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Model for gliadin–glutenin cross‐linking upon SH–SS exchange reactions during hydrothermal treatment. (I.1): In the absence of additives, heating to 90°C leads to conformational changes exposing previously unavailable free SH‐groups and polymerization of glutenin with the oxidation of SH groups. (I.2) Glutenin is able to react to gliadin at temperatures exceeding 90°C via SH–SS interchange and the produced free SH‐group can further react with either gliadin or glutenin. (II.1) Reducing agents depolymerize glutenin and increase the level of free SH‐groups, thereby (II.2) increasing gliadin–glutenin cross‐linking. (III.1) In the presence of an oxidizing agent reduces the level of free SH, thereby hindering glutenin linking and gliadin–glutenin cross‐linking above 90°C. (III.2) Subsequent addition of a SH containing agent can introduce new free SH‐groups in the gluten proteins and once induce gliadin–glutenin covalent cross‐linking (Lagrain, Thewissen, Brijs, & Delcour, 2008)
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Gluten protein, as plant resource, is susceptible to physical, genetic, chemical, and enzymatic treatments. In this study, we reviewed physical modifications such as heating‐ freezing, irradiation, high pressure, ultrasonication, shear, and extrusion of gluten. The mode of action of each modification process was investigated. Conformational changes...
Citations
... These reactions exert an influence on the overall protein structure. Consequently, the reduction in protein content within the extrudates may signify diminished accessibility of these residues, attributed to cross-linking or aggregation of the protein chains, or the alteration or destruction of these amino acids [38]. Consistent with the results of this study, Phillips and Williams [39] reported that extrusion cooking can reduce protein solubility due to protein aggregation and enhance protein digestibility through protein denaturation. ...
The physiochemical, textural and nutritional properties of novel extrudates generated from various kinds of rice
and legume (beans) varieties were comprehensively evaluated and compared in this study. The developed
extruded products were composed of 5 %, 10 %, 15 %, or 20 % of different varieties of rice, including brown rice
(R1), Asemi (R2), solchanmi (R3), sechanmi (R4), sejongchal (R5), and seosi 1 (R6), and legumes varieties
including soybean (B1), chickpea (B2), great northern bean (B3), pea (B4), lentil (B5), and black bean (B6).
Visible appearance analysis reveals that legumes (beans) and rice extrudates appeared more compact as the
concentration of ingredients increased. Meanwhile, the integrity index decreased as the concentration level of
treatment group content decreased (p < 0.05). A marginal difference in textural values is observed between
legume (beans) and rice varieties compared to the control. Furthermore, analysis of nutritional composition
indicates that the crude protein and water holding capacity (WHC) decreased as the concentration of both
extrudates groups decreased (p < 0.05). This study provides useful information regarding the optimization of the
extrusion process and the development of various extrudates by comparative analysis of rice- and legume-based
extrudates
... Disulfide bonds are predominantly found within the alcohol-soluble protein, within and between glutenin molecules, and play a crucial role in forming the protein network structure. However, after exposure to high temperatures (approximately 90 • C) and shearing in the granulator, the disulfide bonds between protein molecules continuously break down, altering the protein structure (Abedi & Pourmohammadi, 2021). This structural change reduces the toughness of gluten pellets and decreases the impact restitution coefficient. ...
To quickly calibrate the discrete element parameters (DEP) of pellets with different moisture content (MC), the angle of repose (AoR) was taken as the target value to conduct experimental and simulation research on gluten pellets. The experimental method obtained the intrinsic parameters, contact parameters, and AoR of pellets with different moisture content. The parameters differed significantly under different moisture content (p < 0.05). The AoR‐MC model (R² = 0.987) was established. The Plackett–Burman test, steepest ascent test, and center compound test were carried out to establish the AoR‐DEP model (R² = 0.969) with a relative error less than or equal to 2.07%. The MC‐DEP model was derived, and verified by the side plate lifting method with a relative error less than or equal to 2.58%. This paper provides a new method for calibrating DEP under different moisture content.
... Such wheat quality indexes can undergo dynamic changes throughout the various stages of wheat production, from cultivation to processing (Banach, Majewska, & Ż uk-Gołaszewska, 2021;Filip et al., 2023). For example, proteins that contribute to the functional and nutritional properties of wheat-based products can undergo aggregation during various stages, such as dough formation, baking, and storage (Abedi, & Pourmohammadi, 2021). Wheat protein aggregation is a complex process that significantly influences the functional properties of wheat-based products (Ortolan, & Steel, 2017). ...
