Wheat Gluten Research Articles

Nutritional, anti-nutritional, antioxidant, and sensory properties of meat alternatives derived from wheat gluten and pumpkin seeds

Nutritional, anti-nutritional, antioxidant, and sensory properties of meat alternatives derived from wheat gluten and pumpkin seeds

Changes in rheological properties and structure of wheat gluten proteins induced by transglutaminase.

To elucidate the effect of transglutaminase (TG) on the rheological properties of wheat gluten, this study investigates the underlying mechanisms by analyzing changes in gluten structure. The results demonstrated that the TG-treated gluten samples had higher storage modulus (G') and loss modulus (G″) compared to the control, conversely, creep and recovery strains followed an opposite trend. Notably, the most pronounced effects were observed with adding 2U/g TG for 20-30min. Size exclusion/reversed phase-high performance liquid chromatography profiles revealed that the treatment with TG elevated the levels of glutenin subunits, alongside reduced α- and γ-gliadins, promoting gluten aggregation. Moreover, the extractability of gluten gradually decreased due to TG-induced oxidation of sulfhydryl groups, which formed new disulfide bonds and cross-linked products. This structural modification reduced surface hydrophobic regions and promoted the aggregation of low molecular weight proteins into larger molecular weight aggregates. Microstructural analysis further confirmed that TG enhanced gluten network stability through covalent cross-linking. Overall, this study demonstrates that TG enhances the rheological characteristics of wheat gluten by facilitating the formation of a more robust network structure, driven by cross-linking reactions and disulfide bond formation.

Construction of wheat gluten amyloid fiber/lutein complex delivery system: Formation mechanism, in vitro bioaccessibility, and photothermal stability

Construction of wheat gluten amyloid fiber/lutein complex delivery system: Formation mechanism, in vitro bioaccessibility, and photothermal stability

Improved toughening attributes of coix seed oil high internal phase Pickering emulsion gel via the carrageenan and super-deamidated wheat gluten microparticles interfacial network fotified by the acid-heat induction strategy.

The toughening coix seed oil (CSO) high internal phase Pickering emulsion (CSO-HIPES) and gel (CSO-HIPESG) comprised of carrageenan (CR)/super-deamidated-gluten (SDG) micro-particles (CR/SDG) were investigated via acid-heat induction. Results showed polysaccharide natural deep eutectic solvent (P-NADES) by citric acid-glucose-carrageenan ((CGCR), molar ratio at 1:1:0.035) was the crucial for the preparation of SDG (deamidation degree, 99.38%). P-NADES super-deamidation significantly enhanced emulsifying properties of SDG, increased the exposure of cysteine residues (26.77μM/g) and strengthened hydrogen bonding interactions between SDG protein molecules. Confocal laser scanning microscope displayed the embedded CSO formed uniformly distributed emulsion droplets of smaller size (from 1253.97 to 253.35nm) along with increased electrostatic repulsion (from 8.72 to 21.03mV) of CSO-HIPES. It had excellent interfacial stability for the storage of 90 d under the optimized conditions at pH5. CSO-HIPESG displayed exceptional stability towards heat (70-78°C, 20-40min), NaCl (20-40mol/L), storage (90 d) upon acid-heat induction of CSO-HIPES, in coordination with the retarded oxidation process of CSO. The texture and stability of CSO-HIPESG were determined superior to commercially cream, especially for plasticity and water retention capacity. These findings further validated the potential of CR/SDG-encapsulated CSO as an exceptional interfacial stabilizer for HIPESG applications.

Comparison of the effects of pectin with different esterification degrees on the thermal aggregation of wheat glutenin and gliadin

Our previous study found that pectin with different degrees of esterification (DE) could affect the thermal aggregation of gluten, but the mechanism was not clear. Analyzing the thermal aggregation of glutenin and gliadin supplemented with pectin can clarify this mechanism. With the increase of temperature, the particle size, disulfide bonds and β-sheet of glutenins increased, the surface hydrophobicity (H0) and fluorescence intensity decreased, and the network gradually aggregated, but the change trend of gliadins was opposite. These results suggested that the thermal aggregation of gluten mainly depended on glutenin. Glutenin and gliadin supplemented with low ester pectin (LEP) were in an aggregated state. At 95 °C, LEP (DE = 37 %) increased the particle size of glutenin and gliadin (141.83 μm and 19.91 μm), promoted the conversion of thiol to disulfide bonds, increased β-sheet (34.01 % and 31.13 %), decreased fluorescence intensity (2186.33 and 5165.33) and H0 (49.65 and 369.26). Scanning electron microscope (SEM) indicated that glutenin and gliadin supplemented with LEP retained a dense network structure, especially glutenin. This study elucidated the specific mechanism of how pectin affected the thermal aggregation of gluten. These results provide a more comprehensive theoretical support and scientific basis for understanding how pectin regulates the final quality of gluten-based products.

