Effect of Single Substitution of Glutenin or Gliadin Proteins on Flour Quality of Alpha 16, a Canada Prairie Spring Wheat Breeders' Line

The effect of genetic variation in the glutenin and gliadin protein alleles of Alpha 16, a Canada Prairie Spring (CPS) wheat line, on the dough mixing, bread, and noodle quality properties were evaluated. The presence of a gliadin component (BGGL) and the low molecular weight glutenin subunit (LMW-GS) 45 found in the selection Biggar BSR were associated with significant increases in dough strength characteristics. The results of the study showed that gliadins, LMW-GS, and high molecular weight glutenin subunits (HMW-GS) can influence bread- and noodle-making properties of wheat flour. Genotype-by-environment interactions were not significant for most of the quality parameters studied, indicating that the differences observed in quality characteristics were mainly due to the effect of genotype.     

Winter Wheat Quality Responses to Water,Environment, and Nitrogen Fertilization

Decreasing carbon (C) footprints by reducing nitrogen (N) and water inputs has been speculated to have negative impacts on wheat grain yield and flour processing quality. The objective of this study was to determine the impact of N and water stress on winter wheat grain yield, protein composition, and dough quality. Wheat fertilized at two N rates (unfertilized and recommended) was grown under water-stressed and well-watered environments. Nitrogen and water stress were measured using the ¹³C isotopic approach. Research showed that (1) N fertilizer and the water-management environment produced similar impacts on wheat quality and yield loss due to N stress and yield loss due to water stress (YLWS); (2) N fertilizer increased flour protein, dough stability, and relative concentration of glutenin (%Glu), unextractable polymeric protein (UPP), and relative amount of high-molecular-weight glutenin subunits (HMW-GS/LMW-GS); (3) the well-watered environment reduced protein contents when N mineralization was low, whereas it did not influence protein content when mineralization was high; and (4) the %Glu was negatively correlated with yield loss due to N stress (YLNS) and positively correlated with stability. This study showed that a clear understanding of the complex relationship between soil variability and climatic conditions should make it possible to develop adaptive management practices, increase profitability, and improve quality.     

施氮量对不同品质类型小麦子粒蛋白质组分含量及加工品质的影响

选用强筋小麦济麦20、中筋小麦泰山23和弱筋小麦宁麦9号,利用反相高效液湘色谱（RP-HPLC）方法测定了施氮量对不同品质类型小麦子粒蛋白质组分含量和高分子量谷蛋白亚基（HMW-GS）、低分子量谷蛋白亚基（LMW-GS）含量的影响,并分析其与子粒加工品质的关系。结果表明,随施氮量增加,强筋小麦济麦20和中筋小麦泰山23的子粒蛋白质含量及各组分含量均呈先增加后降低的趋势,施氮量为N 240 kg/hm2时,蛋白质各组分含量较高,加工品质较好; 过量施氮抑制了HMW-GS合成,这是过量施氮导致强筋和中筋小麦子粒蛋白质品质变劣的原因之一。随施氮量增加,弱筋小麦宁麦9号子粒的蛋白质各组分含量显著增加,加工品质变劣。增施氮肥,3个品种的谷蛋白和醇溶蛋白含量的增加幅度显著高于清蛋白+球蛋白含量,这是施氮改善强筋和中筋小麦子粒加工品质的主要原因。济麦20和泰山23两品种的总蛋白质含量及醇溶蛋白含量无显著差异,但强筋小麦济麦20的谷蛋白含量、贮藏蛋白、HMW-GS、LMW-GS、谷蛋白大聚合体（GMP）含量及谷蛋白与醇溶蛋白含量的比值（Glu/Gli）和HMW-GS与LMW-GS含量的比值（HMW/LMW）高于中筋小麦泰山23,这是强筋小麦济麦20加工品质形成及其面团形成时间和稳定时间显著高于泰山23的重要原因。     