The potential of hyperspectral imaging technology (HIT) for the determination of physicochemical and nutritional components, evaluation of fungal/mycotoxins contamination, wheat varieties classification, identification of non-mildew-damaged wheat kernels, as well as detection of flour adulteration is comprehensively illustrated and reviewed. The latest findings (2018–2023) of HIT in wheat quality evaluation through internal and external attributes are compared and summarized in detail. The limitations and challenges of HIT to improve assessment accuracy are clearly described. Additionally, various practical recommendations and strategies for the potential application of HIT are highlighted. The future trends and prospects of HIT in evaluating wheat quality are also mentioned. In conclusion, HIT stands as a cutting-edge technology with immense potential for revolutionizing wheat quality evaluation. As advancements in HIT continue, it will play a pivotal role in shaping the future of wheat quality assessment and contributing to a more sustainable and efficient food supply chain.
... The retained catalytic activity of enzymes is decreased according to extreme pH, temperature, and pressure conditions. For instance, some of the mechanisms damaging protein integrity irreversibly under such conditions include β-elimination, deamidation, Maillard reactions, oxidation, hydrolysis, and disulfide exchange (Abedi & Pourmohammadi, 2020;Abedi & Pourmohammadi, 2021). ...
High thermostability and catalytic efficiency of α-amylase are required for the industrial applications. To improve catalytic parameters including Michaelis constant, maximum velocity, turnover number, enzyme half-life, and the catalytic efficiency of α-amylase, it was treated alone and/or simultaneously with Ca²⁺ ions (12.5 and 25 mM) and/or ultrasound (USN) (64.5 W, 25 + 40 kHz). The structural analysis of the enzyme (the enzyme’s secondary structure and conformation) was carried out using Fourier transform infrared (FTIR) spectroscopy and circular dichroism (CD) techniques. Moreover, the thermal properties of the enzyme were evaluated using differential scanning calorimetry (DSC). USN + 12.5 mM Ca²⁺ and 25 mM Ca²⁺, changed the maximum velocity (+ 6.5% and + 37.4%), turnover number (+ 6.6% and + 38.2%), enzyme half-life (+ 51.6% and + 113.7%), and catalytic efficiency (+ 18.1% and -3.3%) of α-amylase. The energy barriers of thermo-inactivation and inactivation enthalpy of α-amylase exposed to USN + 25 mM Ca²⁺ were increased by 25% and 5.8%, respectively, without affecting entropy of inactivation, showing how enzyme’s thermal stability was improved after the treatments. The increase in midpoint temperature (35%) and α-helix (14%) values as well as the decrease in the β-sheet structure (39%) of the α-amylase after applying USN + Ca²⁺ (25 mM) confirmed the thermal stability enhancement of α-amylase after the treatment compared to control.
... Snack foods based on cereals and grains are low in nutrient density, high in calories and fat content, and lack some essential amino acids like threonine, tryptophan, and lysine (Ahmad et al., 2017). The combination of moisture, sheer, temperature, and pressure causes rapid cooking during the extrusion process, and resulting in gelatinization of starch, denaturation of protein, inactivation of many native enzymes that cause food deterioration during storage, destruction of naturally occurring toxic substances, and diminishing microbial counts in the final product (Choton et al., 2020;Abedi and Pourmohammadi, 2021). ...
... The ratio of gliadin and glutenin is about 1:1, and the two proteins interact to form gluten network. Gliadin has monomer structures containing four groups including α (25%), β (30%), γ (30%), and ω-gliadins (15%) (2). The glutenin subunit has two fractions containing low-molecular-weight glutenin subunits (LMW-GS) and high-molecularweight glutenin subunits (HMW-GS) (3). ...
Gluten is widely used as a high-quality protein material in the food industry, however, low solubility restricts its development and applications. In this study, gluten was treated with lactate and sodium lactate for lactylation. Lactylation of gluten altered surface charges of the protein, leading to a significant improvement in the solubility. An improvement in oil absorption capacity (OAC) could be attributed to a decrease in protein folding degree after lactylation. In addition, the emulsifying properties of gluten were significantly enhanced. The introduction of lactate group also significantly increased the viscoelasticity of gluten. Fourier transform infrared spectroscopy (FTIR) showed there was a significant decrease in β-turns content and a significant increase in β-sheets content. The folded conformation of gluten was gradually extended after lactation by fluorescence spectroscopy measurement. Both in lactate and sodium lactate treatment, the maximum emission wavelength indicated a blue shift, and the UV intensity showed an increase. These results could demonstrate that lactylation could extend the structure and improve the functional property.
... The complex three-dimensional macromolecular gluten network is produced by covalent bonds (SS bond). On top of that other non-covalent (hydrogen bonds, ionic bonds, hydrophobic bonds) bonds are present and are also crucial to the network formation [33,34]. The creation of this stable and strong matrix is fundamental to obtain stable materials and is influenced by the manufacturing conditions. ...
