Contribution of Hydrophobic Soluble Gluten Proteins,Fractionated by Hydrophobic Interaction Chromatography in Highly Acetylated Agarose,to Dough Rheological Properties

Hydrophobic interaction chromatography with highly acetylated agarose in 1‐mL columns was used to fractionate gliadins and acid‐soluble glutenins. Proteins were eluted in two fractions, the first with acetate buffer (pH 3.6) containing 35% propanol, and the second with Tris buffer in 8M urea. The proportion of eluted protein in the second fraction was called the surface hydrophobicity index. The study included 20 wheat samples of different baking qualities. Multiple regression analysis using the general linear model combined with the stepwise technique was used to relate the surface hydrophobicity index of soluble gluten proteins to specific dough rheological characteristics. Surface hydrophobicity index of gliadins and acetic acid soluble glutenins explained part of the variability of swelling index, extensibility, and work of deformation (dough strength) measured with the alveograph, and part of the farinograph water absorption variability, but showed no relationship to dough mixing characteristics. Hydrophobic soluble gluten proteins fractionated by hydrophobic interaction chromatography (HIC) explained a part of the variability of dough rheological properties.     

Effects of Transglutaminase on Rheology,Microstructure, and Baking Properties of Frozen Dough

The improving effects of transglutaminase (TGase) were investigated on the frozen dough system and its breadmaking quality. Rheological properties and microstructure of fresh and frozen doughs were measured using a Rapid Visco‐Analyser (RVA), dynamic rheometer, and scanning electron microscopy (SEM). The frozen doughs with three storage periods (1, 3, and 5 weeks at –18°C) were studied at three levels (0.5, 1.0, and 1.5%) of TGase. As the amount of TGase increased, hot pasting peak viscosity and final viscosity from the RVA decreased, but breakdown value increased. The TGase content showed a positive correlation with both storage modulus G′ (elastic modulus) and the loss modulus G″ (viscous modulus): G′ was higher than G″ at any given frequency. The SEM micrographs showed that TGase strengthened the gluten network of fresh, unfrozen dough. After five weeks of frozen storage at –18°C, the gluten structure in the control dough appeared less continuous, more disrupted, and separated from the starch granules, while the dough containing 0.5% TGase showed less fractured gluten network. Addition of TGase increased specific volume of bread significantly (P < 0.05) with softer bread texture. Even after the five weeks of frozen storage, bread volume from dough with 1.5% TGase was similar to that of the fresh control bread (P < 0.05). The improving effects of TGase on frozen dough were likely the result of the ability of TGase to polymerize proteins to stabilize the gluten structure embedded by starch granules in frozen doughs.     

Impact of Fat on Dough and Cookie Properties of Sugar‐Snap Cookies

Fat, one of the three major ingredients of sugar‐snap cookies, affects dough properties, changes in dough dimensions during baking, and in the end, the properties of the baked product. We studied the effect of reducing fat levels (from 15.8 to 8.7% on a dough basis) on dough and cookie properties and related it to the SDS extractable protein (SDSEP) levels. Reducing fat levels increased dough elasticity (from 0.19 to 0.60 MPa) and dough intrinsic hardness (from 8.6 to 27.5 N·cm³/g). Because no differences in dough SDSEP levels were noticed when fat levels were reduced, the increased dough elasticity and hardness were related to a more pronounced physical gluten entanglement. Reducing fat levels in the recipe decreased the SDSEP levels of the baked cookies, indicating more protein cross‐linking during baking with lower fat levels. Our data show that the dispersed fat phase interferes with the formation of a gluten network during baking. Reducing the fat level in the recipe increased the intrinsic cookie break strength (from 39.5 to 100.3 N·cm³/g), which was related to more gluten cross‐linking.     

