Impact of Bran Addition on Water Properties and Gluten Secondary Structure in Wheat Flour Doughs Studied by Attenuated Total Reflectance Fourier Transform Infrared Spectroscopy

The aim of this work was to elucidate the underlying physical mechanism(s) by which bran influences whole grain dough properties by monitoring the state of water and gluten secondary structure in wheat flour and bran doughs containing 35–50% moisture and 0–10% added bran. The system was studied with attenuated total reflectance (ATR) FTIR spectroscopy. Comparison of the OH stretch band of water in flour dough with that in H₂O‐D₂O mixtures having the same water content revealed the formation of two distinct water populations in flour dough corresponding to IR absorption frequencies at 3,600 and 3,200 cm^–1. The band intensity at 3,200 cm^–1, which is related to water bound to the dough matrix, decreased and shifted to lower frequencies with increasing moisture content of the dough. Addition of bran to the dough caused redistribution of water in the flour and bran dough system, as evidenced by shifts in OH stretch frequency in the 3,200 cm^–1 region to higher frequencies and a reduction in monomeric water (free water). This water redistribution affected the secondary structure of gluten in the dough, as evidenced by changes in the second‐derivative ATR‐FTIR difference spectra in the amide I region. Bran addition caused an increase in β‐sheet content and a decrease in β‐turn (β‐spiral) content. However, this bran‐induced transconformational change in gluten was more significant in the 2137 flour dough than in Overley flour dough. This study revealed that when bran is added to flour dough, water redistribution among dough components promotes partial dehydration of gluten and collapse of β‐spirals into β‐sheet structures. This transconformational change may be the physical basis for the poor quality of bread containing added bran.     

Changes in Secondary Protein Structures During Mixing Development of High Absorption (90%) Flour and Water Mixtures

Wheat flour and water mixtures at 90% absorption (dry flour basis) prepared at various mixing times were examined using Fourier transform infrared (FT‐IR) reflectance spectroscopy. Spectra were obtained using a horizontal attenuated total reflection (ATR) trough plate. The apparent amount of protein and starch on the surface of the dough varied with mixing time but this was likely due to the polyphasic nature of the substrate and the changing particle distributions as the batter matrix was developed. Deconvolution of the Amide I band revealed contributions from alpha helical, β‐turn, β‐strand, β‐sheet, and random conformations. The ratio of β‐sheet to nonsheet conformations reached its greatest value about the same time that the mixture was most effectively separated by a laboratory‐scale, cold‐ethanol‐based method but before the peak consistency measured by a microfarinograph.     

Description of Chemical Changes Implied During Bread Dough Mixing by FT‐ATR Mid‐Infrared Spectroscopy

The aim of the present study was to investigate the ability of mid‐infrared (MIR) spectroscopy to identify physicochemical changes in the French bread dough mixing process. An ATR FT‐MIR spectrometer at 4000–800 cm^–1 was used. The MIR spectra collections recorded during mixing were analyzed after standard normal variate using principal component analysis (PCA) and after second‐derivative treatment. The results were interpreted in terms of chemical changes involved in dough development and more particularly in terms of secondary structural protein changes (amide III). The loading spectrum associated with principal component 1 (PC1) allows three MIR wave number regions of variations (3500–3000, 1700–1200, and 1200–800 cm^–1) to be identified. The loading spectrum associated with PC1 describes an increase in the relative protein band intensities and a decrease in relative water and starch band intensities. The variation during bread dough mixing time of the different amide III bands identified after the second‐derivative show that α‐helical, β‐turn, and β‐sheet structures increase while random coil structure decreases, suggesting that the gluten structure is becoming a more ordered structure. The MIR mixing time identified as being the maximum scores value on the PC1 scores plots was associated with the time at which the dough apparent torque begin to collapse, suggesting that the MIR spectroscopy could monitor bread dough development.     

