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.     

Growth Environment Influences Grain Protein Composition and Dough Functional Properties in Three Australian Wheat Cultivars

The objectives of this study were to assess how functional properties of proteins in whole meal wheat (Triticum aestivum L.) flour vary across different growth environments. Grain from three commercial Australian Hard milling wheat cultivars was analyzed from four growth locations in 2008 and from two of the corresponding cultivars and locations in 2009. The protein content of the grain, soluble and insoluble extractable protein fractions, swelling index of glutenin (SIG), glutenin‐to‐gliadin ratio (Glu:Gli), percent unextractable polymeric protein (%UPP), and dough properties including force at maximum resistance (Rmax) and extensibility were measured. Based on analysis of variance of aggregated data for the cultivars, growth locations, and seasons, growth environment factors made significant contributions to variability in the total grain protein, Glu:Gli ratio, %UPP, SIG, Rmax, and extensibility of the wheat flour. Variability of protein content of the soluble and insoluble extractable protein fractions was mostly owing to genotype.     

Characteristics and Protein Subunit Composition of Flour Mill Streams from Different Commercial Wheat Classes and Their Relationship to White Salted Noodle Quality

Proximate characteristics and protein compositions of selected commercial flour streams of three Australian and two U.S. wheats were investigated to evaluate their effects on the quality of white salted noodles. Wheat proteins of flour mill streams were fractionated into salt‐soluble proteins, sodium dodecyl sulfate (SDS)‐soluble proteins, and SDS‐insoluble proteins with a sequential extraction procedure. SDS‐soluble proteins treated by sonication were subsequently separated by nonreducing SDS polyacrylamide gel electrophoresis (SDS‐PAGE). There was a substantial amount of variation in distributions of protein content and protein composition between break and reduction mill streams. SDS‐insoluble proteins related strongly to differences in protein quantity and quality of flour mill streams. The soluble protein extracted by SDS buffer included smaller glutenin aggregates (SDS‐soluble glutenin) and monomeric proteins, mainly gliadin (α‐, β‐, γ‐, and ω‐types) and albumin and globulin. SDS‐soluble proteins of different flour mill streams had similar protein subunit composition but different proportions of the protein subunit groups. Noodle brightness (L) decreased and redness (a) increased with increased SDS‐insoluble protein and decreased monomeric gliadin. Noodle cooking loss and cooking weight gain decreased with increased glutenin aggregate (SDS‐soluble glutenin and SDS‐insoluble glutenin) and decreased monomeric gliadin. Noodle hardness, springiness, cohesiveness, gumminess, chewiness, tensile strength, breaking length, and area under the tensile strength versus breaking length curve increased with increased glutenin aggregate. Monomeric gliadin contributed differently to texture qualities of cooked noodles from glutenin aggregate. Monomeric albumin and globulin were not related to noodle color attributes (except redness), noodle cooking quality, and texture qualities of cooked noodles. The results suggested that variation in protein composition of flour mill streams was strongly associated with noodle qualities.     

Quantitative Determination of High Molecular Weight Glutenin Subunits of Hard Red Spring Wheat by SDS-PAGE. I. Quantitative Effects of Total Amounts on Breadmaking Quality Characteristics

Thirteen hard red spring wheat genotypes in which seven genotypes had the same high molecular weight (HMW) glutenin subunits (2*, 7+9, 5+10) were compared for their physical-chemical and breadmaking properties. These samples were categorized into three groups based on their dough mixing and baking performances as follows: the strong dough (SD) group (six genotypes), characterized by the strongest dough mixing (average stability, 35 min); the good loaf (GL) group (four genotypes), characterized by the largest loaf volume; and the poor loaf (PL) group (three genotypes), characterized by the smallest loaf volume. Total flour proteins were fractionated into 0.5M salt-soluble proteins, 2% SDS-soluble proteins, and residue proteins (insoluble in SDS buffer). SDS-soluble proteins, residue proteins, and total flour proteins were analyzed by SDS-PAGE and densitometry procedures to determine the proportions of HMW glutenin subunits, medium molecular weight proteins, and low molecular weight proteins in relation to the total amount of proteins. No differences in the amount of salt-soluble proteins were found among the different groups of samples. Solubilities of gluten proteins (total proteins minus salt-soluble proteins) in SDS buffer were related to the differences in dough strength and baking quality among the three groups. The SD group had the lowest solubility and the PL group had the highest. SDS-PAGE analysis showed that SDS-soluble proteins of the SD group contained a smaller amount of HMW glutenin subunits than those of the GL and PL groups. The highest proportions of HMW glutenin subunits in total flour proteins were found in the SD group, while the PL group had the lowest percentage of HMW glutenin subunits in their total flour proteins. These results showed that the total quantities of HMW glutenin subunits played an important role in determining the dough mixing strength and breadmaking performance of hard red spring wheats.     