Network Formation in Gluten‐Free Bread with Application of Transglutaminase

One of the main problems associated with gluten‐free bread is obtaining a good structure. Transglutaminase (TGase), an enzyme that catalyzes acyl‐transfer reactions through which proteins can be cross‐linked could be a way to improve the structure of gluten‐free breads. The objective of this study was to evaluate the impact of TGase at different levels (0, 0.1, 1, and 10 U of TGase/g of protein) on the quality of gluten‐free bread. The recipe consisted of white rice flour (relative amount: 35), potato starch (30), corn flour (22.5), xanthan gum (1), and various protein sources (skim milk powder [SMP] [12.5], soya flour, and egg powder). The influence of the various proteins in combination with the different addition levels of TGase on bread quality (% bake loss, specific volume, color, texture, image characteristics, and total moisture) was determined. Confocal laser‐scanning microscopy (CLSM) was used to evaluate the influence of TGase on the microstructure of the bread. Baking tests showed that TGase had an effect on the specific volume of the bread. For instance, the SMP bread with 10 U of enzyme contained the most compact structure, which was reflected in the crumb texture profile analysis results (highest values) (P < 0.05), digital image analysis (highest level of cells/cm²) (P < 0.05), and CLSM micrographs (network formation). Finally, it can be concluded that it is possible to form a protein network in gluten‐free bread with the addition of TGase. However the efficiency of the enzyme is dependent on both the protein source and the level of enzyme concentration.     

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.     

Comparison of Small and Large Deformation Rheological Properties of Wheat Dough and Gluten

The rheological properties of dough and gluten are important for end‐use quality of flour but there is a lack of knowledge of the relationships between fundamental and empirical tests and how they relate to flour composition and gluten quality. Dough and gluten from six breadmaking wheat qualities were subjected to a range of rheological tests. Fundamental (small‐deformation) rheological characterizations (dynamic oscillatory shear and creep recovery) were performed on gluten to avoid the nonlinear influence of the starch component, whereas large deformation tests were conducted on both dough and gluten. A number of variables from the various curves were considered and subjected to a principal component analysis (PCA) to get an overview of relationships between the various variables. The first component represented variability in protein quality, associated with elasticity and tenacity in large deformation (large positive loadings for resistance to extension and initial slope of dough and gluten extension curves recorded by the SMS/Kieffer dough and gluten extensibility rig, and the tenacity and strain hardening index of dough measured by the Dobraszczyk/Roberts dough inflation system), the elastic character of the hydrated gluten proteins (large positive loading for elastic modulus [G′], large negative loadings for tan δ and steady state compliance [J_e⁰]), the presence of high molecular weight glutenin subunits (HMW‐GS) 5+10 vs. 2+12, and a size distribution of glutenin polymers shifted toward the high‐end range. The second principal component was associated with flour protein content. Certain rheological data were influenced by protein content in addition to protein quality (area under dough extension curves and dough inflation curves [W]). The approach made it possible to bridge the gap between fundamental rheological properties, empirical measurements of physical properties, protein composition, and size distribution. The interpretation of this study gave indications of the molecular basis for differences in breadmaking performance.     

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.     

Stress Relaxation Behavior of Wheat Dough,Gluten, and Gluten Protein Fractions

Relaxation behavior was measured for dough, gluten and gluten protein fractions obtained from the U.K. biscuitmaking flour, Riband, and the U.K. breadmaking flour, Hereward. The relaxation spectrum, in which relaxation times (τ) are related to polymer molecular size, for dough showed a broad molecular size distribution, with two relaxation processes: a major peak at short times and a second peak at times longer than 10 sec, which is thought to correspond to network structure, and which may be attributed to entanglements and physical cross‐links of polymers. Relaxation spectra of glutens were similar to those for the corresponding doughs from both flours. Hereward gluten clearly showed a much more pronounced second peak in relaxation spectrum and higher relaxation modulus than Riband gluten at the same water content. In the gluten protein fractions, gliadin and acetic acid soluble glutenin only showed the first relaxation process, but gel protein clearly showed both the first and second relaxation processes. The results show that the relaxation properties of dough depend on its gluten protein and that gel protein is responsible for the network structure for dough and gluten.     