Polymer Conformation Structure of Wheat Proteins and Gluten Subfractions Revealed by ATR‐FTIR

The polymer conformation structure of gluten extracted from a Polish wheat cultivar, Korweta, and gluten subfractions obtained from 2 U.K. breadmaking and biscuit flour cultivars, Hereward and Riband, was investigated using attenuated total reflectance Fourier transform infrared spectroscopy (ATR‐FTIR). The results showed the conformation of proteins varied between flour, hydrated flour, and hydrated gluten. The β‐sheet structure increased progressively from flour to hydrated flour and to hydrated gluten. In hydrated gluten protein fractions comprising gliadin, soluble glutenin, and gel protein, β‐sheet structure increased progressively from soluble gliadin and glutenin to gluten and gel protein; β‐sheet content was also greater in the gel protein from the breadmaking flour Hereward than the biscuit flour Riband.     

Structural Modification of Gluten Proteins in Strong and Weak Wheat Dough as Affected by Mixing Temperature

The effects of temperature (≥25°C) on dough rheological properties and gluten functionality have been investigated for decades, but no study has addressed the effect of low temperature (<30°C) on gluten network attributes in flours with strong and weak dough characteristics. This study monitored changes in protein extractability in the presence and absence of reducing agents, the contents of readily accessible and SDS‐accessible thiols, and the secondary structural features of proteins in doughs from commercial hard wheat flour (HWF) and soft wheat flour (SWF) mixed at 4, 15, and 30°C. SWF mixed at 4 and 15°C showed similar mixing properties as HWF mixed at 30°C (which is the standard temperature). The effect of mixing temperature is different at the molecular level between the two flours studied. Protein features of HWF did not change as mixing temperature decreased, with the only exception being an increase in SDS‐accessible thiols. Decreasing mixing temperature for SWF caused an increase in SDS protein solubility and SDS‐accessible thiols as well as an increase in β‐turn structures at the expense of β‐sheet structures. Thus, noncovalent interactions appear to drive protein network at low temperatures (4 and 15°C), whereas covalent interactions dominate at standard mixing temperature (30°C) in doughs from both flours.     

Physicochemical Properties of Corn Starch Selectively Oxidized with 2,2,6,6‐Tetramethyl‐1‐Piperidinyl Oxoammonium Ion

This study was conducted to examine the characteristics of oxidation reaction on the primary alcohol groups in corn starch, when 2,2,6,6‐tetramethyl‐1‐piperidinyl oxoammonium ion (TEMPO) was used, and to determine the optimum conditions for the preparation of oxidized corn starch (OCS). Applicability of the OCS in the food system was also investigated. The effects of TEMPO, sodium bromide (NaBr), and temperature on oxidation reaction time, yield, and selectivity for primary alcohol groups were examined by response surface methodology. As the temperature and the levels of TEMPO and NaBr increased, reaction time and selectivity decreased. Yield decreased with increased NaBr and selectivity decreased with the increased temperature and NaBr. Selectivity increased with higher TEMPO levels up to a certain point and then decreased. Optimum levels of TEMPO, NaBr, and temperature for the preparation of OCS were determined as 0.6 mM/100 mM of anhydroglucose unit (AGU), 45 mM/100 mM AGU, and 7°C, respectively. Water binding capacity, emulsion stability, and viscosity of starch increased significantly by oxidation. Corn starch containing OCS had decreased initial pasting temperature, setback, and gelatinization and retro‐gradation enthalpy (ΔH). Corn starch gel containing OCS showed delayed staling during storage.     