Molecular Weight Distribution of Wheat Proteins

The molecular weight distribution (MWD) of wheat proteins is becoming recognized as the main determinant of physical dough properties. Studies of high polymers have shown that properties such as tensile strength are related to a fraction of polymer with molecular weight above a critical value and the MWD of this fraction. Elongation to break is treated as a kinetic process with energies of activation for breaking noncovalent bonds and for chain slippage through entanglements. These considerations are related to tensile properties of wheat flour doughs such as those measured by the extensigraph. The MWD of wheat proteins is determined by the relative amounts of monomeric and polymeric proteins and the MWD of the polymeric proteins. The latter, in turn, depends on the ratio of high molecular weight glutenin subunits (HMW-GS) to low molecular weight glutenin subunits (LMW-GS), the specific HMW-GS that result from allelic variation, and the presence of modified gliadins that act as chain terminators. The role of these compositional variables in determining dough extensional properties is discussed in terms of present knowledge. Determination of MWD of wheat proteins is hindered by the difficulty of their solubilization and the lack of methods for reliably measuring very high molecular weights. Among the promising techniques for achieving these measurements are multiangle laser light scattering (MALLS) and field flow fractionation (FFF).     

Depolymerization of the Glutenin Macropolymer During Mixing: II. Differences in Retention of Specific Glutenin Subunits

The depolymerization of individual high and low molecular weight (HMW and LMW, respectively) glutenin subunits (GS) from the glutenin macropolymer (GMP) in doughs during mixing was investigated by reversed-phase (RP) HPLC and SDS-PAGE. Cultivars with different dough strengths, as well as lines null for specific HMW-GS and biotypes differing at individual HMW-GS and LMW-GS encoding loci, were studied. During mixing, the proportion of total HMW-GS in GMP decreased, and the ratios of different subunits in the GMP in doughs changed. There was a loss of chromosome 1B- and 1D-encoded x-HMW-GS, while the relative proportions of y-HMW-GS (among HMW-GS) increased. Changes in 1B subunits occurred first, while most of the changes in 1D HMW-GS content occurred during dough breakdown. Changes were more pronounced for doughs of weak to average strengths than for stronger doughs. RP-HPLC analysis demonstrated a consistent increase in the retention times (surface hydrophobicity) of chromosome 1D-encoded HMW-GS but not of other HMW-GS or LMW-GS during mixing. SDS-PAGE and RP-HPLC demonstrated that specific B subunits, typically those with lower hydrophobicity, were selectively depolymerized from the GMP during dough breakdown, while the proportions of specific C subunits, typically those with greater hydrophobicity, increased. Similar trends were seen in analyses of several pairs of biotypes differing at single LMW-GS encoding loci, although there were slight differences in the depolymerization behavior of wheats with different allelic compositions. The results suggest that dough breakdown may be triggered by the loss of specific HMW-GS from the GMP, and a structural hierarchy may exist for different LMW-GS within glutenin in doughs.     

Effects of Prolamins Encoded by Chromosomes 1B and 1D on the Rheological Properties of Dough in Near-Isogenic Lines of Bread Wheat

Fourteen bread wheat near-isogenic lines (NILs) with different alleles at 1B- and 1D-chromosome loci Glu-1, Glu-3 and Gli-1 coding for high molecular weight glutenin subunits (HMW-GS), low molecular weight-GS, and gliadins, respectively, were grown in replicated plots to investigate the individual and combined effects of glutenin and gliadin components on the rheological properties of dough as determined by the Chopin alveograph. NILs did not reveal significant differences in seed yield, protein content, kernel weight, test weight, flour yield, and starch damage. On the contrary, they had a large variation in alveograph dough tenacity P (55–93 mm), swelling G (17–26 mL) and strength W (140–252 J × 10^-4). The null alleles at the Gli-D1/Glu-D3 loci, and allele Glu-D1d (HMW-GS 5+10) were found to have a strong positive influence on dough tenacity and a remarkable negative influence on dough swelling (extensibility) when compared to alleles Gli-D1/Glu-D3b and Glu-D1a (HMW-GS 2+12), respectively. On the other hand, alleles Glu-B1c (HMW-GS 7+9) and Gli-B1/Glu-B3k gave greater G values than alleles Glu-B1u (HMW-GS 7*+8) and Gli-B1/Glu-B3b. The effects of individual Glu-1, Gli-1, or Glu-3 alleles on P and G values were largely additive. The impact of the null allele at Gli-D1/Glu-D3 on gluten strength was highly positive in NILs possessing HMW-GS 2+12, and negligible or negative in NILs containing HMW-GS 5+10, suggesting that there is scope for improving dough quality by utilizing this allele in combination with HMW-GS 2+12. Gli-D1/Glu-D3-encoded prolamins were shown to play a major role in conferring extensibility to dough, and could account for the superior breadmaking characteristics of bread wheat as compared to durum wheat.     

