4: A brief survey of gluten proteins and wheat starches

Plant Foods for Human Nutrition -     

Structural characteristics of corn starches extruded with soy protein isolate or wheat gluten

Commercially available corn starches containing 0, 25, 50 and 70% amylose were extruded with 10, 20 and 30% soy protein isolate (SPI) or wheat gluten (WG) at 22% moisture content (dry basis) in a C.W. Brabender single screw laboratory extruder using a 140°C barrel temperature and a 140 rpm screw speed. True, solid and bulk densities; percent total, closed and open pores; and shear strengths of the extrudates were determined. The microstructures of the extrudates were studied by scanning electron microscopy (SEM). The total pores of the extrudates were affected significantly (p < F=0.0001) by type of protein (SPI or WG) and starch amylose. The open or closed pores, were affected by protein type only. The interaction between amylose and protein contents was highly significant <(p < F=0.0001). In general, the total pores and bulk densities were higher for WG-starch extrudates compared to SPI-starch extrudates. These values decreased as amylose content increased from 0 to 25% and then increased thereafter. The open pores, on the other hand, increased with increasing protein content from 10 to 20% and then decreased. Extrudates containing WG had higher shear strengths than those containing SPI.     

Glass transition temperature of starches with different amylose/amylopectin ratios

The glass transition temperatures (T_g) of starch with different amylose/amylopectin ratios were systematically studied by a high-speed DSC. The cornstarches with different amylose contents (waxy 0; maize 23, G50 50 and G80 80) were used as model materials. The high heating speed (up to 300 °C/min) allows the weak T_g of starch to be visible and the true T_g was calculated by applying linear regression to the results from different heating rates. It is confirmed for the first time, that the higher the amylose content is, the higher the T_g is for the same kind of starch. The sequence of true T_g of cornstarch is G80 > G50 > maize > waxy when samples contain the same moisture content, which corresponds to their amylose/amylopectin ratio. It was found that T_g was increased from about 52 to 60 °C with increasing amylose content from 0 to 80 for the samples containing about 13% moisture. The microstructure and phase transition were used to explain this phenomenon, in particular the multiphase transitions that occur in high-amylose starches at higher temperatures, and the gel-ball structure of gelatinized amylopectin.     

Heat and additive induced biochemical transitions in gluten from good and poor breadmaking quality wheats

Glutens from poor breadmaking quality wheat, cv. Riband, had a higher SDS extractability than glutens from good quality cv. Hereward. Heating of gluten, especially above 70 °C, caused a reduction in the amount of SDS-extractable gluten proteins. Treatment of gluten with redox additives (ascorbic acid, potassium bromate or glutathione) affected extractability, being highest for bromate treated glutens. The SH content of gluten was lower for poor breadmaking Riband and heating resulted in greater decrease in SH content of gluten from good breadmaking Hereward. Hereward gluten had a higher SS content than Riband. The alteration of SS content on heating was not significant and may indicate the heat-induced involvement of non-covalent interactions. SDS-PAGE revealed that oxidants, especially bromate, affect polypeptide composition leading to a more heat stable/tolerant protein structure.     

Deamidation of gluten proteins and peptides decreases the antibody affinity in gluten analysis assays

Wheat gluten is a widely used ingredient in the food industry due to its unique properties and relatively low price. Modification of wheat gluten makes it a versatile ingredient and, thus, increases its applicability in foods. Therefore, gluten proteins can be found in unexpected sources, and this makes the gluten-free diet challenging to follow. Deamidation is one way to modify protein structure. It increases solubility and surface activity of gluten improving its functionality, but consequently, also influencing the accuracy of quantification by immunoassays. In this study, the effect of deamidation on the antibody recognition with gluten analysis methods based on monoclonal R5, omega-gliadin or G12 antibodies was studied. Random deamidation decreased the intensities to 13–54% of the intensity obtained for the intact peptides. Deamidation representing the transglutaminase deamidation decreased the intensities to 4–8%. Deamidation of gluten proteins abolished the recognition by omega-gliadin and G12 antibodies and decreased the recognition of R5 by 600 times when analyzed by the sandwich method and 125 times by the competitive method. In conclusion, with all of the investigated gluten-specific antibodies, deamidation decreased the affinity of antibodies to gluten peptides and proteins, which needs to be considered when assays and regulations are developed for gluten-free products.     

Water availability and state of water resources within water-economic basins in Kazakhstan

Paddy and Water Environment - Water is one of the most important natural resources. The water availability and scarcity depend on various natural and anthropogenic factors. Based on generalization...     