1H Nuclear Magnetic Resonance (NMR) and Differential Scanning Calorimetry (DSC) Studies of Water Mobility in Dough Systems Containing Barley Flour

This study used ¹H nuclear magnetic resonance (NMR) spin‐spin relaxation time (T₂) and differential scanning calorimetric (DSC) measurements of unfreezable water content (UFW), to assess water behavior in freshly prepared (25°C), refrigerator‐stored (4°C, one day), or freezer‐stored (–35°C, one day) doughs containing 5, 10, or 30% whole grain, air‐classified β‐glucan‐diminished, and air‐classified β‐glucan‐enriched (BGB‐E) barley flours. Three populations of water were detected by NMR, depending on moisture content of dough, namely, tightly (T₂₁, 2–5 msec), less tightly (T₂₂, 20–50 msec), and weakly (T₂₃, 100–200 msec) bound water. T₂₂ peak was always detectable, and T₂₂ peak time linearly correlated to moisture content of dough in a range of 0.7–2.0 g/g db (r = 0.99, P < 0.05). Freezer storage showed less effect on water mobility in dough compared with refrigerator storage, whereas cooking and cool storage of cooked dough significantly decreased the water mobility (P < 0.05). Adding barley flour steadily decreased the water mobility in dough, and the reduction was more significant with adding BGB‐E (P < 0.05). Immobile water content was calculated by extrapolating T₂₂ peak time versus total moisture content in dough and significantly correlated to the UFW content measured by DSC (r = 0.72, P < 0.05).     

Bulk Carbohydrate Grain Filling of Barley β‐Glucan Mutants Studied by 1H HR MAS NMR

Temporal and genotypic differences in bulk carbohydrate accumulation in three barley genotypes differing in the content of mixed linkage β‐(1→3),(1→4)‐D‐glucan (β‐glucan) and starch were investigated using proton high‐resolution, magic angle spinning, nuclear magnetic resonance (¹H HR MAS NMR) during grain filling. For the first time, ¹H HR MAS NMR spectra of flour from immature barley seeds are analyzed. Spectral assignments are made using two‐dimensional (2D) NMR methods. Both α‐ and β‐glucan biosynthesis were characterized by inspection of the spectra as well as by calibration to the reference methods for starch and β‐glucan content. Starch was quantified with very good calibrations to the α‐(1→4) peak (5.29–5.40 ppm) and the region 3.67–3.83 ppm covering starch glycopyranosidic protons from H5 and H6. In contrast, the spectral inspection of the β‐anomeric region 4.45–4.85 ppm showed unexpected lack of intensity in the high β‐glucan mutant lys5f at seed maturity, resulting in poor calibration to reference β‐glucan content. We hypothesize that the lack of β‐glucan signal in lys5f indicates partial immobilization of the β‐glucan that appears to be either genotypic dependent or water/β‐glucan ratio dependent.     

Wheat Gluten Polymer Structures: The Impact of Genotype,Environment, and Processing on Their Functionality in Various Applications

For a number of applications, gluten protein polymer structures are of the highest importance in determining end‐use properties. The present article focuses on gluten protein structures in the wheat grain, genotype‐ and environment‐related changes, protein structures in various applications, and their impact on quality. Protein structures in mature wheat grain or flour are strongly related to end‐use properties, although influenced by genetic and environment interactions. Nitrogen availability during wheat development and genetically determined plant development rhythm are the most important parameters determining the gluten protein polymer structure, although temperature during plant development interacts with the impact of the mentioned parameters. Glutenin subunits are the main proteins incorporated in the gluten protein polymer in extracted wheat flour. During dough mixing, gliadins are also incorporated through disulfide‐sulfhydryl exchange reactions. Gluten protein polymer size and complexity in the mature grain and changes during dough formation are important for breadmaking quality. When using the gluten proteins to produce plastics, additional proteins are incorporated in the polymer through disulfide‐sulfhydryl exchange, sulfhydryl oxidation, β‐eliminations with lanthionine formation, and isopeptide formation. In promising materials, the protein polymer structure is changed toward β‐sheet structures of both intermolecular and extended type and a hexagonal close‐packed structure is found. Increased understanding of gluten protein polymer structures is extremely important to improve functionality and end‐use quality of wheat‐ and gluten‐based products.     