Effects of experimental wheat and corn gluten on liver tissue in rats: biochemical, histopathological, immunohistochemical and immunofluorescence methods

Effects of experimental wheat and corn gluten on liver tissue in rats: biochemical, histopathological, immunohistochemical and immunofluorescence methods

Enhancing Water Barriers by Protein-Based Surface Treatments for Cellulose-Based Materials

ABSTRACT The global packaging sector has grown consistently, and the use of sustainable materials, including recycled and biodegradable products, is expected to rise. This study focuses on the potential of producing barriers for water and water in moist air (water vapor) from proteins to protect cellulosic materials. Owing to the specific requirements of packaging materials, the main subject of this research was their barrier and strength properties. The scope of this work includes selecting components and their physicochemical treatment to produce functionalized coatings on sprayed paper and pure films, as well as film-coated samples (paper laminated with film). The following tests were used to estimate the hydrophobic, hygroscopic, and strength properties: Cobb absorption, contact angle testing, dynamic vapor sorption, and dynamic mechanical analysis. In most cases, the spray-coated paper and film-coated samples absorbed less liquid water than untreated paper. Wheat gluten protein was the most effective water barrier. In all variants, the vapor sorption, desorption, and hysteresis effects (or the lack thereof) showed significant differences compared to those of cellulosic materials. All variants of the spray-coated and film-coated samples in the dynamic mechanical analysis showed an increase in the strength properties of the samples in comparison to the untreated paper. The increased humidity caused a significant loss in the mechanical properties of all variants, exceeding the strength loss of the untreated control samples.

Investigation of the Effect of Wheat and Corn Gluten on Inflammation, Transglutaminase, Gliadin and IgA Levels in Healthy Rat Intestines

The aim of this study was to evaluate the effects of wheat and corn gluten on some histopathologic parameters such as villus atrophy, crypt hyperplasia, lymphocyte plasma neutrophils and immunohistochemical parameters such as trans glutaminase, gliadin and IgA in the small intestine of healthy male rats without HLA-DQ2 and HLA-DQ8 genes. In the study, 21 healthy newborn male Sprague Dawley rats were fed wheat, corn and soy with the addition of 7 rats in each group from one-day age to 60 days of age. Histopathological (villous atrophy, lymphocyte plasma neutrophil, crypt hyperplasia) and immunohistochemical (transglutaminase, gliadin, IgA) parameter analyses were performed in small intestinal tissue samples. As a result of the study, it was found that the small intestinal villus lengths of the wheat gluten group were longer than the other groups (P < .05). Cryptic hyperplasia was detected most in the soybean group and the lowest in the wheat group (P < .05). Gliadin antibody levels were found to be in the soybean group with the highest and the lowest in the wheat group (P < .05). In healthy male rats lacking HLA-DQ2 and HLA-DQ8 genes, the effect of wheat gluten on crypt hyperplasia and gliadin levels in small intestinal tissue was significantly lower than in soy and corn gluten groups, while its effect on villous atrophy, lymphocyte plasma neutrophil and transglutaminase was limited. In addition, the intestinal villus lengths of the wheat gluten group were significantly higher than those of the corn and soybean groups.

Cost-Benefit Analysis of the Fattening of Morkaraman Lambs with Different Dietary Plant Protein Sources

This study investigated the effects of different plant protein sources incorporated into feed concentrates on the live weight gain and feed conversion ratio of Morkaraman lambs by days 28, 42 and 56 of fattening, and presents a cost-benefit analysis. The study animals included 24 male Morkaraman lambs with a mean age of 9 months, which were assigned to 3 study groups. The dietary plant protein sources provided to the animals were soybean meal and safflower meal in Group I, wheat gluten in Group II, and corn gluten in Group III. The total feed intake values (kg) of Group I, Group II and Group III were 40.75±1.08, 39.18±0.88, and 37.67±0.62, respectively, during the period between days 0-28 of fattening; 62.77±1.67, 60.14±0.96, and 57.54±1.28, respectively, during the period between days 0-42 of fattening; and 83.31±1.89, 77.79±1.43, and 75.97±1.67, respectively, during the period between days 0-56 of fattening (p<0.05). The live weight gain values (kg) of Group I, Group II and Group III during the period between days 0-56 of fattening were 14.82±0.84, 11.97±0.51, and 13.71±0.91, respectively (p<0.05). The feed conversion ratio was observed not to have a statistically significant effect on production yields (p>0.05). In conclusion, while the highest income from live weight gain during the period between days 0-56 of fattening was achieved with the use of soybean meal and safflower meal as dietary plant protein sources, the lowest fattening cost was achieved with the use of corn gluten.