New lightweight materials made from wheat gluten and disintegrated spruce tree bark were studied. Disintegration of bark by dry milling resulted in rather isodiametric particles, whereas steaming and refining resulted in a more fibrous material. All components were blended and mechanically foamed with a hand mixer and subsequently dried in a conventional oven. The density, thermal conductivity, mechanical properties and water absorption were characterized. Densities vary according to their composition from 60 kg m−3 up to almost 300 kg m−3, as well as thermal conductivity whose lowest values oscillate around 0.04 W m K−1. The mechanical properties are strongly influenced by the type of particle used as reinforcement, with refined particles showing the best results, due to their high aspect ratio. Moreover, the foams produced show water absorption rates ranging from 310 to 480% after 14 h.
... In contrast, the lowest one was found for the gluten derived from conventional cultivation with barley as a forecrop. According to Abedi et al. [41], this trend might be attributed to the internal molecular arrangement between N-and C-terminal domains, which was disrupted by the mechanical stress of the sonication treatment. These terminal domains are the disorder propensity [42]. ...
The potential for enhancing the spring wheat protein content by different cultivation strategies was explored. The influence of ultrasound on the surface and rheological properties of wheat-gluten was also studied. Spring wheat was cultivated over the period of 2018–2020 using two farming systems (conventional and organic) and five forecrops (sugar beet, spring barley, red clover, winter wheat, or oat). The obtained gluten was sonicated using the ultrasonic scrubber. For all organically grown wheat, the protein content was higher than for the conventional one. There was no correlation between the rheological properties of gluten and the protein content in the grain. Gluten derived from organically grown wheat was more elastic than those derived from the conventional one. Sonication enhanced the elasticity of gluten. The sonication effect was influenced by the forecrops. The most elastic gluten after sonication was found for organic barley and sugar beet. The lowest values of tan (delta) were noted for conventional wheat and conventional oat. Cultivation in the monoculture gave gluten with a smaller susceptibility to increase elasticity after sonic treatment. Sonication promoted the cross-linking of protein molecules and induced a more hydrophobic character, which was confirmed by an increment in contact angles (CAs). Most of the organically grown wheat samples showed a lower CA than the conventional ones, which indicated a less hydrophobic character. The gluten surface became rougher with the sonication, regardless of the farming system and applied forecrops. Sonication treatment of gluten proteins rearranged the intermolecular linkages, especially disulfide and hydrophobic bonds, leading to changes in their surface morphology.
... It should be noted though that the strength of the transitions, as well as the size of the mechanical parameters, are not necessarily the same for gliadin, glutenin and the whole wheat gluten. It is depending on several factors, including content and distribution of crosslinks, molar mass, molar mass distribution, amino acid content, polarity differences (degree of water uptake), degree of denaturation, as well as physical and chemical modifications [17,33,39,40]. ...
Many biopolymers are stiff and brittle and require plasticizers. To optimize the choice and amount of plasticizer, the mechanisms behind plasticization need to be understood. For polar biopolymers, such as polysaccharides and proteins, plasticization depends to a large extent on the hydrogen bond network. In this study, glycerol-plasticized protein systems based on wheat gluten were investigated, in combination with the effects of water. The methodology was based on a combination of mechanical tests and molecular dynamics simulations (MD). The simulations accurately predicted the glycerol content where the experimental depression in glass transition temperature (Tg) occurred (between 20 and 30 wt.% plasticizer). They also predicted the strong water-induced depression in Tg. Detailed analysis revealed that in the dry system, the main effect of glycerol was to break protein-protein hydrogen bonds. In the moist system, glycerol was partly outcompeted by water in forming hydrogen bonds with the protein, making the glycerol plasticizer less effective than in dry conditions. These results show that MD can successfully predict the plasticizer concentration at which the onset of efficient plasticization occurs. MD can therefore be an important tool for understanding plasticizer mechanisms, even in a complex system, on a level of detail that is impossible with experiments.
This review presents a comprehensive analysis of plant-based proteins from soybeans, pulses, cereals, and pseudo-cereals by examining their structural properties, modification techniques, bioactivities, and applicability in food systems. It addresses the critical need for a proper utilization strategy of proteins from various plant sources amidst the rising environmental footprint of animal protein production. The inherent composition diversity among plant proteins, their nutritional profiles, digestibility, environmental impacts, and consumer acceptance are compared. The innovative modification techniques to enhance the functional properties of plant proteins are also discussed. The review also investigates the bioactive properties of plant proteins, including their antioxidant, antimicrobial, and antitumoral activities, and their role in developing meat analogs, dairy alternatives, baked goods, and 3D-printed foods. It underscores the consideration parameters of using plant proteins as sustainable, nutritious, and functional ingredients and advocates for research to overcome sensory and functional challenges for improved consumer acceptance and marketability.