Sequential extraction and quantitative recovery of gliadins, glutenins, and other proteins from small samples of wheat flour

Methods to sequentially extract and fractionate wheat flour proteins were evaluated to reliably quantify gliadins, glutenins, and albumins/globulins in single flour samples. Compositions of the resulting protein fractions were analyzed by RP-HPLC combined with SDS-PAGE. Unknown proteins were identified by mass spectrometry or N-terminal sequencing. The best separation and recovery of discrete albumin/globulin, gliadin, and glutenin fractions from the same flour sample was achieved by extraction with 0.3 M NaI in 7.5% 1-propanol followed by 2% SDS, 25 mM DTT in 25 mM TRIS, pH 8.0, and precipitation of the solubilized proteins with ammonium acetate/methanol followed by acetone. Average flour composition for the variety Butte86 was 10% albumin/globulin, 40% gliadin, and 48% glutenin. This method should be useful for determining flour composition in diverse samples and evaluating relationships between proteins and end-use functionality.     

Studies on Effects of Microbial Transglutaminase on Gluten Proteins of Wheat. I. Biochemical Analysis

The enzyme transglutaminase (TG) is known to have beneficial effects on breadmaking. However, only limited information is available on the structural changes of gluten proteins caused by TG treatment. The effect of TG has, therefore, been systematically studied by means of model peptides, suspensions of wheat flours and doughs. The treatment of synthetic peptides mimicking amino acid sequences of HMW subunits of glutenin with TG results in isopeptide bonds between glutamine and lysine residues. To study the effect on gluten proteins, different amounts of TG (0 to 900 mg enzyme protein per kg) were dissolved in a buffer and added to wheat flour. The flour suspensions were incubated and centrifuged and the residues were successively extracted with water, a salt solution, 60% aqueous ethanol (gliadin fraction) and SDS solution including a reducing agent (glutenin fraction). The characterization of the fractions by amino acid analysis, SDS‐PAGE, gel permeation HPLC and reversed‐phase HPLC has indicated that the quantity of extractable gliadins decreases by increasing TG amounts. Among gliadins, the ω5‐type was affected to the greatest extent by the reduction of extractability, followed by the ω1,2‐, α‐ and γ‐types. The oligomeric portion of the gliadin fractions (HMW gliadin) was strongly reduced when flour was treated with 450 and 900 mg TG per kg of flour, respectively. In the first instance, the quantity of the glutenin fractions increased by the treatment of flour with 90 and 450 mg TG per kg of flour, and significantly decreased by the treatment of flour with 900 mg TG per kg of flour. Parallel to an increase in TG concentration, the amounts of glutenin‐bound ω‐gliadins and HMW subunits were strongly reduced, whereas the LMW subunits reached a maximal amount after treatment with 450 mg TG per kg of flour. The insoluble residue was almost free of protein when flour was treated with lower amounts of TG. Higher amounts led to a great increase of protein in the residues. The effects of TG on doughs were similar to those of flour suspensions, but less strongly pronounced probably due to the lower water content of the dough system. Sequence analysis of peptides from a thermolytic digest of the insoluble residue revealed that HMW subunits of glutenin and α‐gliadins were predominantly involved in cross‐links formed by TG treatment.     

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.     

Distribution of Protein Composition in Bread Wheat Flour Mill Streams and Relationship to Breadmaking Quality

Wheat protein quantity and composition are important parameters for wheat baking quality. The objective of this study was to use fractionation techniques to separate the proteins of flour mill streams into various protein fractions, to examine the distribution of these protein fractions, and to establish a relationship between protein composition and breadmaking quality. Nine break streams, nine reduction streams, and three patent flours obtained from three samples of Nekota (a hard red winter wheat) were used in this study. A solution of 0.3M NaI + 7.5% 1-propanol was used to separate flour protein into monomeric and polymeric proteins. The protein fractions, including gliadin, albumin+globulin, HMW-GS, and LMW-GS, were precipitated with 0.1M NH₄Ac-MeOH or acetone. The fractions were statistically analyzed for their distribution in the mill streams. The quantities of total flour protein and protein fractions in flour were significantly different among mill streams. The ratio of polymeric to monomeric proteins in break streams was significantly greater than in the reduction streams. The relationship between protein composition and breadmaking quality showed that the quantities of total flour protein, albumin+ globulin, HMW-GS, and LMW-GS in flour were significantly and positively correlated with loaf volume. The ratio of HMW-GS to LMW-GS had little association with loaf volume. The gliadin content in total flour protein was negatively and significantly correlated with loaf volume. These results indicated that the quantity and composition of protein among the mill streams was different, and this resulted in differences in breadmaking quality.     