Effect of Transglutaminase,Citrate Buffer,and Temperature on a Soft Wheat Flour Dough System

Transglutaminase (TGase) can improve the functional characteristics of proteins by introducing covalent bonds inter‐ or intrachains. Temperature and pH interfere with the protein structure and the catalytic activity of enzymes. Because these three factors can act synergistically, TGase, citrate buffer, and temperature were evaluated for their effects on the rheological and chemical changes in low‐protein wheat flour dough. Dough strength, measured by microextension test, significantly increased with increasing levels of TGase (8 U/g of protein), with changes in pH of the citrate buffer (pH 6.5), and by the effect of interaction between these factors. The same trend was observed in the size‐exclusion HPLC measurements, indicating that these two parameters have the effect of increasing gluten protein aggregation. Temperature had a significant effect on dough extension, measured by microextension test. The changes in secondary structure of gluten protein were investigated by FTIR second‐derivative spectra (amide I region, 1,600–1,700 cm⁻¹) and showed an increase in β‐sheet structures initiated by TGase, citrate buffer pH, and their interaction.     

Effects of Secondary Structures of Heated Egg White Protein on the Binding Between Prime Starch and Tailings Fractions in Fresh Wheat Flour

Dried egg white protein was heated at 120°C for 1 hr, added to a fresh wheat flour (protein 8.6%), and the protein and wheat flour were subjected to acetic acid (pH 3.5) fractionation. The results showed that egg white protein increased the binding between prime starch (PS) and tailings (T) fractions in wheat flour. Several conditions for heating of egg white protein were examined to determine 1) the effect of the amount of water added to the protein before heating; 2) the effect of heating time (hr) on protein at 120°C; and 3) the effect of heating temperature on the binding between PS and T fractions. The amount of protein per 50.0 g of wheat flour was further examined for the maximum binding between PS and T fractions. The heated egg white protein was analyzed by Fourier transform infrared (FT‐IR) spectroscopy, and the changes in the secondary structures (α‐helix, β‐sheets, and others) of the protein caused by heating were studied. When egg white protein was heated at 120°C for 8 hr, 9.0% of the α‐helix structures of egg white protein decreased to 3.0%, and 37.0% of the β‐sheet structures increased to 41.0%. The decrease of α‐helix and increase of β‐sheet structures of heated egg white protein were related to the increase in the binding between PS and T fractions in the same heated egg white protein and wheat flour sample. A relationship between the structural changes in heated egg white protein (180°C, 1 hr) and the binding between PS and T fractions in the heated egg white protein and wheat flour was also observed.     

Viscosity and Solubility of β‐Glucan Extracted Under In Vitro Conditions from Barley β‐Glucan‐Fortified Bread and Evaluation of Loaf Characteristics

Fortifying bread with β‐glucan has been shown to reduce bread quality and the associated health benefits of barley β‐glucan. Fortification of bread using β‐glucan concentrates that are less soluble during bread preparation steps has not been investigated. The effects of β‐glucan concentration and gluten addition on the physicochemical properties of bread and β‐glucan solubility and viscosity were investigated using a less soluble β‐glucan concentrate, as were the effects of baking temperature and prior β‐glucan solubilization. Fortification of bread with β‐glucan decreased loaf volume and height (P ≤ 0.05) and increased firmness (P ≤ 0.05). Gluten addition to bread at the highest β‐glucan level increased height and volume (P ≤ 0.05) to values exceeding those for the control and decreased firmness (P ≤ 0.05). β‐Glucan addition increased (P ≤ 0.05) extract viscosity, as did gluten addition to the bread with the highest β‐glucan level. Baking at low temperature decreased (P ≤ 0.05) β‐glucan viscosity and solubility, as did solubilizing it prior to dough formulation. Utilization of β‐glucan that is less soluble during bread preparation may hold the key to effectively fortifying bread with β‐glucan without compromising its health benefits, although more research is required.     

