Whey Protein Concentrate Treated with Heat or High Hydrostatic Pressure in Wheat-Based Products

Commercial whey protein concentrate (CWPC) treated with heat or with high hydrostatic pressure (HHP) was incorporated by replacement into wheat flour, and its effects on dough rheology and the quality of cookies, noodles, and bread were evaluated. Wheat flour fortified with heat- or HHP-treated CWPC produced smaller cookies than those fortified with untreated CWPC. Increasing the fortification level of heat- or HHP-treated CWPC from 5 to 10% further decreased cookie diameter. The water absorption for noodle dough decreased by 5% with 10% fortification of untreated CWPC. Both heat- and HHP-treated CWPC increased water absorption from 33% in the control to 35.8%. Incorporation of untreated CWPC decreased the lightness (L*) value of Cantonese noodle dough, while dough fortified with heat- or HHP-treated CWPC had higher L* values compared to those of the control. Yellowness (b*) was improved with incorporation of both untreated and treated CWPC. Cooking loss of Cantonese noodles fortified with untreated or heat- or HHP-treated CWPC was comparable to or lower than that of the control. Incorporation of untreated CWPC increased hardness and cohesiveness of Cantonese noodles. Noodles fortified with heat- or HHP-treated CWPC had similar hardness and were softer than the control and the noodles fortified with untreated CWPC. Wheat flour fortified with 10% untreated CWPC produced wet and sticky bread dough and a small loaf (730 mL). Handling properties of dough were improved and bread volume was increased by 50 mL when heat- or HHP-treated CWPC was incorporated. Incorporation of 10% CWPC increased protein content of bread up to 20.2% and also increased the proportion of essential amino acids.     

Protein Digestibility of Selected Legumes Treated with Ultrasound and High Hydrostatic Pressure During Soaking

In vitro protein digestibility (IVPD) of lentils, chickpeas, peas, and soybeans treated with ultrasound or high hydrostatic pressure (HHP) during soaking and then heated for 30 min at 98°C was determined using the three-enzyme method (trypsin, chymotrypsin, and peptidase). The IVPD of raw legumes ranged from 72% for soybeans to 83% for dry green peas. The increase in the IVPD after soaking was observed in lentils but not in other legumes. Heating increased the IVPD of the tested legumes by 2–13%. While the effects of applying ultrasound or HHP on IVPD of legumes were mostly inconsistent or insignificant, soaking under HHP for 1 hr and subsequent heating at 98°C for 30 min increased IVPD of legumes. Compared with raw legumes, the soluble protein concentrates exhibited 2–4% higher IVPD, while insoluble proteins exhibited 0.2–1.5% lower IVPD. SDS-PAGE of legume proteins before enzyme digestion exhibited 8–18 protein bands from 20 kDa to 100 kDa representing isolated soluble proteins and from 20 kDa to 100 kDa representing insoluble proteins. After enzyme digestion, soluble proteins exhibited 2–6 minor protein bands with molecular weights <30 kDa, while insoluble proteins of lentils, chickpeas, and peas exhibited one major protein band at ≈52 kDa and two or three minor protein bands with molecular weights <30 kDa. The major insoluble proteins observed as electrophoresis bands after enzyme digestion may be responsible for the reduced protein digestibility of legume proteins.     

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.     

Rheological Behavior of Undeveloped and Developed Wheat Dough

Undeveloped wheat dough is essentially wheat flour that has become fully hydrated without being deformed. The rheological properties of this material were compared to dough (developed dough) made using the standard method involving a farinograph. Flow behavior of undeveloped and developed dough samples made from hard and soft wheat flours were tested using creep tests, frequency sweep oscillatory tests, and temperature sweep oscillatory tests. All experiments showed that the undeveloped dough requires less resistance for deformation than developed dough. The differences are due to the energy input received by the developed dough and the influence of this factor in forming the protein matrix associated with developed dough. To attain a comparable state as the dough made in the farinograph, an energy input must be applied to the undeveloped dough material. Understanding the differences between undeveloped and developed dough may lead to new products, equipment, and processes in the bakery industry.     

Functional Characteristics of Extruded Blends of Whey Protein Concentrate and Corn Starch

The aim of this work was to study the effects of extrusion barrel temperature (70–180°C), feed moisture (18–30%), pH (3–8), different proportions of corn starch (75–95%), and whey protein concentrate (WPC, 80% protein concentration) (25–5%) on the preparation of functional blends. Expansion index (EI), bulk density (BD), compression force (CF), color, water absorption index (WAI), water solubility index (WSI), gel strength (GS), syneresis of the gel, and in vitro digestibility were evaluated. Barrel temperature and the proportion of WPC had significant effects on BD; at higher temperatures, BD was lower. Feed moisture and pH had significant effects on EI; with lower moisture and higher pH, the EI increased. An interaction of barrel temperature and feed moisture had an effect on WAI; at lower moisture content, the temperature effect was nonexistent, whereas at higher temperatures and feed moisture content, the WAI increased. The pH level had a significant effect on WSI, showing high WSI when lower pH levels were used. Color analysis showed that higher protein content and pH generated higher δE values; low feed moisture and low pH resulted in gel syneresis. Higher in vitro digestibility was obtained when a higher WPC proportion and pH were used. Extruded WPC-CS blends under alkaline and acidic conditions were affected by the preparation of diverse formulations that potentially can be used in foods to improve some functional and protein content.     