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.     

Sulfur,Protein Size Distribution,and Free Amino Acids in Flour Mill Streams and Their Relationship to Dough Rheology and Breadmaking Traits

The aim of this study was to analyze sulfur content, protein size distribution, and free amino acids in flour mill streams (FMS) and their associations to dough rheology and breadmaking traits. Break FMS had higher nitrogen and sulfur quantities than reduction FMS. The third break FMS had the highest nitrogen and sulfur contents among FMS but low bread loaf volume partly due to high ash content. Sulfur quantity had greater or equivalent correlations with dough rheology and breadmaking properties compared with nitrogen quantity when the effect of percent ash content was removed statistically. FMS also showed significant quantitative variation in HMW polymeric proteins of the SDS‐unextractable fraction that had greater association with sulfur content and dough rheology and breadmaking traits than other protein fractions. Asparagine, which is a major amino acid in flour, was found at higher levels in the third break and third reduction FMS. Ratio of nitrogen to sulfur was significantly correlated with asparagine concentration (r = 0.73, α = 0.01). This study indicates that information on sulfur, protein size distribution, and free amino acid is potentially useful in research for more precise blending of FMS in commercial flour mills to meet customer specifications for high quality flour.     

Quantitative Variation of HMW Glutenin Subunits from Hard Red Spring Wheats Grown in Different Environments

The objective of this study was to investigate the quantitative variation of HMW glutenin subunits in relation to glutenin polymers and hence breadmaking quality across different environments. Six genotypes of hard red spring (HRS) wheat were grown at seven locations in North Dakota in 1998 in a randomized complete‐block experimental design with three replicates at each location. Unreduced SDS‐soluble glutenins of flour were fractionated by multistacking SDS‐PAGE into different sized glutenin polymers, followed by SDS‐PAGE and imaging densitometry to determine the quantitative variation of HMW glutenin subunits. SDS‐insoluble glutenin polymers also were examined for their quantitative composition of HMW glutenin subunits. The results showed that the percentage of HMW glutenin subunits was significantly affected by growing locations. The quantity of HMW glutenin subunits in SDS‐insoluble glutenins was significantly and positively correlated with loaf volume. SDS‐insoluble glutenin polymers had a higher percentage of HMW glutenin subunits than did SDS‐soluble glutenins. SDS‐insoluble glutenin polymers in flour were positively and significantly correlated in proportions of both total and individual HMW glutenin subunits in total SDS glutenins. SDS‐insoluble glutenin polymers also were positively and significantly correlated with the combined proportion of HMW glutenin subunits 2* + 5. The results of this study indicated that either subunit 2* or 5 might be more important in forming a greater quantity of larger SDS‐insoluble glutenin polymers than other subunits. SDS‐insoluble glutenin polymers from different cultivars or locations could have different quantities of HMW glutenin subunits in their composition. SDS‐insoluble glutenin polymers with more HMW glutenin subunits might be larger sized than those with less HMW glutenin subunits. Environment significantly influenced the quantitative variation of HMW glutenin subunits, which in turn affected the size distribution of glutenin polymers, and hence breadmaking quality.     

Relationship between endogenous protein disulfide isomerase family proteins and glutenin macropolymer

The effects of endogenous protein disulfide isomerase (PDI) family proteins on the properties of gluten proteins in dough during breadmaking were determined using bacitracin, an inhibitor of PDI. Bread loaf volume in the presence of bacitracin was increased to 118% of that in the absence of bacitracin. The addition of bacitracin caused a decrease in the extension tolerance of the dough. The amount of sodium dodecyl sulfate (SDS)-insoluble glutenin macropolymer (GMP) in dough decreased to approximately 70% of that in flour during the 20 min of mixing for doughmaking. The addition of bacitracin to dough caused a dramatic GMP decrease, corresponding to ～20-30% of that in flour during the 20 min of mixing. The decrease in GMP was compensated by an increase in SDS-soluble glutenin polymer. Taken together, these results suggest that the endogenous PDI family proteins in flour suppress the depolymerization of GMP during dough mixing.     