Gluten Structural Evolution During Pasta Processing of Refined and Whole Wheat Pasta from Hard White Winter Wheat: The Influence of Mixing,Drying, and Cooking

An attempt was made to evaluate gluten structural changes in refined and whole wheat pasta from hard white winter wheat to elucidate the impact of whole wheat components on the formation and structure of the gluten network in pasta. Attenuated total reflectance–FTIR spectroscopy was used to track gluten secondary structure through most of the major steps in pasta processing: raw material, mixing, drying, and cooking. Protein solubility, accessible thiols, and SDS‐PAGE data were also collected to provide additional information on the nature of protein interactions and network composition. Few secondary structural differences were observed between refined and whole wheat flours from hard white wheat. However, mixing induced a significant shift to β‐sheet structures in refined dough that was not equally matched by whole wheat dough. Drying under both high temperature, short time (HT) and low temperature, long time (LT) conditions resulted in a reversion to structural distributions similar to those for flour in both pastas. However, greater protein denaturation in HT samples was indicated by lower protein solubility also in the presence of denaturants and disulfide reducing agents. Cooking generated a substantial increase in β‐sheet structures for both pasta systems. This structure was greatest in refined and LT samples. Thiol accessibility data indicate the presence of a highly aggregated, compact gluten network in refined pasta, mostly driven by hydrophobic association. Conversely, the network in whole wheat pasta was more loosely associated and dependent on disulfide bonding, both of which fit well with the secondary structural data.     

Effect of Formulation and Processing Treatments on Viscosity and Solubility of Extractable Barley β‐Glucan in Bread Dough Evaluated Under In Vitro Conditions

β‐Glucan shows great potential for incorporation into bread due to its cholesterol lowering and blood glucose regulating effects, which are related to its viscosity. The effects of β‐glucan concentration, gluten addition, premixing, yeast addition, fermentation time, and inactivation of the flour enzymes on the viscosity of extractable β‐glucan following incorporation into a white bread dough were studied under physiological conditions, as well as, β‐glucan solubility in fermented and unfermented dough. β‐Glucan was extracted using an in vitro protocol designed to approximate human digestion and hot water extraction. The viscosity of extractable β‐glucan was not affected by gluten addition, the presence of yeast, or premixing. Fermentation produced lower (P ≤ 0.05) extract viscosity for the doughs with added β‐glucan, while inactivating the flour enzymes and increasing β‐glucan concentration in the absence of fermentation increased (P ≤ 0.05) viscosity. The physiological solubility of the β‐glucan concentrate (18.1%) and the β‐glucan in the unfermented dough (20.5%) were similar (P > 0.05), while fermentation substantially decreased (P ≤ 0.05) solubility to 8.7%, indicating that the reduction in viscosity due to fermentation may be highly dependent on solubility in addition to β‐glucan degradation. The results emphasize the importance of analyzing β‐glucan fortified foods under physiological conditions to identify the conditions in the dough system that decrease β‐glucan viscosity so that products with maximum functionality can be developed.     

Effects of Temperature on Sorption of Water by Wheat Gluten Determined Using Deuterium Nuclear Magnetic Resonance

The effects of lipids and residual starch components of wheat flour gluten on gluten hydration properties were investigated using nuclear magnetic resonance (NMR) and Fourier transform infrared (FTIR) techniques. Whole or native, lipid-free, starch-free, and lipid- and starch-free gluten samples were prepared from wheat (Triticum aestivum) cv. Mercia. ²H NMR relaxation on gluten samples hydrated with deuterium oxide (D₂O) was measured over a 278–363 K temperature range. FTIR spectra were recorded in dry and fully hydrated material. Transverse relaxation (T₂) results indicated that all four gluten samples were hydrophilic in nature. There was little difference in relaxation behavior of whole and lipid-free gluten samples. T₂ values and populations of the relaxation components were very similar in each. The FTIR spectra of both samples showed an increase in extended β-sheet secondary structures on hydration. These results suggest that lipid binding in gluten, if it occurs, has little effect on wheat gluten properties. Adding starch to the gluten matrix results in an increase in water sorption on heating that may be attributed to the effects of starch gelation. However, the whole water uptake of the gluten cannot be accounted for by the contribution of the residual starch, as estimated by the effects of added starch. Extraction of residual starch required solubilization of the protein, including breaking of the disulfide bonds. This process altered the gluten structure and properties. Light microscope investigation showed that glutens with residual starch extracted were unable to form fibrillar strands on hydration. NMR and FTIR results showed greater water sorption in both samples with extracted starch than in the unextracted samples.     