Influence of Sodium Caseinate and Whey Protein on Baking Properties and Rheology of Frozen Dough

Dairy ingredients are added to bakery products to increase nutritional and functional properties. Sodium caseinate (SC) and whey protein concentrate (WPC) were incorporated into frozen dough. WPC was subjected to heat treatment (WPCHT) to eliminate undesirable weakening of the gluten network. 2% SC or 4% SC decreased proof time, increased loaf volume, and improved texture. Effects of adding 4% SC on baking quality were similar to adding ascorbic acid (AA) and diacetyl tartaric acid esters of monoglycerides (DATEM). WPC increased proof time, decreased volume, and negatively affected texture. Heat treatment of WPC improved baking performance. Bread with WPCHT had volume similar to that of the control without dairy ingredients. Adding 4% SC decreased resistance to extension (R_5cm measured with the extensigraph), while adding 4% WPC increased extensibility. Dynamic oscillation testing determined the effects of the ingredients on fundamental rheological properties. WPC decreased storage modulus (G′) and loss modulus (G″), while heat treatment of WPC increased G′ and G″. Confocal laser scanning microscopy (CLSM) showed that milk proteins affect frozen dough ultrastructure. Frozen doughs with SC had an enhanced gluten network compared with the control, while untreated WPC appeared to interfere with the gluten network.     

Thermomechanically Induced Protein Aggregation and Starch Structural Changes in Wheat Flour Dough

Various studies have been carried out on wheat flour to understand protein and starch changes when subjected to mixing and temperature constraints, but structural changes of proteins and starch at the typical moisture levels of a dough system are not fully understood. The aim of this research was to improve our understanding of (micro)structural changes at the mesoscopic level, through empirical rheology, microscopy (light and scanning electron microscopy), sequential protein extractions, and glutenin macropolymer wet weight along the mixing, heating, and cooling stages of the Mixolab assay. Studies were performed on three wheat flours with different protein contents. The rheological analysis allowed identifying the role of the proteins and the relationship between the protein content and different primary and secondary parameters obtained from the recorded curves. The progressive heating and mixing stages during the Mixolab assay resulted in a dynamic de‐ and restructuring of proteins involving interactions between the flour proteins from water soluble to SDS soluble to SDS insoluble and vice versa. The microstructure analysis with light, polarized, and scanning electron microscopy revealed the changes that proteins and starch molecules underwent during mixing, heating, and cooling. Qualitatively, the starch structural changes, swelling, and gelatinization observed by microscopic techniques showed some parallels with protein (and glutenin) content of the respective flour. Nevertheless, this tentative finding needs further confirmation by studying flour samples with large differences in glutenin content.     

灌浆期高温胁迫对不同品种小麦蛋白组分及面团揉混特性的影响

为研究灌浆期高温胁迫对不同品种小麦蛋白组分及面团揉混特性的影响,以济麦22(JM22)和新麦26(XM26)为材料,通过灌浆初期(S1)和灌浆中期(S2)在田间搭棚进行高温胁迫处理,以未进行高温胁迫的大田小麦作对照(CK),收获后对小麦淀粉黏滞谱、蛋白质组分含量和揉混参数等进行分析。结果表明,与各自CK相比,JM22的黏滞谱参数除回复值和糊化温度降低外,其余参数均升高,XM26的黏滞谱参数除峰值时间外均降低。S1和S2使JM22的峰值黏度、低谷黏度、崩解值、最终黏度、峰值时间分别较CK提高2.81%和18.63%、7.71%和19.51%、11.88%和21.15%、1.88%和12.22%、2.45%和4.08%,且S2均大于CK和S1,S1与CK差异不显著;S1和S2使XM26的峰值黏度、低谷黏度、最终黏度、回复值分别较CK降低12.95%和31.21%、1.81%和27.18%、2.50%和22.22%、3.57%和14.39%,其中,S2、S1与CK三者之间的峰值黏度均达显著水平。与CK相比,高温胁迫后JM22的蛋白质含量降低,而XM26升高。两品种各组分蛋白含量均发生改变,S...     