Effects of black soybean peel anthocyanins on the structural and functional properties of wheat gluten.

Wheat gluten (WG) is a crucial cereal protein commonly utilized in the food, biological and pharmaceutical industries. However, WG is poorly soluble in water, resulting in poor functional properties, which restrict its application in the food industry. As a result, there is an urgent need for improving the properties of WG. This study was conducted to examine the functional properties of WG after binding with black soybean peel anthocyanin extract (BAE). Results showed that BAE enhanced the solubility, water-holding and antioxidant capacity, foaming properties and emulsifying activity of WG, while decreasing the emulsion stability. The degree of hydrolysis of WG and retention rate of BAE became higher in the digested WG-BAE complex than in the control groups. Additionally, an analysis was conducted on the mechanism of interaction between cyanidin-3-O-glucoside (C3G) and WG/gliadin (Gli)/glutenin (Glu). The secondary structure of WG/Gli/Glu was altered after adding C3G. C3G had high affinity for WG/Gli/Glu since their binding constants were greater than 104 L mol-1. The primary binding forces between C3G and WG/Gli were hydrophobic interactions, whereas the main interaction forces between C3G and Glu were hydrogen bonding and van der Waals forces. Moreover, C3G increased the thermal stability and changed the network structure of WG/Gli/Glu. This study revealed that BAE effectively enhanced a range of functional properties of WG. The interaction between WG and BAE also improved the bioavailability and nutritional value of them. Furthermore, the interaction mode between BAE and WG was investigated. These findings lay a foundation for utilizing gluten-anthocyanins in the food sector. © 2024 Society of Chemical Industry.

Spray-Dried Wheat Gluten Protein Hydrolysate Microcapsules: Physicochemical Properties, Retention of Antioxidant Capability, and Release Behavior Under Simulated Gastrointestinal Digestion Conditions.

Wheat gluten is a by-product of the wheat starch industry, rich in bioactive peptides. Spray drying is an effective method for improving the stability of bioactive compounds. So, the aim of this study was to produce gluten hydrolysate by different proteases (alcalase, pancreatin, and trypsin) at different times (40-200 min). The hydrolysate with the strongest antioxidant potential (produced by pancreatin after 200 min of hydrolysis) was encapsulated by spray drying. The effect of wall material's type (maltodextrin, potato starch, and their combination at different ratios) on the encapsulation efficiency, physicochemical properties (moisture content, solubility, water activity, tapped and bulk density, and hygroscopicity), release behavior under simulated gastrointestinal digestion conditions, and morphology of microcapsules were evaluated. The microcapsules produced by maltodextrin and potato starch at a 30:70 ratio possessed the highest water activity (0.36), encapsulation efficiency (85.79%), and moisture content (8.2%). An increase in maltodextrin concentration increased the solubility, bulk, and tapped density. SEM images showed that microparticles were spherical with wrinkled surfaces. The microcapsules showed higher stability than free gluten hydrolysate. The combination of maltodextrin and potato starch at a 30:70 ratio could control the release of gluten hydrolysate under simulated gastrointestinal conditions. As a result, the use of maltodextrin and potato starch carriers at a 30:70 ratio in spray drying could effectively protect the bioactive properties of gluten hydrolysate and control its release.

Application of AprX from Pseudomonas paralactis for the improvement of the emulsifying properties of milk, plant and insect protein and estimation of their hydrolysate’s bitter potential

AbstractProtein properties can be modified by selective enzymatic hydrolysis. In this study, the alkaline metalloendopeptidase AprX (Serralysin; EC 3.4.24.40) from Pseudomonas paralactis was used for the tailored hydrolysis of different food proteins resulting in the production of protein hydrolysates with improved emulsifying properties. Sodium caseinate, wheat gluten and buffalo worm protein were used for AprX hydrolysis at 40 °C and pH 8 to cover a spectrum of different protein sources. A maximum degree of hydrolysis (DH) of 13.1 ± 0.2%, 14.2 ± 0.1% and 20.7 ± 0.1% was reached for sodium caseinate, wheat gluten and the worm protein, respectively. The corresponding hydrolysate properties were analyzed regarding their particle size, peptide composition, solubility, viscosity, surface hydrophobicity and interfacial tension. The emulsifying properties were investigated by the oil-droplet size, ζ-potential and stability of emulsions prepared from the hydrolysates. Using partially hydrolyzed sodium caseinate (DH = 10.6%) as an emulsifier lead to an eightfold increase of the emulsion stability (t1/2 = 180 ± 0 min) compared to unhydrolyzed sodium caseinate. The emulsion stability using wheat gluten hydrolysates (DH = 11.9%) was increased 30-fold (t1/2 = 45 ± 5 min). Simultaneously, the solubility of gluten was increased by 60%. Buffalo worm hydrolysates (DH = 14.6%) had a twofold (t1/2 = 85 ± 5 min) increased emulsion stability. In conclusion, AprX can be used to improve the solubility and emulsifying properties of food proteins at a relatively high DH.

