Reoxidation Behavior of Wheat and Rye Glutelin Subunits

The ability of HMW and LMW subunits of wheat glutelin to form a polymeric gluten network by intermolecular disulfide bonds is responsible for the unique rheological properties and baking quality of wheat dough. Because the mechanism of gluten formation is not fully understood, the reoxidation behavior of HMW and LMW subunits of wheat glutelin and HMW subunits of rye glutelin was studied. The subunits were isolated from wheat flour cv. Rektor (REK) and from rye flour cv. Danko (DAN) with a selective extraction and precipitation method. For reoxidation, different oxidants (KBrO₃ and KIO₃), protein concentrations (0.5, 1.0, and 2.0%), solvent compositions, pH values (2.0 and 8.0), and reaction times (0–360 min) were compared. The characterization of reoxidized products was achieved by the determination of the thiol content with the Ellman's reagent, and of the M_r distribution by gel‐permeation chromatography. The results demonstrated that both HMW and LMW subunits could be slowly reoxidized with KBrO₃ to polymers with M_r up to several millions. Yield and M_r distribution of polymers were dependent both on the protein concentration and on the molar ratio of oxidants to thiol groups. The HMW subunits of wheat glutelin (HMW‐REK) yielded slightly higher quantities of polymeric proteins than did the HMW subunits of rye (HMW‐DAN). Reoxidation with KIO₃ proceeded much faster than with KBrO₃ and led to lower proportions of polymerized proteins for HMW‐REK and HMW‐DAN. Obviously, more intra‐ and fewer intermolecular disulfide bonds were formed by reoxidation with KIO₃ compared with KBrO₃. In contrast, LMW‐REK was reoxidized with KIO₃ to higher amounts of polymeric aggregates, which indicated that LMW subunits formed intermolecular disulfide bonds with both KIO₃ and KBrO₃. Independent of the protein type and the oxidant used for reoxidation, more inter‐ and fewer intramolecular disulfide bonds were formed when the protein concentration was increased. Single subunits 5, 7, and 10 were isolated from HMW‐REK by preparative acid‐PAGE and were reoxidized with KBrO₃ for 360 min. The M_r distribution indicated that x‐type subunit 5 had a greater tendency to form polymers than x‐type subunit 7. The y‐type subunit 10 was characterized by a lower proportion of polymers after reoxidation than x‐type subunits 5 and 7.     

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.     

Biochemical characterization of soluble proteins in pecan [Carya illinoinensis (Wangenh.) K. Koch

Pecans (cv. Desirable) contained approximately 10% protein on a dry weight basis. The minimum nitrogen solubility (5.9-7.5%) at 0.25-0.75 M trichloroacetic acid represented the nonprotein nitrogen. Among the solvents assessed for protein solubilization, 0.1 M NaOH was the most effective, while borate saline buffer (pH 8.45) was judged to be optimal for protein solubilization. The protein solubility was minimal in the pH range of 3-7 and significantly increased on either side of this pH range. Increasing the NaCl concentration from 0 to 4 M significantly improved ( approximately 8-fold increase) protein solubilization. Following Osborne protein fractionation, the alkali-soluble glutelin fraction (60.1%) accounted for a major portion of pecan proteins followed by globulin (31.5%), prolamin (3.4%), and albumin (1.5%), respectively. The majority of pecan polypeptides were in the molecular mass range of 12-66 kDa and in the pI range of 4.0-8.3. The pecan globulin fraction was characterized by the presence of several glycoprotein polypeptides. Lysine was the first limiting essential amino acid in the defatted flour, globulin, prolamin, and alkaline glutelin fractions. Leucine and tryptophan were the first limiting essential amino acids in albumin and acid glutelin fractions, respectively. Rabbit polyclonal antibodies detected a range of pecan polypeptides in the 12-60 kDa range, of which the globulin fraction contained the most reactive polypeptides.     