Physicochemical and Rheological Characterization of Wheat Flour Dough

Rheological and structural behavior of dough prepared with two Argentinean flours (FI and FII) of different dough extensibilities were studied. Flours were analyzed by composition and rheological assays. Structural properties of dough prepared at different mixing times were analyzed by scanning electron microscopy, free sulfhydryls quantification, and yield of different protein fractions, as well as their protein surface hydrophobicity. Size of high molecular weight glutelin soluble aggregates was analyzed through multistacking gel electrophoresis. Dynamic viscoelasticity of dough was also studied. Flours FI and FII presented similar physicochemical properties but different rheological properties. Structural properties of both flour components were different. Starch from FI flour generated a more viscous paste than that of FII. FI presented a higher glutenin‐to‐gliadin ratio and a higher content of free sulfhydryls than FII. The resulting dough of FI showed a high development time and was more stable than FII. FI contained a high proportion of soluble HMW glutenins and formed dough with a more depolymerized insoluble protein residue containing a lower amount of gliadin in its matrix than FII. FI also formed a more elastic and stable dough with higher development time than FII. The specific structural characteristic of FI turns this flour into suitable raw material for the preparation of different bakery products in which elasticity of dough would be an important functional property.     

Effects of Wheat Protein Fractions on Flour Tortilla Quality

Commercial wheat protein fractions (10) were evaluated during processing for quality of tortillas prepared using pastry, tortilla, and bread flours. Protein fractions that separately modify dough resistance and extensibility were evaluated in tortillas to determine whether the proteins could increase diameter, opacity, and shelf stability. Tortillas were prepared using laboratory‐scale, commercial equipment with fixed processing parameters. Dough and tortilla properties were evaluated using analytical methods, a texture analyzer, and subjective methods. Tortillas were stored in plastic bags at 22°C for up to 20 days. Adjustments in water absorption and level of reducing agent were made to normalize differences in functionality of 3% added proteins on dough properties. Tortilla weight, moisture, pH, opacity, and specific volume were not affected by added proteins, except for glutenin and vital wheat gluten treatments, which had decreased opacity in tortillas prepared from pastry flour. Increased insoluble polymeric protein content corresponded to decreased tortilla diameter and improved shelf stability. Treatments yielding tortillas with improved shelf stability and similar tortilla properties were produced when commercially processed vital wheat gluten products, FP600, FP6000, FP5000, or gliadin were added to pastry or tortilla flour. These wheat protein fractions improved processing and tortilla quality of wheat flours, especially pastry flour, by modifying protein content and quality.     

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.     

Breadmaking Quality of Selected Durum Wheat Genotypes and Its Relationship with High Molecular Weight Glutenin Subunits Allelic Variation and Gluten Protein Polymeric Composition

Twenty‐seven durum wheat genotypes originating from different geographical areas, all expressing LMW‐2 at Glu‐B3, and five bread wheats were evaluated for flour mixing properties, dough physical characteristics, and baking performance. Gluten polymeric composition was studied using size‐exclusion HPLC of unreduced flour protein extracts. As a group, durum wheats had poorer baking quality than bread wheats in spite of higher protein and total polymer concentrations. Durum wheats exhibited weaker gluten characteristics, which could generally be attributed to a reduced proportion of SDS‐unextractable polymer, and produced less extensible doughs than did bread wheats. However, substantial variation in breadmaking quality attributes was observed among durum genotypes. Better baking performance was generally associated with greater dough extensibility and protein content, but not with gluten strength related parameters. Extensibility did not correlate with gluten strength or SEHPLC parameters. Genotypes expressing high molecular weight glutenin subunits (HMW‐GS) 6+8 exhibited better overall breadmaking quality compared with those expressing HMW‐GS 7+8 or 20. Whereas differences between genotypes expressing HMW‐GS 6+8 and those carrying HMW‐GS 7+8 could only be attributed to variations in extensibility, the generally inferior baking performance of the HMW‐GS 20 group relative to the HMW‐GS 6+8 group could be attributed to both weaker and less extensible gluten characteristics.     

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.     

Pan Bread and Chinese White Salted Noodle Qualities of Chinese Winter Wheat Cultivars and Their Relationship with Gluten Protein Fractions

