and GMP content in fresh dough, and GMP particle size increased. The effect of RCL on GMP properties was not significant, but its combination with TG dramatically increased the proportion of the larger particles and weighted average volume (D_4.3) in GMP. The treatment with the enzyme combination could have inhibited the depolymerization of GMP, which slowed down the decrease rate of some parameters such as GMP content, proportion of larger particles, D_4.3, and release of free amino and thiol groups during frozen storage. The modification of GMP properties by enzyme treatment weakened the effect of the freezing process on rheological properties of dough, especially TG treatment and its combination with RCL. Correlation between GMP particle size and dough properties (dough tensile force and elastic modulus) after freezing and enzyme treatment were confirmed.     

Effects of Genotype and Environment on Glutenin Polymers and Breadmaking Quality

Six genotypes of hard red spring (HRS) wheat were grown at seven environments in North Dakota during 1998. Effects of genotype and environment on glutenin polymeric proteins and dough mixing and baking properties were examined. Genotype, environment, and genotype‐by‐environment interaction all significantly affected protein and dough mixing properties. However, different protein and quality measurements showed differences for relative influences of genotype and environment. Total flour protein content and SDS‐soluble glutenin content were influenced more by environmental than genetic factors, while SDS‐insoluble glutenin content was controlled more by genetic than environmental factors. Significant genotypic and environmental effects were found for the size distribution of SDS‐soluble glutenins and between SDS‐soluble and SDS‐insoluble glutenins as well as % SDS‐insoluble glutenins. With increased flour protein content, the proportions of monomeric proteins and SDS‐insoluble glutenin polymers appeared to increase, but SDS‐soluble glutenins decreased. Flour protein content and the size distribution between SDS‐soluble and SDS‐insoluble glutenin polymers were significantly correlated with dough mixing properties. Environment affected not only total flour protein content but also the content of different protein fractions and size distributions of glutenin polymers, which, in turn, influenced properties of dough mixing. Flour protein content, % SDS‐insoluble glutenin polymers in flour, and ratio of SDS‐soluble to SDS‐insoluble glutenins all were highly associated with dough mixing properties and loaf volume.     

Controlled Stepwise Reduction of Disulfide Bonds and Heat-Induced Modification of Wheat Dough Proteins

A reducing solution of 2-mercaptoethanol and its oxidized form 2-hydroxyethyl disulfide, whose variable concentrations set variable disulfide reduction potentials, was applied to progressively reduce the disulfide bonds of proteins extracted from doughs made from Meneba and Robin Hood flour. Several dough proteins had disulfide bonds stronger than those of other dough proteins. A SDS-sedimentation method was applied to monitor the baking of dough into bread. Dough proteins susceptible to heat (baking) were studied by SDS-fractionation, extraction with reducing alcoholic solution, SDS-PAGE, and N-terminal protein sequencing. High or low molecular weight glutenins, α, β, and γ-gliadins, α-amylase inhibitor, and α-amylase trypsin inhibitor were identified among the dough proteins modified by heat (as shown by reduced solubility in aqueous-SDS solution). The heat-induced modification of the gliadins and glutenins might contribute to the coagulation of dough proteins, while the heat-induced modification of the amylase or trypsin inhibitors might contribute to the regulation of endogenous or exogenous amylolytic or proteolytic activities in dough or bread.     

Structural Modifications of Gluten Proteins in Strong and Weak Wheat Dough During Mixing

The network‐forming attributes of gluten have been investigated for decades, but no study has comprehensively addressed the differences in gluten network evolution between strong and weak wheat types (hard and soft wheat). This study monitored changes in SDS protein extractability, SDS‐accessible thiols, protein surface hydrophobicity, molecular weight distribution, and secondary structural features of proteins during mixing to bring out the molecular determinants of protein network formation in hard and soft wheat dough. Soft wheat flour and dough exhibited greater protein extractability and more accessible thiols than hard wheat flour and dough. The addition of the thiol‐blocking agent N‐ethylmaleimide (NEM) resulted in similar results for protein extractability and accessible thiols in hard and soft wheat samples. Soft wheat dough had greater protein surface hydrophobicity than hard wheat and exhibited a larger decrease in surface hydrophobicity in the presence of NEM. Formation of high‐molecular‐weight (HMW) protein in soft wheat dough was primarily because of formation of disulfides among low‐molecular‐weight (LMW) proteins, as indicated by the absence of changes in protein distribution when NEM was present, whereas in hard wheat dough the LMW fraction formed disulfide interaction with the HMW fraction. Fourier transform infrared spectroscopy indicated formation of β‐sheets in dough from either wheat type at peak mixing torque. Formation of β‐sheets in soft wheat dough appears to be driven by hydrophobic interactions, whereas disulfide linkages stabilize secondary structure elements in hard wheat dough.     

Effect of Multiple Substitution of Glutenin and Gliadin Proteins on Flour Quality of Canada Prairie Spring Wheat

The effect of genetic substitution of two to four glutenin and gliadin subunits from a Canada Prairie Spring (CPS) cv. Biggar BSR into Alpha 16, another CPS wheat line, was studied for rheological and baking quality. Results from double substitution showed that the presence of a gliadin component from Biggar BSR (BGGL) and low molecular weight glutenin subunit 45 (LMW 45) contributed to improved dough strength characteristics. Presence of BGGL in combination with high molecular weight glutenin subunit 1 (HMW 1) or 17+18 (HMW 17+18) also showed improved dough strength over control Alpha lines. When three or four protein subunits were substituted, even though improved quality performance was observed, it was associated with the negative effect of lowered flour water absorptions in spite of similar protein contents. The study confirms that LMW glutenins, as well as gliadins, play an important role along with HMW glutenins in wheat flour quality. CPS wheat lines with improved dough strength properties can be selected from the double substitution lines with the combination of BGGL/LMW 45 and BGGL/HMW 1.