Predicting Protein Composition,Biochemical Properties,and Dough-Handling Properties of Hard Red Winter Wheat Flour by Near-Infrared Reflectance

Breadmaking quality in wheat is one of several considerations that plant breeders face when developing new cultivars. In routine breeding programs, quality is assessed by small-scale dough-handling and bake tests, and to some extent, by biochemical analysis of gluten proteins. An alternative, not yet fully examined, method for wheat flour quality assessment is near-infrared reflectance (NIR) spectrophotometry. The present study was performed on 30 genotypes of hard red winter wheat grown during two crop years at eight to nine locations in the Great Plains area of the United States. Biochemical testing consisted of measuring protein fractions from size-exclusion HPLC (M _r > 100k, M _r 25–100k, and M _r < 25k designated as glutenin, gliadins, and albumin and globulins, respectively), pentosan content, and SDS sedimentation volume. Dough-handling properties were measured on a mixograph and recorded as the time to peak dough development, the peak resistance, the width of the mixing curve, and the width of the curve at 2 min past peak. Partial least squares analyses on diffuse NIR spectra (1,100–2,498 nm) were developed for each constituent or property. When applied to a separate validation set, NIR models for glutenin content, gliadin content, SDS sedimentation volume, and mixograph peak resistance demonstrated reference vs. predicted correlations ranging from r = 0.87 to r = 0.94. Such models were considered sufficiently accurate for screening purposes in breeding programs. NIR spectra were responsive to each constituent or property at a level higher than expected from a correlation between the constituent or property and protein content (recognizing that protein content is modeled by NIR with high accuracy).     

Characterization of Protein Fractions of Rice Bran to Devise Effective Methods of Protein Solubilization

Proteins from the defatted brans of representative rice cultivars were fractionated into albumins, globulins, prolamins, and acid-soluble glutelins, accounting for 34, 15, 6, and 11% of the total bran proteins, respectively. The remaining insoluble residue protein, after treatment with 0.1M sodium hydroxide, resulted in the solubilization of 95% of the residue protein, representing 32% of the total bran protein. The relative molecular mass (M_r) values determined by size-exclusion HPLC were 10–100 kDa, 10–150 kDa, 33–150 kDa, and 25–100 kDa for the fully dissociated polypeptides of albumins, globulins, prolamins, and acid-soluble glutelins, respectively. Despite a breakdown of disulfide bonds of the residue protein during sodium hydroxide solubilization, the M_r of the majority of the fully dissociated polypeptides of this fraction ranged from 45 to 150 kDa. Insolubility of residue protein was due mainly to its strong aggregation and extensive disulfide bond cross-linking. Efficient methods may be developed for solubilizing up to 98% of rice bran protein by the use of dissociating and disulfide breaking agents currently in use in the food industry.     

Detection of Proteins in Starch Granule Channels

Proteins were detected in channels of commercial starches of normal maize, waxy maize, sorghum, and wheat through labeling with a protein‐specific dye and examination using confocal laser scanning microscopy (CLSM). The dye, specifically 3‐(4‐carboxybenzoyl)quinoline‐2‐carboxaldehyde (CBQCA), fluoresces only after it reacts with primary amines in proteins, and CLSM detects fluorescence‐labeled protein distribution in an optical section of a starch granule while it is still in an intact state. Starch granules in thin sections of maize kernels also had channel proteins, indicating that proteins are native to the channels and not artifacts of isolation. Incubation of maize starch with protease (thermolysin) removed channel proteins, showing that channels are open to the external environment. SDS‐PAGE analysis of total protein from gelatinized commercial waxy maize starch revealed two major proteins of about M_r 38,000 and 40,000, both of which disappeared after thermolysin digestion of raw starch. Commercial waxy maize starch granule surface and channel proteins were extracted by SDS‐PAGE sample buffer without gelatinization of the granules. The major M_r 40,000 band was identified by MALDI‐TOF‐MS and N‐terminal sequence analysis as brittle‐1 (bt1) protein.     