Effects of dietary cysteamine addition to a plant-based diet on growth performance, body composition, hepatosomatic histological structure and metabolism of taurine synthesis in turbot (Scophthalmus maximus L.)

This present study was conducted to illustrate the effect of dietary cysteamine on feeding, growth, biochemistry composition, hepatosomatic histological structure and metabolism of taurine synthesis in juvenile turbot (Scophthalmus maximus L.) (2.0 ± 0.01 g) fed high plant protein diets. A fishmeal-based diet (72.5% FM) was designed as the control diet (DietFM). Four isonitrogenous and isolipidic diets consist of 14.0% FM, 23.0% soybean meal and 30.0% wheat gluten meal, which were formulated to substitute FM with 0.0%, 0.05%, 0.1% and 0.15% cysteamine hydrochloride (labeled as DietPP, DietCS-0.05%, DietCS-0.1% and DietCS-0.15% respectively). Fish were stochastically allocated into fifteen 200L tanks and fed twice daily (06:30 and 18:30) to apparent satiation for 9 weeks. Feed intake (FI) in fish-fed DietCS-0.05% was conspicuously higher than that in fish-fed DietPP (p<0.05), and no notable difference was discovered among fish-fed diets with cysteamine inclusion (p>0.05). No conspicuously upward trend was found with the increase of dietary cysteamine in FBW, SGR, WGR, FER, PER, and SR when there was a downward trend in CF, VSI, and HSI (p>0.05). A remarkable increase was discovered from 0.0% to 0.05% cysteamine inclusion in ash content (p<0.05) when no noticeable difference was observed among all the cysteamine inclusion groups in moisture, protein, and lipid content (p>0.05). Only the body taurine content showed a notable increase between fish-fed DietCS-0.05% and fish-fed DPP among the indexes of body taurine, liver taurine, and serum taurine content (p<0.05), whereas no notable difference was observed in hepatosomatic L-cysteine sulfinate decarboxylase (CSD) and cysteamine dioxygenase (CDO) activities among all the cysteamine inclusion groups (p>0.05). The cellular morphology and cell veins in the liver of fish-fed diets with cysteamine inclusion were clearer than those of fish-fed DPP. The results showed that 0.05% cysteamine addition in a high plant protein diet is optimal.

Synergistic growth suppression of Fusarium oxysporum MLY127 through Dimethachlon Nanoencapsulation and co-application with Bacillus velezensis MLY71

Fusarium oxysporum is a destructive plant pathogen with robust survival mechanisms, complicating control efforts. This study aimed to develop nanoformulated fungicides, screen antagonistic bacteria, and evaluate their combined efficacy. A novel self-emulsifying nanoemulsion (DZW) was formulated using zein and benzaldehyde-modified wheat gluten (BgWG) as carriers for dimethachlon (DTN). The preparation process optimized material ratios and emulsification techniques. Concurrently, antagonistic bacterial strains against F. oxysporum were screened via the plate standoff method, identifying Bacillus velezensis MLY71 as both antagonistic and compatible with DTN. The DZW nanoemulsion achieved a particle size of 93.22 nm, an encapsulation efficiency (EE) of 90.57%, and a DTN loading capacity (LC) of 67.09%, with sustained release over 96 h. The combination of DTN (0.04 mg·mL⁻¹) and B. velezensis MLY71 (1 × 10⁴ CFU·mL⁻¹) achieved a 76.66% inhibition rate against F. oxysporum MLY127, 1.71 times greater than DTN alone, indicating significant synergy. At a DTN concentration of 0.20 mg·mL⁻¹, the combination of DZW and MLY71 showed a synergy coefficient of 1.33. This synergy was also observed in soil environments, indicating its adaptability for controlling soil-borne pathogens. As sustainable management continues to gain attention in agricultural disease control, this study offers a promising strategy for achieving higher efficacy with the same fungicide dose or satisfactory control with reduced fungicide application. The excellent drug-loading performance of BgWG also expanded the applications of the wheat by-product gluten.