Genetic variability at the Glu-1 loci in old and modern wheats (triticum aestivum L.) cultivated in Slovakia

The high molecular weight glutenin subunits (HMW-GS) composition at the Glu-1 complex loci, in 23 old original wheat genotypes cultivated in Slovakia several decades ago and 32 modern Slovak and Czech wheat cultivars growed in Slovakia at present were studied by SDS-PAGE. Some of the HMW-GS – subunit pairs 3+12, 17+18, and subunit 20, present in old historical wheats were missing in modern cultivars utilized in Slovakia nowadays. There were observed 15 different HMW-GS encoded by 11 alleles or allelic pairs in old genotypes. Lower number of different HMW-GS and competent alleles were observed in a set of modern wheat cultivars – 11 different HMW glutenin subunits encoded by 8 alleles or allelic pairs. The same number of different HMW-GS patterns was revealed in both sets of wheats. From the point of view of genetic variability, it could be concluded that long-term effort of breeders and decreasing of cultivation of landraces and old cultivars are associated with the loss of several HMW-GS alleles and decreasing of genetic variability of wheats. Molecular characterization can reveal broad allelic variability of old wheat genotypes and landraces. Their maintenance in genetic resource collections can prevent losses of these interesting genes.     

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.     

Immunoassay for wheat processing quality: utilization of a sandwich assay incorporating an immobilized single-chain fragment.

A single-chain fragment (scFv) was engineered from a monoclonal antibody to high molecular weight glutenin subunits (HMW-GS), wheat flour polypeptides that play a major role in determining the mixing- and extension strength-related properties of dough and its subsequent baking performance. The scFv was expressed in a thioredoxin mutant Escherichia coli strain that allows disulfide bond formation in the cytoplasm and incorporated into a diagnostic test for wheat quality. Although the scFv lacks the more highly conserved antibody constant regions usually involved with immobilization, it was able to be directly immobilized to a polystyrene microwell solid phase without chemical or covalent modification of the protein or solid phase and utilized as a capture antibody in a double-antibody (two-site) immunoassay. In the sandwich assay, increasing HMW-GS concentrations produced increasing assay color, and highly significant correlations were obtained between optical densities obtained in the ELISA using the scFv and the content of large glutenin polymers in flours as well as measures of dough strength as measured by resistance to dough extension in rheological testing. The assay using the scFv was able to be carried out at lower flour sample extract dilutions than that required for a similar assay utilizing a monoclonal capture antibody. This research shows that engineered antibody fragments can be utilized to provide superior assay performance in two-site ELISAs over monoclonal antibodies and is the first application of an engineered antibody to the analysis of food processing quality.     