Use of Solvent Retention Capacity Profile to Predict the Quality of Triticale Flours

The solvent retention capacity test (SRC) was used to evaluate flour functionality for end use applications and select wheat for production of flour with required functionality, but there is little information about SRC test application on triticale flour quality. The ability of flour to retain a set of four solvents produces a flour quality profile for predicting bakery performance. The objective of this study was to evaluate the capacity of SRC and its micro test to determine the potential quality of 25 triticale flours, as well as studying the relationship between the SRC parameters and flour chemical composition. The SRC parameters of triticale flours were correlated with the flour components that have been proposed by the method: sucrose SRC‐pentosan (r = 0.57), carbonate SRC‐damaged starch (r = 0.80), lactic SRC‐glutelin (r = 0.42), water SRC‐all hydrophilic constituents (damaged starch [r = 0.72], protein [r = 0.61], glutelin [r = 0.66], pentosan [r = 0.46]). Triticale flours have shown higher water and sodium carbonate SRC, similar sucrose SRC, and lower lactic SRC values than published results of typical flours used for cookie production. Summarizing, the high level of association found between SRC and micro SRC parameters with flour composition and quality flour tests evidence that either the SRC profile or the micro test SRC could be used to determine the potential quality of triticale flours.     

Optimizing Extraction of Zein and Glutelin‐Rich Fraction During Sequential Extraction Processing of Corn

This study was conducted to improve yields and qualities of corn protein co‐products produced by the sequential extraction process (SEP), a process using ethanol to fractionate corn in producing fuel ethanol. A two‐stage extraction protocol was evaluated to recover zein and subsequently recover a glutelin‐rich fraction (GRF). After the simultaneous oil‐extraction and ethanol‐drying step of SEP, zein was extracted from the anhydrous‐ethanol‐defatted, flaked corn by using 70% (v/v) ethanol at 60°C for 1.5 hr in a shaking water bath. Zein was recovered by ultrafiltering and then drying in a vacuum‐oven. Zein yield was 65% of the available zein in the flaked corn. SDS‐PAGE band patterns of the recovered zein closely resembled that of commercial zein. After zein extraction, the GRF was extracted using 45% ethanol and 55% 0.1M NaOH at 55°C for 2 hr. The extract was concentrated by ultrafiltration and then freeze‐dried. GRF yield was ≈65% of the available protein. Freeze‐dried GRF contained 90% crude protein (db), which classified the protein as a protein isolate. As with the protein concentrate from the original SEP, the GRF isolate was highly soluble in water at pH ≥ 7, had good emulsifying and foaming properties, formed stable emulsions, and was heat‐stable.     

Functionality of Barley Proteins Extracted and Fractionated by Alkaline and Alcohol Methods

This research optimized the extraction of different protein fractions from barley grains and assessed the physicochemical properties of the fractions obtained. Pearling was first used to remove the grain's outer layers (mainly bran and germ) so that the barley cytoplasmic proteins (albumin and globulin) would be enriched in the pearling flour (PF), while endosperm proteins (hordein and glutelin) would be enriched in the pearled grain flour (PGF). Salt, alcohol, and alkaline solutions were then used to extract different barley protein fractions from PF and PGF. The effects of extraction solvent type, pH, temperature, and extraction time on protein content and extraction efficiency were studied. Aqueous ethanol (55%, v/v) efficiently extracted barley hordein from PGF at 60°C, whereas pH 11.5 alkaline solution was the most efficient for extracting both cytoplasmic and endosperm proteins from barley PF and PGF at 23°C. Subunit molecular weight, amino acid composition, and the functional properties of each isolated barley protein fraction were investigated. Barley glutelin demonstrated superior oil‐binding property and emulsifying stability, whereas barley hordein exhibited good foaming capacity.     