Effect of hydrostatic pressure and temperature on the chemical and functional properties of wheat gluten III. Studies on gluten films

Numerous gluten preparations were produced by the variation of pressure and temperature. Optimal conditions for the production of gluten films on a laboratory-scale were by suspending of gluten (1 g) in a mixture of ethanol (3 mL), glycerol (0.5 g) and conc. formic acid (10 mL), casting and drying at 40 °C. Small-scale laboratory methods for the production of gluten films by casting and moulding were developed. Film strips obtained were examined by micro-extension tests, which resulted in curves similar to extensigrams for dough and gluten and allowed the determination of the resistance to extension, extensibility and elasticity. The results demonstrated that pressure treatment of gluten in combination with variable cultivars, temperature, process parameters and additives, allow the production of films with a wide range of rheological properties – from soft and smooth to strong and hard rubber like. Finally, it was demonstrated that the addition of fibres to gluten enhanced the stability of films. Thus, high pressure treatment allows a selective modification of gluten as raw material for film production. In comparison with conventional plastic films, gluten films have considerable advantages, because they can be produced from renewable plants and they are readily biodegradable.     

Pasting,thermal and rheological properties of octenylsuccinylate modified starches from diverse small granule starches differing in amylose content

Waxy maize (a standard starch of normal granule size) and five small granule starches from different botanical sources (rice, wheat B type, oat, quinoa and amaranth) were subjected to 2-octenyl-1-succinic anhydride (OSA) modification. Changes of pasting, gel texture, thermal and rheological properties were investigated. Different small granule starches showed quite different property changes after OSA modification. Pasting viscosity was generally increased in OSA starches, among which OSA oat starch had notably high peak and breakdown viscosity but low setback viscosity. Gel hardness of rice, wheat B type, oat and quinoa starches was reduced by OSA treatment, whereas that of waxy maize and amaranth starches was increased. Amylose content was considered to be the major factor influencing pasting, gel and thermal property of OSA starches. Esterification increased pseudoplastic flow behavior of all starches, while OSA oat starch uniquely had reduced flow consistency coefficient. The dynamic rheological properties were also changed differentially among OSA starches. Viscoelastic properties of rice, wheat B type, oat and quinoa starches were increased after OSA treatment, whereas those of waxy maize and amaranth starches were decreased. This study showed that diverse functionalities from OSA small granule starches may fulfil different demands in product development.     

Effect of hydrostatic pressure and temperature on the chemical and functional properties of wheat gluten: Studies on gluten, gliadin and glutenin

The effect of hydrostatic pressure (0.1–800 MPa) in combination with various temperatures (30–80 °C) on the chemical and physical properties of wheat gluten, gliadin and glutenin was studied. Chemical changes of proteins were determined by extraction, reversed-phase high-performance liquid chromatography (HPLC), sodium dodecylsulphate (SDS) polyacrylamide gel electrophoresis (PAGE), circular dichroism (CD) spectroscopy, thiol measurement and studies on disulphide bonds. Rheological changes were measured by extension tests and dynamic stress rheometry. Treatment of gluten with low pressure (200 MPa) and temperature (30 °C) increased the proportion of the ethanol-soluble fraction (ESF) and decreased gluten strength. The enhancement of both pressure and temperature provoked a strong reduction of the ESF and the thiol content of gluten. Within gliadin types, cysteine containing α- and γ-gliadins, but not cysteine-free ω-gliadins were sensitive to pressure and were transferred to the ethanol-insoluble fraction. Disulphide peptides isolated from treated gluten confirmed that cleavage and rearrangement of disulphide bonds were involved in pressure-induced reactions. Increased pressure and temperature induced a significant strengthening of gluten, and under extreme conditions (e.g. 800 MPa, 60 °C), gluten cohesivity was lost. Isolated gliadin and glutenin reacted differently: solubility, HPLC and SDS-PAGE patterns of gliadin having a very low thiol content were not influenced by pressure and heat treatment; only conformational changes were detected by CD spectroscopy. In contrast, the properties of isolated glutenin having a relatively high thiol content were strongly affected by high pressure and temperature, similar to the effects on total gluten.     

Effect of temperature, time and wheat gluten moisture content on wheat gluten network formation during thermomolding

A plastic-like material can be obtained by thermomolding wheat gluten protein which consists of glutenin and gliadin. We studied the effect of molding temperature (130-170 °C), molding time (5-25 min) and initial wheat gluten moisture content (5.6-18.0%) on the gluten network. Almost no glutenins were extractable after thermomolding irrespective of the molding conditions. At the lowest molding temperature, the extractable gliadin content decreased with increasing molding times and moisture contents. This effect was more pronounced for the α- and γ-gliadins than for the ω-gliadins. Protein extractabilities under reducing conditions revealed that, at this molding temperature, the cross-linking was predominantly based on disulfide bonds. At higher molding temperatures, also non-disulfide bonds contributed to the gluten network. Decreasing cystine contents and increasing free sulfhydryl and dehydroalanine (DHA) contents with increasing molding temperatures and times revealed the occurrence of β-elimination reactions during thermomolding. Under the experimental conditions, the DHA derived cross-link lanthionine (LAN) was detected in all gluten samples thermomolded at 150 and 170 °C. LAN was also formed at 130 °C for gluten samples containing 18.0% moisture. Degradation was observed at 150 °C for samples thermomolded from gluten with 18.0% moisture content or thermomolded at 170 °C for all moisture contents.     