施氮量对小麦氮代谢相关酶活性和子粒蛋白质品质的影响

在2003～2004年和2004～2005年小麦生长季,以强筋小麦济麦20为材料,分别设置N 0、96、168、240、276 kg/hm2 5个施氮量处理和0、96、168、240 kg/hm2 4个施氮量处理,研究不同施氮量对小麦氮代谢相关酶活性和子粒蛋白质品质的影响。两年度的试验结果均表明,在一定施氮量范围内,随施氮量增加,公顷穗数、穗粒数、蛋白质含量、子粒产量和蛋白质产量均显著升高;继续增加施氮量子粒产量显著降低,公顷穗数、穗粒数、蛋白质产量降低或无显著差异。其中2004～2005年生长季,在0～168 kg/hm2施氮量范围内,随施氮量增加,旗叶谷氨酰胺合成酶（GS）活性、开花21d后的旗叶內肽酶（EP）活性、旗叶游离氨基酸含量、子粒醇溶蛋白含量、高分子量谷蛋白亚基（HMW-GS）和低分子量谷蛋白亚基（LMW-GS）含量、HMW-GS / LMW-GS比值、子粒蛋白质含量、公顷穗数和穗粒数、子粒产量均显著升高,面团形成时间和稳定时间延长;继续增加施氮量至240 kg/hm2,GS活性无显著变化,但开花21 d后的EP活性、-醇溶蛋白、-醇溶蛋白、HMW-GS、LMW-GS和子粒蛋白质含量仍显著提高,面团稳定时间继续延长,子粒产量显著降低。说明施氮过多对小麦氮素同化和产量无益;提高开花后旗叶GS活性和灌浆后期旗叶EP活性,有利于HMW-GS和LMW-GS的积累及HMW-GS/ LMW-GS比值的提高。适量施氮不仅提高了子粒灌浆所需氮源的供给能力,而且显著增加公顷穗数和穗粒数,扩大了单位面积库容,增加了单位面积上的氮素和光合产物在子粒中的贮存,这是适量施氮实现子粒品质和产量同步提高的生理原因。本试验条件下高产优质高效的施氮量为168～240 kg/hm2。     

Prolamin aggregation, gluten viscoelasticity, and mixing properties of transgenic wheat lines expressing 1Ax and 1Dx high molecular weight glutenin subunit transgenes

The composition of high molecular weight (HMW) subunits of glutenin determines the gluten strength and influences the baking quality of bread wheat. Here, the effect of transgenes coding for subunits 1Ax1 and 1Dx5 was studied in two near-isogenic wheat lines differing in their HMW subunit compositions and mixing properties. The subunits encoded by the transgenes were overexpressed in the transformed lines and accounted for 50-70% of HMW subunits. Overexpression of 1Ax1 and 1Dx5 subunits modified glutenin aggregation, but glutenin properties were much more affected by expression of the 1Dx5 transgene. This resulted in increased cross-linking of glutenin polymers. In dynamic assay, the storage and loss moduli of hydrated glutens containing 1Dx5 transgene subunits were considerably enhanced, whereas expression of the 1Ax1 transgene had a limited effect. The very high strength of 1Dx5 transformed glutens resulted in abnormal mixing properties of dough. These results are discussed with regard to glutenin subunit and glutenin polymer structures.     

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

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

Depolymerization of the Glutenin Macropolymer During Dough Mixing: I. Changes in Levels,Molecular Weight Distribution,and Overall Composition

Changes in the amounts, molecular weight distributions, and levels of major groups of subunits in the glutenin macropolymer (GMP) of doughs during mixing were investigated. The GMP (gel protein) is the unreduced fraction of gluten protein that remains as a layer on top of the starch after extraction of SDS-soluble proteins and centrifugation. Experiments involved doughs prepared from flours derived from one weak and one strong cultivar and lines derived from cv. Olympic that were null for specific high molecular weight glutenin subunits (HMW-GS). During mixing, the amount of GMP decreased; the major changes occurred before peak mixing time (MT, achievement of peak resistance). In addition, the average apparent molecular weight of GMP (determined by both size-exclusion HPLC and multilayer gel electrophoresis) decreased during mixing, but in this case, the major changes were seen later in the mixing process, during dough breakdown. Even after extensive mixing, polymers and oligomers were released, not free glutenin subunits. During dough breakdown, the composition of GMP also changed, such that the proportion of HMW-GS decreased but β-amylases/D low molecular weight glutenin subunits (LMW-GS) increased. Changes in the total amounts of other LMW-GS typically were smaller with a decrease in the proportion of B subunits and an increase in the proportion of C subunits. The major changes in GMP composition were observed after peak MT (peak resistance) occurring earlier and to a greater extent in the weaker dough. Our results suggest that dough breakdown during mixing may be triggered by loss of HMW-GS, leading to changes in the molecular weight distribution and composition of the disulfide-bonded GMP.     