Effect of Protein Quality,Protein Content,Bran Addition,DATEM, Proving Time,and Their Interaction on Hearth Bread

The effect of protein quality, protein content, bran addition, diacetyl tartaric acid ester of monoglycerides (DATEM), proving time, and their interaction on hearth bread characteristics were studied by size‐exclusion fast protein liquid chromatography, Kieffer dough and gluten extensibility rig, and small‐scale baking of hearth loaves. Protein quality influenced size and shape of the hearth loaves positively. Enhanced protein content increased loaf volume and decreased the form ratio of hearth loaves. The effect of protein quality and protein content was dependent on the size‐distribution of the proteins in flour, which affected the viscoelastic properties of the dough. Doughs made from flours with strong protein quality can be proved for a longer time and thereby expand more than doughs made from weak protein quality flours. Doughs made from strong protein quality flours tolerated bran addition better than doughs made from weak protein quality flours. Doughs made from high protein content flours were more suited for hearth bread production with bran than doughs made from flours with low protein content. DATEM had small effect on dough properties and hearth loaf characteristics compared with the other factors.     

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.     

Formation of Homopolymers and Heteropolymers Between Wheat Flour and Several Protein Sources by Transglutaminase‐Catalyzed Cross‐Linking

The effect of different protein sources (soy flour, lupin flour, egg albumin, gelatin powder, protein‐rich beer yeast flour) on wheat dough functionality was tested by determining gluten index, texture properties, and thermomechanical parameters. Transglutaminase (TG) was also added to improve the dough functionality by forming cross‐links. The presence of protein sources had a significant effect on the gluten index, with the exception of lupin flour. Gelatin and the presence of TG resulted in significant single effects on the texture properties of the wheat‐protein dough. All the protein sources significantly modified the mixing characteristics of the dough or the thermal behavior. Capillary electrophoresis studies of the water‐soluble, salt‐soluble, and glutenin proteins indicated that interactions were mainly within proteins, thus homologous polymers. Scanning electron microscopy studies of the doughs made from blends of wheat and protein sources doughs supported the formation of heterologous structures in the wheat‐lupin blends. The combination of TG and lupin would be a promising method to be used on the treatment of insect‐damaged or weak flours, to increase the gluten strength.     

Kinetics of transglutaminase-induced cross-linking of wheat proteins in dough

The effects of TGase in dough after 15, 30, 45, and 60 min of resting time after mixing were studied with a Kieffer test. The resistance to stretching of control dough did not change greatly during the 60 min time period after mixing. In dough, TGase decreased extensibility and increased resistance to stretching and this change was already observed after the first 15 min (first measurement). The higher the enzyme dosage was, the higher the magnitude of the rheological change was. All of the doughs that contained TGase 3.8 or 5.7 nkat/g flour had a higher resistance to stretching and lower extensibility than control dough 15 min after mixing. Resistance to stretching clearly increased at a dosage of 5.7 nkat/g flour during the 15-60 min period after mixing. Extensibility increased in the control dough and in the doughs with a low enzyme dosage almost at the same rate. The evolution of air bubbles during proofing was determined with bright field microscopy and image analysis. In the presence of 5.7 nkat/g TGase, the fermented dough contained more of the smallest and less large air bubbles in comparison to the control dough. The effect of TGase and water content on the specific volume of the conventional and organic wheat bread was studied. Water did not have a significant effect on the specific volume of bread. TGase increased the specific volume of breads baked from organic flour only, when additional water (+10% of farinogram absorption) and a small enzyme dosage were used. Microstructural characterization showed that bread baked without TGase from conventional flour had a stronger protein network than that baked from organic flour. TGase improved the formation of protein network in breads baked from either normal or organic flour but at higher dosage caused uneven distribution.     

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.     