超高压下酶解处理对甘薯蛋白乳化特性的影响

为研究在超高压下酶解处理后甘薯蛋白酶解产物乳化特性的变化,选用蛋白酶K(Proreinase.K)、碱性蛋白酶(Alcalase)、中性蛋白酶AS1.398、中性蛋白酶Neutrase和木瓜蛋白酶(Papain)5种酶,在4种压力(100、200、300和400 MPa)及最适酶活温度和pH下处理5种酶与甘薯蛋白的混合液4min后,取上清液并测定其水解度、乳化液的微观结构、乳化活性指数(EAI)、乳化稳定性指数(ESI)。结果表明,与常压下相比,超高压下5种酶解产物的水解度均显著增加,超乳化液颗粒除Alcalse外,其余4种均变得更为细小均一,且4种产物的EAI显著提高,其中Papain在300MPa下处理的酶解产物EAI最佳,为101.59m~2·g~(-1)。而经超高压下酶解处理后5种酶解产物的ESI均比常压下提高,Neutrase在300MPa下处理后的ESI最好,达到75.80min。此外,选用Papain(p H值7,55℃)在300MPa(EAI最佳的条件)下处理6min,酶解产物的EAI和ESI均达到最大值,分别为129.58m2·g-1和21.98min。本研究为甘薯蛋白作为乳化剂在食品工业中的应用提供了基础理论支撑。     

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

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

Genetic Control of High Protein Content and Its Association with Bread-Making Quality in Wheat

ABSTRACT

A population of recombinant inbred lines (RILs) developed from a cross of Triticum aestivum cvs. WL711 and PH132 using the single-seed descent method was used to investigate the genetics of high protein content and its contribution to bread-making quality. Four-year data on protein content of parents and 124 RILs suggested that the difference in protein content between the two parents was controlled by two major genes with an additive effect. The individual gene gave intermediate protein content. Seven RILs with high protein content and without any yield penalty were selected, multiplied, and investigated for various milling, dough, and bread-making characteristics. PH132 and all seven selected RILs had higher protein content, higher sodium dodecyl sulphate (SDS) sedimentation value, longer dough development time, a lower mixing tolerance index, higher stability, and better loaf volume and loaf quality than the bread wheat cultivars WL711 and PBW343. High molecular weight (HMW) glutenin subunit composition of various high-protein RILs indicated a recombination of parental protein subunits. “2?” coded by Glu-A1 locus, 17 + 18 subunits coded by Glu-B1 locus, and “5 + 10” coded by Glu-D1 locus were predominant. One of the selected RILs, T-74, possessing 2 + 12 at Glu-D1 locus, also had superior bread-making quality, indicating that grain-protein content above a certain minimum value is a relatively more important determinant of bread-making quality than HMW glutenin subunits 5 + 10.     

Demixing in Wheat Doughs—Its Influence on Dough and Gluten Rheology

Reshaping of relaxed wheat doughs leads to an increase in firmness that significantly changes the results of rheological measurements involving large uniaxial deformations of the dough, whereas the gluten properties remain unaffected. Microscopic investigations reveal that directly after kneading, starch and gluten are thoroughly mixed. However, the shaping procedure of a relaxed dough or shear-flow during rheological measurements cause a separation of gluten and starch. The dilatant behavior of the starch granules and the capacity of gluten to aggregate account for the observed dough-hardening.     

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.     

Effect of Varying Protein Content and Glutenin-to-Gliadin Ratio on the Functional Properties of Wheat Dough

Gluten, starch, lipids, and water-soluble material were separated from seven wheat samples with a range of protein contents and breadmaking quality. The isolated glutens were further partitioned into gliadin- and gluteninrich fractions using pH precipitation. Protein content and glutenin-togliadin ratio were systematically altered by blending these fractions into the original flours in calculated amounts. Mixing properties, extension-tester parameters, and baking performance of composite flours were determined using small-scale techniques. Results of dough testing with blends of constant glutenin-to-gliadin ratio showed increases in the mixing time, mixograph peak resistance, maximum resistance to extension, extensibility, and loaf volume as the protein content increased. At constant protein content, increases in glutenin-to-gliadin ratio were associated with increases in mixing time, mixograph peak resistance, maximum resistance to extension, and loaf volume, and with decreases in extensibility. Thus, total protein content and glutenin-to-gliadin ratio independently affected dough and baking properties. The results have allowed the separation of the effects of flour protein quantity and composition on breadmaking properties.     