Effects of Solution Nitrogen and Plant Density on Annual Grass Seed Biochemistry and Progeny Phenotypic Plasticity

Abstract

Cogenerational phenotypic plasticity compensation to nutrient limitations and shoot densities (light limitation) among individual plants of the same species could provide an increased fitness. Planting density varying between 4 and 16 plants per container and solution nitrogen varying between 5 and 19 mM were used to test phenotypic plastic responses in oat (Avena sativa cv. Montezuma) seed biochemistry and the resulting progeny. Seed Kjeldahl nitrogen (N), magnesium (Mg), and both albumin–globulin (l M NaCl soluble) and prolamin–glutelin (residue) protein fractions were affected by a solution N × plant density interaction. Phosphorus (P) content was influenced by both treatment variables. The protein fractions, P, N, and Mg, in seeds from parent treatments were generally highest in the two higher planting densities. The contents of N, P, Mg, and the prolamin–glutelin fraction were highest at mid‐N (9 mM), except for the 16 plants per container where they were maximal at high‐N (19 mM). In contrast, the albumin–globulin fraction responded linearly to N availability. Seeds per plant decreased while seed weights increased, as plant density increased. The seed content of N, albumin–globulin, prolamin–glutelin, P, and Mg were all negatively associated with the number of seeds per plant. Germination rates of progeny were inversely related to parent plants N treatment. Progeny from the treatment plants (seeds × germination percent) were inversely related, over a five‐fold range, to parent density. Progeny shoot/root ratios (S/R) were directly influenced by the N treatment of parent plants, with progeny from the highest parent N treatment having the highest S/R. Seed N and P content and the prolamin–glutelin protein fraction concentration were correlated with progeny SR. Seed weight was negatively correlated with progeny S/R. Annual grass seed numbers and weights and the allocation of several seed constituents are environmentally influenced by plant density and solution N. These seed biochemical and physiological effects result in a reproductive fitness change and a cogenerational phenotypic plasticity influenced progeny fitness (S/R attribute).     

Protein and Quality Characterization of Complete and Partial Near‐Isogenic Lines of Waxy Wheat

The objective of this study was to evaluate protein composition and its effects on flour quality and physical dough test parameters using waxy wheat near‐isogenic lines. Partial waxy (single and double nulls) and waxy (null at all three waxy loci, Wx‐A1, Wx‐B1, and Wx‐D1) lines of N11 set (bread wheat) and Svevo (durum) were investigated. For protein composition, waxy wheats in this study had relatively lower albumins‐globulins than the hard winter wheat control. In the bread wheats (N11), dough strength as measured by mixograph peak dough development time (MDDT) (r = 0.75) and maximum resistance (R_max) (r = 0.70) was significantly correlated with unextractable polymeric protein (UPP), whereas in durum wheats, moderate correlation was observed (r = 0.73 and 0.59, respectively). This may be due to the presence of high molecular weight glutenin subunits (HMW‐GS) Dx2+Dy12 at the Glu‐D1 locus instead of Dx5+Dy10, which are associated with dough strength. Significant correlation of initial loaf volume (ILV) to flour polymeric protein (FPP) (r = 0.75) and flour protein (FP) (r = 0.63) was found in bread wheats, whereas in durum wheats, a weak correlation of ILV was observed with FP (r = 0.09) and FPP (r =0.51). Significant correlation of ILV with FPP in bread wheats and with % polymeric protein (PPP) (r = 0.75) in durum lines indicates that this aspect of end‐use functionality is influenced by FPP and PPP, respectively, in these waxy wheat lines. High ILV was observed with 100% waxy wheat flour alone and was not affected by 50% blending with bread wheat flour. However, dark color and poor crumb structure was observed with 100% waxy flour, which was unacceptable to consumers. As the amylopectin content of the starch increases, loaf expansion increases but the crumb structure becomes increasingly unstable and collapses.     