On-line interferometric study on the mechanical fracture behaviour by crazing observed in stretched polypropylene fibres

Two-beam polarizing light interference microscope devised by Pluta is used for in situ investigation of fracture mechanism of as-spun isotactic polypropylene (iPP) fibres by crazing during cold drawing process. The study includes characterization of crazing of polypropylene fibres (involving craze initiation, craze propagation and craze breakdown) as a function of crazing strain, crazing temperature and stretching speed. The investigation of craze damage showed that it is increased rapidly with stretching speed and then increased slowly to level off. Also it was found that, stretching iPP fibre at relatively low speed (lower than 0.015 cm/sec) at constant temperature 19 °C would reduce the effect of fracture on the stretched filaments. The time to crazing, the time to failure and the areal craze density of iPP fibres during cold drawing process are estimated. Finally, observing the craze formation at different temperatures showed that there was a critical value of stretching temperature for the formation of crazes in iPP fibre, and it was found to be 40 °C. The obtained results are correlated to the corresponding variations in some optical and structural properties of iPP fibres due to stretching.     

Effect of native aggregation state of soluble wheat gluten on deamidation behavior in a carboxylic acid/heat water solution

To understand the role of native aggregation state (NAS) of soluble wheat gluten and fractions during deamidation in a carboxylic acid/heat water solution, changes in conformation and deamidation behavior as function of protein concentration from dilute to semi-concentrated regimes to control NAS were investigated by physicochemical properties, SDS-PAGE, molecular force change, intrinsic fluorescence emission spectroscopy (IFES) and FTIR. Our data show that, in this solution, the deamidated proteins displayed features characteristic of more scattered and flexible polymer structure in dilute concentration than concentrated ones. Degree of deamidation (DD), HD and Zeta potential exhibited strongly oppositely with the decreasing concentration. HWM-GS, ω-gliadins and LWM-GS degraded into smaller peptides with decreasing of NAS. FTIR and IFES displayed that improved molecular flexibility with decreasing of concentration as detected by the increasing content of β-turn and β-sheet, as well as the red-shift of wheat gluten and gliadins at the expense of α-helix. Hydrophobic and hydrogen bond increased gradually and were dominant in inter-molecule as function of increasing concentration. The above information demonstrated that NAS of soluble wheat gluten dominated changes of deamidation behavior and conformation in a carboxylic acid/heat water solution.     

Migration of gluten under shear flow as a novel mechanism for separating wheat flour into gluten and starch

This paper describes a novel principle for the separation of wheat flour into starch and gluten in a concentrated medium. The process is based on the use of simple shear flow in a cone-and-cone device. The separation takes place in two steps. Initially, local segregation of gluten and starch phases occurs, leading to formation of macroscopically visible gluten patches distributed throughout the dough. This local segregation can be understood by considering the dough as a visco-elastic matrix containing an inert filler (starch). Further shearing leads to aggregation of those patches and migration (large-scale separation) towards the apex of the cone. As a result, the wheat dough is separated into a protein-poor fraction, containing less than 4% protein, and a protein-rich fraction containing almost 50% protein on a dry weight basis. However, under the process conditions used, upon a very long shearing, a redistribution of the aggregated gluten structures in the starch phase was observed, demonstrating a processing limit for the separation performance. Compared to traditional processing, the separation process presented shows opportunities for producing high quality gluten accompanied with significant water savings. Considering the fact that simple shear flow in steady rate is less harmful to gluten quality, such a separation process could benefit gluten quality.     

Evidence that pentosans and xylanase affect the re-agglomeration of the gluten network

In the gluten-starch separation process gluten is formed first as a result of breakdown of the gliadin-glutelin structures during mixing followed by their re-agglomeration. To date the effect of pentosans and enzymes have not been studied separately. A simple modification of TNO Glutomatic system enables pentosans, enzymes, and other materials to be added after the mixing step allowing the effect of these additives to be studied separately. Using this technique, we observed that re-aggregation of gluten proteins starts immediately after the first mixing step during the dough dilution phase. Xylanase addition prior to dough mixing can lead to ‘overdose effects’ but these were not observed when xylanase was added later during the re-agglomeration phase. We were able to distinguish between physical and chemical effects of pentosans on gluten formation. The effect of water-extractable pentosans is only partly related to its viscosity, a ferulic acid (FA) related reaction is more important. Pentosans affect the affect the agglomeration by increasing the size of the glutenin macropolymer particles. When the water-extractable pentosan effect is prevented by xylanase or FA addition, aggregation during dilution is more extensive and the glutenin macropolymer has a lower average particle size with a resulting difference in gluten rheology.     

The effect of gluten on the retrogradation of wheat starch

The retrogradation of amylopectin in a wheat starch and a wheat starch/gluten (10:1) blend prepared by extrusion and containing 34% water (wet weight basis) was studied using X-ray diffraction, differential scanning calorimetry and NMR relaxometry during storage at constant water content and temperature (25 °C). For both samples, amylopectin ‘fully’ retrograded after 2–3 days storage, i.e. the different parameters monitored with time to follow the retrogradation had reached their maximum value, and crystallised predominantly into the A polymorph. Under the experimental conditions used, there was no evidence of any significant effects of the presence of gluten on the kinetics, extent or polymorphism of amylopectin retrogradation.