Improvement of food processing quality has become a major breeding objective in China. Nineteen Chinese leading winter wheat cultivars with improved quality and two Australian cultivars with high bread and noodle-making qualities were sown in four locations for two years to investigate dough properties, pan bread, and Chinese white salted noodle (CWSN) qualities, and their association with the quantity of protein fractions. The results indicated that genotype, environment, and genotype-by-environment interaction significantly affected most of quality traits and amount of protein fractions. Genotype mainly determined the quantity of gluten protein fractions and pan bread quality parameters, while environment was the most important source of variation for the noodle quality parameters. Chinese cultivars were characterized by acceptable protein content (11.1–13.4%), medium to strong dough strength (maximum resistance 176.9–746.5 BU), medium to poor dough extensibility (166.5–216.4 mm), fair to very good pan bread qualities, and good to very good CWSN qualities. Gliadin contributed more in quantity to protein content (r = 0.80, P < 0.001), however, glutenin and its subgroups were more important to dough strength. The quantity of glutenin, HMW-GS, and LMW-GS were highly and significantly correlated with dough strength-related traits such as farinograph development time, stability, extensigraph maximum resistance, and extension area (r = 0.70–0.91, 0.65–0.89, and 0.70–0.91, respectively; P < 0.001). The quantity of LMW-GS could explain 82.8% of the total variation of dough maximum resistance. The quantity of gliadin and the ratio of HMW-GS to LMW-GS determined dough extensibility (r = 0.75 and r = –0.59, respectively; P < 0.001 and P < 0.01, respectively). Higher quantity of glutenin and lower ratio of gliadin to glutenin resulted in higher bread score with r = 0.70 (P < 0.001) and r = –0.74 (P < 0.001), respectively. However, protein content and its fractions have a moderate undesirable effect on CWSN parameters such as color, firmness, and taste. Therefore, both allelic variation and quantity of storage protein fractions should be considered in breeding cultivars with improved pan bread making quality.     

Swelling Index of Glutenin Test. I. Method and Comparison with Sedimentation,Gel‐Protein,and Insoluble Glutenin Tests

Molecular weight distribution of wheat proteins is primarily responsible for the viscoelastic properties of flour dough. Furthermore, the amount of SDS insoluble proteins (mainly high molecular weight glutenin) plays the major role. We have developed a simple test to determine the swelling power of glutenin (swelling index of glutenin or SIG) for predicting dough properties and end‐use quality. Flour samples (40 mg) were hydrated in distilled water and then allowed to swell in nonreducing solvents (SDS, lactic acid, or mixtures of the two) followed by low speed centrifugation. The SIG was calculated as the weight of the residue divided by the original sample weight. The SIG test was compared with the results from other small‐scale tests for 20 flour samples. SIG tests showed highly significant correlations with the gel protein and insoluble glutenin test (r ≥ 0.85, r ≥ 0.93, P < 0.001, respectively) and significant correlations with SDS and Zeleny sedimentation tests (r ≥ 0.74, r ≥ 0.72, P < 0.001, respectively). The swelling capacity of glutenin depended on swelling time and mixing intensity in nonreducing solvents. Swelling curves obtained from SIG values versus different swelling time can be divided into three distinct stages: swelling, swollen, and breakdown. These stages may reflect soluble and insoluble glutenin contents and quality among different cultivars. SIG test values for short swelling time and low mixing intensity were significantly correlated to gel protein content and SDS‐sedimentation values (r = 0.96, r = 0.90, P < 0.001, respectively). SIG test values for long swelling time and high mixing intensity were significantly correlated to insoluble glutenin content (r = 0.96, P < 0.001). The difference of swelling condition (time and mixing intensity) among these small‐scale methods is the reason for their different correlations with insoluble glutenin content. Because large numbers of samples can be analyzed in a short time with excellent reproducibility, the SIG test may be a useful screening test in a breeding program, predicting the quantity and quality of insoluble glutenin.     

Comparison of Quality Characteristics and Breadmaking Functionality of Hard Red Winter and Hard Red Spring Wheat

Various whole‐kernel, milling, flour, dough, and breadmaking quality parameters were compared between hard red winter (HRW) and hard red spring (HRS) wheat. From the 50 quality parameters evaluated, values of only nine quality characteristics were found to be similar for both classes. These were test weight, grain moisture content, kernel size, polyphenol oxidase content, average gluten index, insoluble polymeric protein (%), free nonpolar lipids, loaf volume potential, and mixograph tolerance. Some of the quality characteristics that had significantly higher levels in HRS than in HRW wheat samples included grain protein content, grain hardness, most milling and flour quality measurements, most dough physicochemical properties, and most baking characteristics. When HRW and HRS wheat samples were grouped to be within the same wheat protein content range (11.4–15.8%), the average value of many grain and breadmaking quality characteristics were similar for both wheat classes but significant differences still existed. Values that were higher for HRW wheat flour were color b*, free polar lipids content, falling number, and farinograph tolerance. Values that were higher for HRS wheat flour were geometric mean diameter, quantity of insoluble polymeric proteins and gliadins, mixograph mix time, alveograph configuration ratio, dough weight, crumb grain score, and SDS sedimentation volume. This research showed that the grain and flour quality of HRS wheat generally exceeds that of HRW wheat whether or not samples are grouped to include a similar protein content range.