Changes in total protein profiles of barley cultivars in response to toxic boron concentration

In this study, ten‐day‐old seedlings of barley {Hordeum vulgare L. cultivar Anadolu [boron (B)‐tolerant] and Hamidiye (B‐sensitive)} were used. Boron‐treated plants were grown on H₃BO₃ solution (final concentration of 10 mM) for five days. Control plants received no B treatment during this period. Total protein patterns were obtained by analysis of total protein extract from root and leaf tissues of control and B‐treated plants using two‐dimensional gel electrophoresis followed by silver staining. The protein profile of B‐treated seedlings of each cultivar was compared to the profile of control (no stress treatment) plants of the same cultivar. Silver‐stained gels showed that B stress caused increases or decreases in a number of proteins in root and leaf tissues. Moreover, as a result of B treatment, one newly synthesized protein with relative molecular weight (M_r) of 35.0 kDa was detected in root profile of the tolerant cultivar. This protein failed to show up in root profile of the B‐treated sensitive cultivar. Three proteins were quantitatively increased in B‐treated root profile of both cultivars. Following B treatment, three proteins were increased in root profile of the tolerant cultivar, but were not changed in the sensitive one. In leaf tissues, however, there were remarkable changes in total protein profiles after B treatment, relative to the control. Following B treatment, in leaf tissues, at least seven proteins were increased in amount in tolerant cultivar but were unchanged in the susceptible one. In tolerant and sensitive cultivars, amounts of two proteins were increased in B‐treated plants, relative to control seedlings. In addition, four proteins (M_r:29, 58, 58, and 22 kDa) were unchanged in control and B‐treated seedlings of the tolerant cultivar. In the susceptible cultivar however, among these four proteins, the first one (M_r:29) was very much reduced and the others (M_r: 58, 58, and 22 kDa) were completely lost in B‐treated seedlings. Moreover, following B treatment, a set of high‐molecular‐weight proteins was quantitatively decreased in the susceptible cultivar but was unchanged in the tolerant cultivar. These results indicate that in barley, certain proteins may be involved in tolerance to B toxicity. In this study, changes in polypeptide composition as a result of B toxic concentration in leaf tissues were more abundant than in roots. Therefore, it is suggested that these changes, especially at shoot level may form the basis of the tolerance mechanism to B toxicity.     

Effects of Micronization on Protein and Rheological Properties of Spring Wheat

This research investigated the effects of micronization, at different moisture levels, on the chemical and rheological properties of wheat. A set of tests designed to analyze protein fraction characteristics and rheological behaviors were conducted on samples from four wheat cultivars (AC Karma, AC Barrie, Glenlea, and Kanata). After being subjected to infrared radiation at three moisture levels (as‐is, 16%, and 22%), the seeds were milled to produce straight‐grade flour. The protein fractionation test revealed significant decreases (P ≤ 0.01) in both monomeric proteins (from 54% of total protein in the control to 37% in the tempered micronized sample) and soluble glutenins (9.4–2.5%). There was a strong negative correlation (r = ‐0.98) between the percentages of monomeric proteins and insoluble glutenins. Total extractable proteins of micronized samples tempered to 22% moisture decreased 43.5% when compared with nonmicronized control samples using size‐exclusion HPLC (SE‐HPLC). Micronization had a significant effect on gluten properties, as seen from a decrease in water absorption (P ≤ 0.01) and dough development time (P ≤ 0.01). Results showed that micronization at 100 ± 5°C had detrimental effects on wheat flour gluten functionality, including a decrease in protein solubility and impairment of rheological properties. These phenomena could be due to the formation of both hydrophobic and disulfide bonds in wheat during micronization.     

Effect of acetic acid added to cooking water on the dissolution of proteins and activation of protease in rice

The effect of acetic acid on the dissolution of proteins in rice was studied to elucidate the mechanism for the textural change induced by the acid by chemical and SDS-PAGE analyses of the rice proteins in the soaking solution. More proteins were extracted with 0.2 M acetic acid (pH 2.7) than with water (pH 6.8). The effect of acetic acid on the protein dissolution increased with increasing temperature. Immunoblotting confirmed that, when rice was soaked in acetic acid, glutelin was dissolved into the soaking solution and degraded by aspartic proteinase. Aspartic proteinase degraded glutelin much more than it did albumin and globulin. It was found that the combined amount of albumin and globulin dissolved into the acetic acid solution was much larger than that of glutelin, despite the smaller amounts present of albumin and globulin than of glutelin. Metal ions were extracted more with acetic acid than with water. In addition, carboxypeptidase was activated under the acidic condition and resulted in an increase in the amount of free amino acids. The main effect of acetic acid on the dissolution of rice proteins was enhancement of the solubility of albumin, globulin, and glutelin, the effect of proteases being minor.     