Impact of Industrial Dough Processing on Structure: A Rheology,Nuclear Magnetic Resonance,and Electron Microscopy Study

Dough processing is an important factor determining the quality of bread. The most important mechanical steps in industrial dough processing are kneading, extrusion, and molding. In all of these processing steps, considerable changes in the structure and properties of the dough can occur. On a laboratory‐scale level, these (structural) effects are well characterized but, so far, no systematic study has been performed at the level of a large‐scale industrial dough processing line. The molecular and microstructural changes that can take place during industrial dough processing were studied with the help of nuclear magnetic resonance (NMR), fundamental rheology, and scanning electron microscopy (SEM). After the kneading step, the dough shows a well‐developed gluten network with a homogeneous dispersion of starch particles (at optimum kneading time). After the extrusion step (a sheeting procedure), the structure of the dough becomes coarser and the dough gluten network is oriented and partially disrupted. This is accompanied with an increase in both rheological stress and water mobility. After molding, the network structure is restored and both the rheological stress and the mobility of water decrease. These findings provide a novel microstructurally‐lead approach to make recommendations for optimization of industrial dough processing lines.     

Effect of Processing on Functional Properties of Wheat Gluten Prepared by Cold‐Ethanol Displacement of Starch

Functional properties of gluten prepared from wheat flour are altered by separation and drying. Gluten was separated and concentrated by batterlike laboratory methods: development with water, dispersion of the batter with the displacing fluid, and screening to collect the gluten. Two displacing fluids were applied, water or cold ethanol (70% vol or greater, ‐13°C). Both the water‐displaced gluten (W‐gluten) and ethanol‐displaced‐ gluten (CE‐gluten) were freeze‐dried at ‐20°C as a reference. Samples were dried at temperatures up to 100°C using a laboratory, fluidized‐bed drier. Tests of functionality included 1) mixing in a mixograph, 2) mixing in a farinograph, and 3) the baked gluten ball test. Dough‐mixing functionality was assessed for Moro flour (9.2% protein) that was fortified up to 16% total protein with dried gluten. In the mixograph, CE‐gluten (70°C) produced improved dough performance but W‐gluten (70°C) degraded dough performance in proportion to the amount added in fortification. In the microfarinograph, there was a desirable and protein‐proportional increase in stability time for CE‐gluten (70°C) but no effect on stability for W‐gluten (70°C). Baking was evaluated using the baked gluten ball test and the percentage increase in the baked ball volume relative to the unbaked gluten volume (PIBV). PIBV values were as high as 1,310% for freeze‐dried CE‐gluten and as low as 620% for W‐gluten dried at 70°C. PIBV for CE‐gluten was reduced to 77% of the freeze‐dried control by fluid‐bed drying at 70°C. Exposure of CE‐gluten to 100°C air gave a PIBV that was 59% of the reference, but this expansion was still greater than that of W‐gluten dried at 70°C. The highest values of PIBV occurred at the same mixing times as the peak mixograph resistance.     

Effect of Physical States of Nonpolar Lipids on Rheology,Ultracentrifugation, and Microstructure of Wheat Flour Dough

In the previous study, we investigated effect of physical state of nonpolar lipids of gluten‐starch model dough. This experiment examined a real wheat flour dough system to assess the role of fat crystals in the breadmaking processes. These experiments were performed with a baking test and an investigation of wheat flour dough through rheological measurements (both large and small deformations), scanning electron microscopy, and ultracentrifugation. As a result, we found that the added oil was absorbed in the gluten structure, causing the aggregation of the gluten, which gave rise to more elastic behavior. In contrast, solid fat seemed to be distributed uniformly between the starch granules in the dough, reducing the friction between the starch granules and facilitating thin gluten gel layers. These properties lead to the lower G′ value and the increased viscous behavior, which yields an increase in loaf volume. In addition, the supposed mechanism behind the large loaf volume described in the previous study was that fat provides a uniform distribution of the dough components, and that the dough can thus expand easily, resulting in a larger loaf volume, which was supported in the wheat flour dough system. In conclusion, we found that thin, expandable gluten films and the uniform dispersion of gluten and starch granules in the dough are prerequisites for attaining better baking performance.     