Molecular characterization of two novel Glu-D1-encoded subunits from Chinese wheat (Triticum aestivum L.) landrace and functional properties of flours possessing the two novel subunits

The high molecular weight glutenin subunits (HMW-GS) can be used for wheat quality improvement. Two novel alleles (designated 1Dx1.5* and 1Dy12.2*, respectively) at the Glu-D1 locus were identified in the Chinese wheat landrace variety ‘Jiuquanjinbaoyin’ by comparison of subunit mobility with that previously identified in several standard hexaploid wheats. The 1Dx1.5* and 1Dy12.2* genes were isolated using the allele-specific PCR primers and the complete open reading frames (ORFs) were obtained. Allele 1Dx1.5* consists of 2487 bp encoding a mature protein of 827 amino acid residues, whereas 1Dy12.2* consists 1980 bp encoding 658 residues. Comparisons of amino acid sequences analysis showed that 1Dx1.5* had higher similarity with the HMW-GS isolated from the wheat related species (Aegilops tauchi Coss.) than from the bread wheat varieties (Triticum aestivum L.). The 1Dy12.2* amino acid sequence showed a generally similar to the 1Dy12* isolated from Chinese endemic wheats. Meanwhile, the dough properties of the lines expressing (null, 7+8, 1.5*+10), (null, 7+8, 2+12.2*) and (null, 7+8, 2+12), respectively, were measured by a Mixograph, which demonstrates that the alleles 1.5*+10 can be considered as having positive impact on dough strength when compared with the alleles 2+12. In addition, the subunits 2+12.2* also showed a greater impact on dough strength than 2+12.     

Link Between Mixing Requirements and Dough Strength

Industrial bakeries in Australia and New Zealand using the mechanical dough development (MDD) process have experienced undesirable increases in dough mixing requirements. This problem is an unwanted outcome of breeding programs that have endeavored to increase dough strength as a desirable characteristic. Research was undertaken to determine the nature of the link between dough strength and mixing requirements and its relevance to the MDD process across a wide range of wheat lines. Data from three similar trials of 20 wheat lines confirmed the existence of an apparently tight, positive correlation between mixing requirements and dough strength. Although a wide range in genotypes and environments was used, no significant outliers were found, despite the belief that the link between these quality attributes was breakable or at least flexible. This creates a dilemma, as it would be desirable to reduce work input (WI) for economic reasons but not at the expense of loaf quality, which could have a deleterious effect on product marketability. The resultant nexus between mixing requirements, as measured by MDD WI, and dough strength measured by extensigraph resistance to extension (Rmax), appeared to be influenced by the application of nitrogen fertilizer during cultivation, while the nexus between mixing requirements as measured by mixograph development time (MDT) and Rmax, was influenced by other factors associated with crop location. The nexus between farinograph development time (FDT) and Rmax was affected by both location and nitrogen fertilizer application. The rates of increase in WI, MDT, and FDT against Rmax appeared to differ between high molecular weight glutenin subunits (HMW-GS) 5+10 or 2+12 (the Glu-D1 alleles). The Glu-A1 and Glu-A3 loci also played a significant role, indicating that by manipulating them it may be possible to shift or manipulate the nexus between mixing requirements and dough strength. Alleles at these loci appeared to be additive in effect on WI, MDT, and FDT, as well as Rmax.     

Identification of isopeptide bonds in heat-treated wheat gluten peptides

Results in this paper confirm heat-induced isopeptide bond formation in wheat gluten. Heating (24 h, 130 °C) of wheat gluten [moisture content 7.4%] decreased its extractability in sodium dodecyl sulfate containing buffer (pH 6.8), even after reduction of disulfide (SS) bonds. Thus, both SS bonds and non-SS bonds were responsible for the extractability loss. Cross-links of the lysinoalanine and lanthionine type were not present in the heated samples, but heat treatment reduced levels of available amino groups. Heating of purified and alkylated high molecular weight glutenin subunits (HMW-GS) under similar conditions also resulted in extractability loss, demonstrating that cross-linking did not solely depend on the availability of cysteine or cystine. These observations indicated that heat treatment had induced isopeptide bond formation, resulting in larger and unextractable molecules. Heating HMW-GS lysine- and glutamine-containing peptides induced the formation of isopeptide bonds, thereby supporting the above hypothesis. The level of isopeptide bond formation increased with heating time.     