Factors Associated with Dough Stickiness as Sensed by Attenuated Total Reflectance Infrared Spectroscopy

Attenuated total reflectance (ATR) and Fourier transform infrared (FTIR) spectroscopy have been applied in the characterization of sticky dough surfaces. The characterization provides insight in the chemical distribution of gluten protein, starch, water, and fat during dough kneading. ATR is especially useful for selective sampling of dough surfaces because the depth of penetration of radiation is quite shallow. For dough, it is calculated to be in the order of 0.5–4 μm in the mid‐infrared, ideal for measurements of stickiness effects, where only the dough surface is of interest. To investigate the cohesive and adhesive properties of the individual dough constituents, dough was peeled from the ATR plate to study the material that adhered to it. The infrared spectra obtained indicate that fat and gluten protein appear to be located at the outer sticky dough surfaces, rather than water and starch. In comparison with gluten, the fatty component showed relatively strong adhesive forces to the ATR plate; a high residual fraction was measured after peeling the dough. Gluten proteins display different cohesion and adhesion properties that are strongly dependent on their hydration state. This indicates that the degree of hydration of gluten proteins contributes to the sticky properties of (overkneaded) dough. When analyzing gluten protein in D₂O instead of a dough matrix, more or less similar results were obtained. Significant differences in amide I and amide II intensities were measured for kneaded and stretched gluten protein in comparison to untreated, wet gluten. Besides changes in the vibrational properties of the amide groups, conformational changes in the tertiary protein structure also were observed. It appears that kneading and stretching of dough results in a major decrease in α‐helices content, accompanied by an increase of extended β‐sheet conformations.     

Salt tolerance of Casuarina equisetifolia and Frankia Ceq1 strain isolated from the root nodules of C. equisetifolia

Effects of NaCl on the seed germination and growth of Casuarina equisetifolia seedlings and multiplication of the Frankia Ceq1 strain isolated from the root nodules of C. equisetifolia were examined. The germination rate of the seeds markedly decreased as the NaCl concentration increased and germination did not occur at 300 mM NaCl. The fresh weight of both shoots and roots of the seedlings treated with NaCl for 6 weeks apparently decreased as the NaCl concentration increased. However, root nodules were formed by inoculation with the Frankia Ceq1 strain in some seedlings treated with 300 mM NaCl and the viability of the seedlings at 500 mM NaCl was almost the same as that of the seedlings not subjected to the NaCl treatment. The Na⁺ concentration in the shoots sharply increased with the elevation of the NaCl concentration in the ambient solution, but the level was approximately 300 mM even in the seedlings treated with 500 mM NaCl for 6 weeks. On the other hand, the increase of the Na⁺ concentration in the roots by the NaCl treatment was much smaller than that in the shoots and the level was less than 150 mM. The growth of the free-living Frankia Ceq1 strain was approximately linearly suppressed as the NaCl concentration in the medium increased and the hyphae became somewhat thicker and shorter or disintegrated in the medium containing NaCl at a concentration above 150 mM. The Na⁺ concentration in the cells increased as the NaCl concentration in the medium increased, but the level was maintained at less than 30 mM even in the medium containing 500 mM NaCl. The cells whose growth was suppressed by the NaCI treatment grew actively again at almost the same rate as the control cells (not subjected to the NaCl treatment) when they were transferred to NaCl-free medium. These results strongly suggested that both C. equisetifolia seedlings and Frankia Ceq1 strain are highly tolerant to salt and this symbiotic system is useful for the recovery of the vegetation in areas with severe salt accumulation.     