Role of Gluten in Flour Tortilla Staling

Effects of protease and transglutaminase (TG) on dough and tortilla microstructures, shelf‐stability, and protein profile were determined to infer the role of gluten in tortilla staling. Control and enzyme‐treated tortillas were prepared using a standard bake test procedure and evaluated for three weeks. Confocal micrographs of control dough showed thin protein strands forming a continuous web‐like matrix. Protease‐treated dough had pieces of proteins in place of the continuous matrix, while TG‐treated dough had thicker protein strands that were heterogeneously distributed. Control tortillas had a well‐distributed continuous protein structure. Protease‐treated tortilla had a continuous structure despite being composed of hydrolyzed proteins in the dough, while the TG‐treated tortilla retained clumps of proteins. Both treatments resulted in shorter shelf‐stability of tortillas. An evenly distributed and moderately stronger gluten network is necessary for longer retention of tortilla flexibility. Solubility of protein fractions differed among treatments, but molecular weight distribution did not differentiate control and treated dough or tortillas. The proportion of each protein fraction appears to affect staling.     

Effect on Dough Functional Properties of Partial Fractionation,Redistribution, and In Situ Deposition of Wheat Flour Gluten Proteins Exposed to Water,Ethanol, and Aqueous Ethanol

The application of the cold‐ethanol laboratory fractionation method to the bulk separation of wheat starch and gluten is accompanied by incidental dissolution, removal, or redeposition of a small part of the functional gliadin protein. The new distribution resulting from process incidental redeposition of soluble components or by purposeful add‐back of soluble and leached components can lead to differences in functionality and more difficult recovery of native properties. To assess this issue, we exposed several wheat flour types to ethanol and water (50–90% v/v) solutions, water, and absolute ethanol at 22°C and –12°C. The exposure was mass conserving (leached components returned to substrate by evaporation of the solvent without separation of phases) or mass depleting (leached components not returned to substrate). The result of the mass‐conserving contact would be flour with altered protein distributions and intermolecular interactions. The result of the mass‐depleting contact would also include altered protein content. Furthermore, the mass‐conserving contact would model an industrial outcome for a cold‐ethanol process in which leached components would be added back from an alcohol solution. The leaching result was monitored by mixography of the flour, nitrogen analysis, and capillary zone electrophoresis of extracts. Although dough rheology was generally like that of the source flour, there were notable differences. The primary change for mass‐conserving contact was an increase in the time to peak resistance and a decrease in the rate of loss of dough resistance following peak resistance. These changes were in direct proportion to the amount of protein mobilized by the solvent. Leaching at 22°C, prevented dough formation for most aqueous ethanol concentrations and greatly reduced gliadin protein content. Minimal changes were noted for solvent contact at –12°C regardless of the ethanol concentration. The data suggested that 1) the conditions applied in cold‐ethanol enrichment of protein from wheat will generally preserve vital wheat gluten functionality, 2) functionality losses can be recovered by returning the solubilized fractions, and 3) the flour to which the gluten is added may require more mixing.     

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.     

Qualitative Effect of Added Gluten on Dough Properties and Quality of Chinese Steamed Bread

Glutens isolated from 15 soft red winter (SRW) wheat flours were added into a SRW wheat flour to obtain protein levels of 9.6 and 11.3% for determination of the qualitative effect of added gluten on the dough properties and quality of northern‐style Chinese steamed bread (CSB). Sodium dodecyl sulfate sedimentation (SDSS) volume of the gluten source flour exhibited positive relationships with mixograph absorption, midline peak time (MPT), and midline peak value (MPV) of the gluten‐added flours and with surface smoothness, crumb structure, and total score of CSB prepared from the gluten‐added flours regardless of protein content. Positive correlations were also observed between SDSS volume of the gluten source flour and specific volume and stress relaxation score of CSB prepared from the gluten‐added flours of 11.3% protein. The increase in protein content from 9.6 to 11.3% by gluten addition raised mixograph absorption, MPT, and MPV but had no apparent effect on resistance breakdown, dough maximum force for extension, and extensibility, and it increased CSB specific volume and crumb structure score without affecting surface smoothness, stress relaxation, and total score. Mixograph parameters exhibited significant relationships with CSB total score, indicating that they could be effective predictors of the CSB‐making quality of flours.