Protein Changes During Various Stages of Breadmaking of Four Spring Wheats: Quantification by Size-Exclusion HPLC

Protein changes for four hard red spring wheat genotypes (Len, Marshall, 215, and Butte 86) were assessed at various stages of breadmaking using a size-exclusion HPLC technique. Breadmaking stages considered were flour, after mixing, before punching, after punching, after fermentation, and after proofing. Quality and functional characteristics of the four wheat genotypes were determined. The three main protein groups isolated by SE-HPLC were further characterized by SDS-PAGE. A direct relationship between polymeric glutenin (peak I of SE-HPLC fractions) in flours and loaf volume was found for the three wheat genotypes with identical high molecular weight glutenin subunit (HMW-GS) composition (2*, 7+9, 5+10) and one line with similar HMW-GS composition (2*, 7+9, 2+12), differing in the Glu-D1 locus. Quantitative changes in the distribution of SDS-soluble proteins fractionated by SE-HPLC were also examined. Peak I proteins (polymeric proteins) from SDS-extractable proteins tend to decrease during breadmaking, while peak III proteins (low molecular weight) tend to increase. Peak II (monomeric proteins, medium molecular weight) did not show a change in quantity during breadmaking. These results seem to indicate that some type of rearrangement took place during the breadmaking process to release proteins of smaller molecular weight.     

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

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

施氮量对不同小麦品种高分子量麦谷蛋白亚基表达量及品质影响的研究

采用盆栽试验和SDS-PAGE技术,研究了氮肥对强筋和中筋小麦亚基表达量、品质性状及相关关系的影响。结果表明,施用氮肥提高了优质小麦高分子量谷蛋白亚基表达量,对强筋小麦影响较小,而对中筋小麦影响较大。施氮后,强筋小麦的亚基表达量与醇溶蛋白和谷蛋白的含量极显著相关,而中筋小麦的亚基表达量仅与谷蛋白的含量显著相关,说明氮肥对不同亚基组成小麦高分子量谷蛋白表达量及蛋白组分调控有一定差异。施氮后,高分子量谷蛋白亚基表达量与各项加工品质指标呈正相关;强筋小麦的亚基表达量与湿面筋含量、稳定时间、沉降值和评价值相关性达到显著或极显著水平;而中筋小麦的亚基表达量仅与沉降值相关性达到显著水平。     

Role of Gluten and Its Components in Determining Durum Semolina Dough Viscoelastic Properties

Gluten was isolated from three durum wheat cultivars with a range in strength. Gluten was further fractionated to yield gliadin, glutenin and high molecular weight (HMW) and low molecular weight (LMW) glutenin subunits (GS). The gluten and various fractions were used to enrich a base semolina. Enriched dough samples were prepared at a fixed protein content using a 2‐g micromixograph. Mixing strength increased with addition of gluten. Dynamic and creep compliance responses of doughs enriched with added gluten ranked in order according to the strength of the gluten source. Gliadin addition to dough resulted in weaker mixing curves. Gliadin was unable to form a network structure, having essentially no effect on dough compliance, but it did demonstrate its contribution to the viscous nature of dough (increased tan δ). Source of the gliadin made no difference in response of moduli or compliance. Addition of glutenin to the base semolina increased the overall dough strength properties. Glutenin source did influence both dynamic and compliance results, indicating there were qualitative differences in glutenin among the three cultivars. Enrichment with both HMW‐GS and LMW‐GS increased overall dough strength. Source of HMW‐GS did not affect compliance results; source of LMW‐GS, however, did have an effect. The LMW‐2 proteins strengthened dough to a greater extent than did LMW‐1. Mechanisms responsible for dough viscoelastic properties are described in terms of reversible physical cross‐links.