Mixing Properties,Baking Potential,and Functionality Changes in Storage Proteins During Dough Development of Triticale‐Wheat Flour Blends

Flours from advanced lines or cultivars of six triticales and two prime hard wheats, along with triticale‐wheat blends, were investigated for mixing, extension (excluding blends), and baking properties using microscale testing. Percentage total polymeric protein (PPP) and percentage unextractable polymeric protein (UPP) of flours and doughs, including blends, mixed to optimal dough development were estimated using size‐exclusion HPLC to determine the changes in protein solubility and association with blend composition (BC), mixing properties, and loaf height. Each triticale was blended with flours of each of the two wheat cultivars (Hartog and Sunco) at 0, 30, 40, 50, 60, 70, and 100% of wheat flour. Nonlinear relationships between BC and mixograph parameters (mixing time [MT], bandwidth at peak resistance [BWPR], and resistance breakdown [RBD]) were observed. A linear relationship between BC and peak resistance (PR) was predominant. PPP of triticale flours was mostly higher than PPP of wheat cultivars. UPP of all triticales was significantly lower than wheat cultivars. PPP of freeze‐dried doughs was mostly nonsignificant across the blends and showed a curvilinear relationship with BC. The deviations from linearity of MT and PPP were higher in triticale‐Sunco blends than in triticale‐Hartog blends. UPP of blends was closer to or lower than the lower component in the blend. The deviations from linearity for MT and UPP were greater in triticale‐Hartog blends than triticale‐Sunco blends. A highly significant correlation (P < 0.001) was observed between BWPR and loaf height. This suggested that BWPR in triticale‐wheat flour blends could be successfully used for the prediction of loaf height. Triticale flour could be substituted for wheat flour up to 50% in the blend without drastically affecting bread quality. Dough properties of triticale‐wheat flour blends were highly cultivar specific and dependent on blend composition. This strongly suggested that any flour blend must be tested at the desired blend composition.     

Effect of Foliar Sulfur and Nitrogen Fertilization on Wheat Storage Protein Composition and Dough Mixing Properties

Nitrogen (N) and sulfur (S) supplies have a strong influence on the quality and quantity of wheat storage proteins, which play an important role in the breadmaking process. Nitrogen derived from urea, S from micronized elemental sulfur, and a mixture of both (N+S) were applied at anthesis stage on wheat by foliar spray. To relate N and S incorporation in storage proteins to the quality of dough, their incorporation into each storage protein fraction was measured: monomers, low molecular weight glutenin subunits (LMW‐GS), and high molecular weight glutenin subunits (HMW‐GS). Then protein fraction quantities, molecular weight distribution (MWD), polymerization index (PI), and molecular dimensions of unextractable polymeric protein (UPP), as well as dough mixing properties were determined. Fertilizers N and S were differentially incorporated into each storage protein fraction, influencing protein synthesis. Moreover, after the N+S fertilization, the increase of the polymeric proteins induced an increase in molecular weight and compactness, as well as in dough strength and consistency. These results provide evidence that N and S fertilizers applied by foliar spray route at anthesis, simultaneously, play an important role in controlling the storage protein synthesis and the degree of polymerization, which in turn influence dough mixing properties.     

Thermal Behavior and Nonfreezing Water of Soybean Protein Components

Thermal denaturation and hydration of two soybean protein components were studied using differential scanning calorimetry (DSC). Results showed that temperature of denaturation (T_d) of both 11S and 7S globulins decreased sharply with an increase in water content. Enthalpy of denaturation (ΔH_d) of 11S increased with increasing water content at first, and then leveled off at high water content. However, ΔH_d of both 7S and 11S components in 7S samples first increased and then decreased at high water content. The preparation method of samples influenced the ΔH_d value significantly but had little effect on the T_d. Nonfreezing water was determined from the DSC results. It increased in both 11S and 7S as water content increased but was more abundant in 7S, probably because of different compositions and structures. Threshold value of water content for the appearance of freezing water was 0.30–0.32 h (g of water/g of protein, mass ratio) for 11S. The water absorbed by both 11S and 7S during denaturation increased quickly at low water contents and remained almost constant at high water contents. The results were attributed to different structure and conformation of proteins before and after denaturation.     

Influence of Added Starch on Mixing of Dough Made with Three Wheat Flours Differing in High Molecular Weight Subunit Composition: Rheological Behavior

The effect of mixing time (6 and 20 min) and starch content were studied on doughs prepared with three wheat flours differing in high molecular weight subunit composition. Rheological measurements were performed in dynamic oscillation: frequency and strain sweeps, stress relaxation, and in large deformation viscosity measurements. The flours were diluted with starch to cover flour protein contents of 10–15%. Water was added to keep the starch‐water ratio constant when doughs were prepared with different protein contents. By increasing the starch content of the doughs, the rheological properties approached those of a starch‐water mixture prepared with the same starch‐water ratio as in the dough. The effect of the starch granules was reinforced by prolonged mixing. This may explain the higher values of the storage modulus and relaxation times observed after 20 min of mixing. Qualities related to gluten properties, appeared more clearly in large deformation viscosity measurements.