Impact of Cultivar and Environment on Size Characteristics of Wheat Proteins Using Asymmetrical Flow Field‐Flow Fractionation and Multi‐Angle Laser Light Scattering

The use of multi‐angle laser light scattering (MALLS) in conjunction with asymmetrical flow field‐flow fractionation (A‐FFFF) was investigated for the determination of the molecular weight distribution (MWD) of wheat proteins. The wheat flour proteins were dissolved by sonication in 0.1M sodium phosphate (pH 6.9) containing 2% SDS. The results presented make it evident that efficient separation and size characterization of monomeric (M < 10⁵ g/mol) and polymeric protein (10⁵ ≤ M < 10⁸ g/mol) wheat proteins can be achieved with A‐FFFF/MALLS/UV in a single run. Therefore, this method appears to be able to detect significant modifications of MWD of wheat protein, whatever the factor inducing these alterations (i.e., genetic or environmental) and whatever the nature of these alterations (i.e., monomeric‐to‐polymeric ratio or MWD of polymeric protein). In the present study, we have indeed demonstrated that the MWD of wheat proteins can be altered from one cultivar to another in three main ways: by changing the relative amounts of monomeric and polymeric proteins, by changing the MWD of polymeric protein, and then by changing both the monomeric‐to‐polymeric ratio and the MWD of polymeric protein.     

Quantification and In Vitro Bioaccessibility of Selenium from Osborne Fractions of Selenium‐Rich Cereal Grains

Cereal crops cultivated in the seleniferous belt of Punjab, India, were observed to hyperaccumulate a significantly high concentration of selenium (20–123 µg/g). Selenium concentration (µg/g) in storage proteins of wheat, maize, and rice, namely, albumin (401, 280, and 29, respectively), globulin (264, 192, and 242, respectively), glutelin (563, 359, and 178, respectively), and prolamin (629, 339, and 257, respectively) indicated variable selenium levels, with prolamin contributing significantly higher levels of selenium when compared with other proteins with reference to the total concentration of the protein fraction. The simulated gastric and gastrointestinal digestion studies indicated better accessibility of selenium during intestinal digestion, with variability across proteins and cereal types. The observations provide an insight into the bioavailability of selenium in selenium‐rich cereal grains, used in the study, and their potential use as source for selenium supplementation to deficient populations, or as “bioactive” selenium‐rich nutraceutical blends for health benefits.     

Effects of supplemental‐nitrogen on the quality of rice proteins

A study was conducted on the effect of supplemental nitrogen (N) (20 hg/ha) applied as a foliar spray or to the soil on seed production, protein percentage, and protein fractions of rice. Plants were grown in a greenhouse over two different periods of time, i.e., August 1988 to January 1989 (Period I), and December 1988 to April 1989 (Period II). Nitrogen was applied to the leaves 10 and 20 days after anthesis (DAA), and to the soil at anthesis and at 15 DAA. Average temperature was 28.7°C during Period I and 32°C during Period II, corresponding to 18.7 and 22.0 growing degree‐day/day (GDD/day), respectively. The difference in GDD/day reduced the plant cycle from 130 days during Period I to 109 days during Period II. Plants grown during Period II had larger numbers of spikelets, a higher percentage of “full grown grains”;, and higher grain weight. Although percentage crude protein was about the same for the two periods, prolamin content was increased and the albumin+globulin fraction was decreased during Period II, but with no difference in glutelin content. The increase in number of spikelets, percent full grains, and grain weight appeared to result in a greater energy demand for plants grown during Period II. This may explain the increase in prolamins, since prolamin synthesis requires less energy than globulin or albumin synthesis. There was a simultaneous decrease in albumin and globulin synthesis during Period II. The content of glutelins, which represent the major reserve proteins in rice grains, was constant during both periods.     