Physicochemical and structural properties of novel cornmeal, pea protein isolate and wheat gluten meat analogues prepared by high moisture extrusion

Physicochemical and structural properties of novel cornmeal, pea protein isolate and wheat gluten meat analogues prepared by high moisture extrusion

Rye secalin isolates to develop reference materials for gluten detection.

Gluten-free products must not contain more than 20mg/kg of gluten to be safe for consumption by celiac disease patients. Almost all analytical methods are calibrated to wheat, wheat gluten or gliadin, and there is no rye-specific reference material available. The aim of this study was to assess the effect of the harvest year on rye gluten composition and to generate distinct rye isolates to serve as calibration standards. Four different extraction procedures of a specific rye cultivar mixture were tested yielding prolamins (PROL), glutelins (GLUT), gluten (G) and acetonitrile/water-extractable proteins (AWEP). The isolates were characterized using different methods such as RP-HPLC, GP-HPLC, SDS-PAGE and LC-MS/MS. The isolates were evaluated in the R5 ELISA which resulted in the following response order: PROLiso>AWEPiso>Giso>GLUTiso. This paper represents a significant step towards improving gluten analysis, particularly in the context of rye-contaminated gluten-free products.

Effects of interaction between wheat bran dietary fiber and gluten protein on gluten protein aggregation behavior.

Effects of wheat bran dietary fiber (WBDF) as a nutritional additive on flour products quality mainly depends on the interaction between WBDF and gluten protein. In this study, the effects and mechanisms of WBDF with different particle sizes and additive amounts on gluten protein aggregation behavior were investigated. The results showed that the addition of WBDF led to a decrease in free sulfhydryl content, particle size, molecular weight and gluten macromer (GMP) content, an increase in zeta potential and SDS-extractable protein content, and a deterioration in the gluten network morphology compared to the control group, suggesting that the aggregation behavior of gluten protein was inhibited. When WBDF was added at 3% and 6%, dilution effect, mechanical shear, steric hindrance, and non-covalent binding were the main mechanisms leading to depolymerization. Further addition of WBDF (9%, 12%) inhibited the depolymerization of gluten protein due to competitive hydration and non-covalent binding. However, when WBDF was added at 15%, the dilution effect, mechanical shear and steric hindrance of WBDF (88μm<particle size<150μm) dominated, and their inhibitory of aggregation induced the formation of a loose gluten network structure. In contrast, the weaker mechanical shear and steric hindrance effects of WBDF (particle size<88μm) mitigated the degradation of gluten network structures by WBDF.

Non-thermal shearing effect on gluten conformation for plant-based anisotropic structures

Wheat gluten manipulation to obtain fibrillar structures is a promising approach for elaborating meat analogs on large or small scales. Alternatively to extrusion, mild methods can save energy and avoid sensory attributes/protein degradation. This study aimed to evaluate low-temperature shearing to create gluten-based fibers, assessing the material structure as a function of processing intensity. The effect of the non-thermal shearing length (up to 10 min) and added mechanical energy (up to 565.5 J/g) applied on a highly hydrated wheat gluten-based matrix was investigated in terms of density, exudation, secondary protein structure (FTIR), protein network attributes (confocal laser scanning microscopy), elongation attributes, morphology (SEM), and anisotropicity of cooked matrices. The progression of the shearing process was associated with the development of β-sheet secondary structures (26 % to 50 % predominancy), higher elongation attributes, raw matrix density, and anisotropicity of cooked matrices. Higher protein vessel length and width were associated with the formation and stacking of β-sheets. Exudation, cooked matrix density, and endpoint rate were associated with higher α-helices content (lowered from 39 % to 11 % of predominancy) and lower shearing-added energies. A principal component analysis of the entire dataset confirmed these observations, and the morphology revealed the evolution of the matrix organization during the shearing process. These results underscore the potential of mild-temperature shearing of a highly hydrated gluten-enriched matrix to alter the protein conformation, opening possibilities for controlling fiber structure development, valid for new foods such as meat analogs.

Mechanistic insights into curdlan-induced fibrous structure formation in soybean protein and wheat gluten extrudates via dead-stop operation and rheological characterization

Mechanistic insights into curdlan-induced fibrous structure formation in soybean protein and wheat gluten extrudates via dead-stop operation and rheological characterization

Structural analysis of wheat glutenins by diagonal electrophoresis for disulfide bond detection

Structural analysis of wheat glutenins by diagonal electrophoresis for disulfide bond detection