Estimation of the Deoxynivalenol and Moisture Contents of Bulk Wheat Grain Samples by FT‐NIR Spectroscopy

Deoxynivalenol (DON) levels in harvested grain samples are used to evaluate the Fusarium head blight (FHB) resistance of wheat cultivars and breeding lines. Fourier transform near‐infrared (FT‐NIR) calibrations were developed to estimate the DON level and moisture content (MC) of bulk wheat grain samples harvested from FHB screening trials. Grains in a rotating glass petri dish were scanned in the 10,000–4,000 cm⁻¹ (1,000–2,500 nm) spectral range using a Perkin Elmer Spectrum 400 FT‐IR/FT‐NIR spectrometer. The DON calibration predicted the DON levels in test samples with R ² = 0.62 and root mean square error of prediction (RMSEP) = 8.01 ppm. When 5–25 ppm of DON was used as the cut‐off to classify samples into low‐ and high‐DON groups, 60.8–82.3% of the low‐DON samples were correctly classified, whereas the classification accuracy of the high‐DON group was 82.3–94.0%. The MC calibration predicted the MC in grain samples with R ² = 0.98 and RMSEP = 0.19%. Therefore, these FT‐NIR calibrations can be used to rapidly prescreen wheat lines to identify low‐DON lines for further evaluation using standard laboratory methods, thereby reducing the time and costs of analyzing samples from FHB screening trials.     

Effect of Mixing Time on Gluten Recovered by Ultracentrifugation Studied by Microscopy and Rheological Measurements

The effect of mixing time on gluten formation was studied for four commercial flour mixtures. The gluten phase was separated from dough using a nondestructive ultracentrifugation method. Small deformation dynamic rheological measurements and light and scanning electron microscopy were used. The recovered gluten was relatively pure with a small amount of starch granules embedded. The protein matrix observed by microscopy became smoother with prolonged mixing. No effect of overmixing was observed on the storage modulus (G′) of gluten for any of the flours. The amount of water in gluten increased from optimum to over‐mixing for most of the flours. Increased water content during prolonged mixing was not related to an effect on G′. The Standard flour resulted in the highest water content of gluten, which increased considerably with mixing time. The Strong flour had the lowest G′ of dough, a high G′ of gluten, and no increase in gluten water content from optimum to over‐mixing. The Durum flour did not show gluten development and breakdown similar to the other flours. The differences in gluten protein network formation during dough mixing are genetically determined and depend on the flour type.     

Effects of Wheat Cultivar and Nitrogen Application on Storage Protein Composition and Breadmaking Quality

Influences of cultivar and nitrogen application on protein concentration and composition, and amount and size‐distribution of different protein components, were investigated in 10 spring wheat cultivars (Triticum aestivum L.) with widely varying gluten strength, grown under four nitrogen fertilizer conditions. The results showed that cultivar differences in gluten strength were determined by storage protein composition, differences in total amount of HMW glutenin subunits, the glutenin‐to‐gliadin ratio, and the relationship between SDS‐soluble and SDS‐insoluble protein polymers. Negative correlations were found between protein parameters related to gluten strength and bread volume. No cultivar stability for gluten strength in relation to differences in nitrogen application was found. Thus, the gluten strength was influenced by the nitrogen application in all the investigated cultivars. Increased nitrogen supply correlated significantly to an increase in all protein components containing gliadins and glutenins, but not to those containing albumins and globulins. The increase in protein components containing gliadins and glutenins correlated significantly with an increase in protein concentration and bread volume.