Correlation of Quality Parameters with the Baking Performance of Wheat Flours

The baking performance of a set of flours from 13 wheat cultivars was determined by means of two different microscale baking tests (10 g of flour each). In the micro‐rapid‐mix test the dough was mixed for a fixed time at a high speed, whereas the microbaking test used mixing to optimum dough consistency in a microfarinograph. Quality parameters such as sedimentation value, crude protein content, dough and gluten extension data, and microfarinograph data were also determined. Finally, quality‐related protein fractions (gliadins, glutenins, SDS‐soluble proteins, and glutenin macropolymer) were quantitated by extraction/HPLC methods with reversed‐phase and gel‐permeation columns. All quality parameters were correlated with the bread volumes of both baking tests. The results demonstrated that the microbaking test (adapted mixing time) was much more closely related to the quality parameters than the micro‐rapid‐mix test (fixed mixing time), which hardly showed any correlation. Among the standard quality parameters, only the crude protein content showed a medium correlation with the bread volume of the microbaking test (r = 0.71), whereas the contents of gliadins (r = 0.80), glutenins (r = 0.76), and glutenin macropolymer (r = 0.80) appeared to be suitable parameters to predict the baking performance of wheat flour. All other quality parameters were not or were only weakly correlated and unsuitable for predicting baking performance.     

Functional Properties of 7s Globulin Extracted from Cowpea Vicilins

The seed of cowpea (Vigna unguiculata L.) is rich in protein and the amino acid profiles of the meal are suitable for human dietary products, but little is known about the structure and chemical properties of the protein extracted from this legume. This study determined the functional properties of two selected cowpea cultivars and their solubility, emulsifying capacity, surface hydrophobicity, and thermal stability. Seeds of red and black cowpea were surface sterilized and the 7s globulin was isolated and purified using column chromatography with Sephacryl S‐300 (Hi‐Prep 26/60) gel column. Also, SDS‐PAGE and protein structure were analyzed using biochemical procedures. At high ionic strength (μ = 0.5), cowpea 7s globulin fraction exhibited better solubility for a wide range of pH levels, higher emulsifying capacities, and greater thermal stability than those obtained at low ionic strength (μ = 0.08). The lowest solubility was observed at pH 5.3–6.4 at the low ionic strength. Emulsifying capacities at high protein concentration were greater when compared with low protein concentration. T_m values of black cowpea globulin fraction were higher than those of red cowpea globulin fraction, whereas the surface hydrophobicity of the globulin fraction in red cowpea was larger than that in black cowpea.     

Levels of Protein and Protein Composition in Hard Winter Wheat Flours and the Relationship to Breadmaking

Protein and protein fractions were measured in 49 hard winter wheat flours to investigate their relationship to breadmaking properties, particularly loaf volume, which varied from 760 to 1,055 cm³ and crumb grain score of 1.0–5.0 from 100 g of flour straight‐dough bread. Protein composition varied with flour protein content because total soluble protein (SP) and gliadin levels increased proportionally to increased protein content, but albumins and globulins (AG), soluble polymeric proteins (SPP), and insoluble polymeric protein (IPP) levels did not. Flour protein content was positively correlated with loaf volume and bake water absorption (r = 0.80, P < 0.0001 and r = 0.45, P < 0.01, respectively). The percent SP based on flour showed the highest correlation with loaf volume (r = 0.85) and low but significant correlation with crumb grain score (r = 0.35, P < 0.05). Percent gliadins based on flour and on protein content were positively correlated to loaf volume (r = 0.73, P < 0.0001 and r = 0.46, P < 0.001, respectively). The percent IPP based on flour was the only protein fraction that was highly correlated (r = 0.62, P < 0.0001) with bake water absorption followed by AG in flour (r = 0.30, P < 0.05). Bake mix time was correlated positively with percent IPP based on protein (r = 0.86) but negatively with percent SPP based on protein (r = ‐0.56, P < 0.0001).