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1.
J Biomed Mater Res A ; 2024 Jul 04.
Article in English | MEDLINE | ID: mdl-38963322

ABSTRACT

Corneal blindness affects over 10 million patients worldwide. Due to the limited supply of donor corneas and frequent graft failure, bioengineered alternatives are crucial. To overcome drawbacks associated with corneal substitutes from synthetic biomaterials, fabrication from plant-derived biomaterials is a potential alternative. Herein, soy protein and glutenin in combination with different crosslinkers were evaluated for fabrication of corneal substitutes. Optical, mechanical, and biochemical properties of fabricated constructs and control rabbit corneas were evaluated in vitro. Soy protein crosslinked with peroxidase/H202 possessed transparency and mechanical properties comparable to controls, although their water content and biocompatibility were inferior. In contrast, soy protein crosslinked with tannic acid showed similar water content, tensile strength, and biocompatibility as rabbit corneas; however, these constructs displayed significantly lower transparency and higher strain to failure. Finally, glutenin cross-linked using formaldehyde showed excellent transparency, strain to failure, and biocompatibility, however; they exhibited significantly lower water content and tensile strength than controls. This study is the first to establish CIELAB color values for the rabbit cornea, allowing quantitative optical evaluation of tissue-engineered substitutes. Thus, a crosslinking strategy utilizing plant-derived proteins for fabrication of constructs with properties comparable to rabbit corneas is a promising direction for development of tissue-engineered corneal substitutes.

2.
J Sci Food Agric ; 2024 Jul 05.
Article in English | MEDLINE | ID: mdl-38967243

ABSTRACT

BACKGROUND: Mycotoxin contamination of food has been gaining increasing attention. Hidden mycotoxins that interact with biological macromolecules in food could make the detection of mycotoxins less accurate, potentially leading to the underestimation of the total exposure risk. Interactions of the mycotoxins alternariol (AOH) and alternariol monomethyl ether (AME) with high-molecular glutenin were explored in this study. RESULTS: The recovery rates of AOH and AME (1, 2, and 10 µg kg-1) in three types of grains (rice, corn, and wheat) were relatively low. Molecular dynamics (MD) simulations indicated that AOH and AME bound to glutenin spontaneously. Hydrogen bonds and π-π stacking were the primary interaction forces at the binding sites. Alternariol with one additional hydroxyl group exhibited stronger binding affinity to glutenin than AME when analyzing average local ionization energy. The average interaction energy between AOH and glutenin was -80.68 KJ mol-1, whereas that of AME was -67.11 KJ mol-1. CONCLUSION: This study revealed the mechanisms of the interactions between AOH (or AME) and high-molecular glutenin using MD and molecular docking. This could be useful in the development of effective methods to detect pollution levels. These results could also play an important role in the evaluation of the toxicological properties of bound altertoxins. © 2024 Society of Chemical Industry.

3.
Food Chem ; 455: 139909, 2024 Oct 15.
Article in English | MEDLINE | ID: mdl-38843717

ABSTRACT

In our study, we explored how gluten's role during dough formation and thermal processing can mitigate the adverse effects of physical factors on product quality. We discovered that a gluten network with a gliadin/glutenin ratio of 5:5 effectively limits oil penetration into the dough's core. This particular ratio is found to reduce the exposure of hydrophobic groups due to the presence of hydrated ß-sheet structures. In contrast, gluten networks with higher gliadin proportions than typical wheat gluten tend to be looser, leading to increased chromophore exposure and facilitating more oil absorption. These observations highlighted the complex link between changes in gluten structure, varying protein compositions, and oil content in fried dough sticks. This research provided a foundation for developing specialized low-fat wheat flour and improving the quality of fried dough products.


Subject(s)
Cooking , Flour , Glutens , Hot Temperature , Triticum , Glutens/chemistry , Glutens/analysis , Flour/analysis , Triticum/chemistry , Gliadin/chemistry , Gliadin/analysis , Bread/analysis
4.
Sci Rep ; 14(1): 10940, 2024 05 13.
Article in English | MEDLINE | ID: mdl-38740888

ABSTRACT

Improving the baking quality is a primary challenge in the wheat flour production value chain, as baking quality represents a crucial factor in determining its overall value. In the present study, we conducted a comparative RNA-Seq analysis on the high baking quality mutant "O-64.1.10" genotype and its low baking quality wild type "Omid" cultivar to recognize potential genes associated with bread quality. The cDNA libraries were constructed from immature grains that were 15 days post-anthesis, with an average of 16.24 and 18.97 million paired-end short-read sequences in the mutant and wild-type, respectively. A total number of 733 transcripts with differential expression were identified, 585 genes up-regulated and 188 genes down-regulated in the "O-64.1.10" genotype compared to the "Omid". In addition, the families of HSF, bZIP, C2C2-Dof, B3-ARF, BES1, C3H, GRF, HB-HD-ZIP, PLATZ, MADS-MIKC, GARP-G2-like, NAC, OFP and TUB were appeared as the key transcription factors with specific expression in the "O-64.1.10" genotype. At the same time, pathways related to baking quality were identified through Kyoto Encyclopedia of Genes and Genomes. Collectively, we found that the endoplasmic network, metabolic pathways, secondary metabolite biosynthesis, hormone signaling pathway, B group vitamins, protein pathways, pathways associated with carbohydrate and fat metabolism, as well as the biosynthesis and metabolism of various amino acids, have a great deal of potential to play a significant role in the baking quality. Ultimately, the RNA-seq results were confirmed using quantitative Reverse Transcription PCR for some hub genes such as alpha-gliadin, low molecular weight glutenin subunit and terpene synthase (gibberellin) and as a resource for future study, 127 EST-SSR primers were generated using RNA-seq data.


Subject(s)
Gene Expression Profiling , Gene Expression Regulation, Plant , RNA-Seq , Triticum , Triticum/genetics , Triticum/growth & development , Triticum/metabolism , RNA-Seq/methods , Gene Expression Profiling/methods , Transcriptome , Edible Grain/genetics , Edible Grain/metabolism , Cooking , Bread , Plant Proteins/genetics , Plant Proteins/metabolism , Genotype , Flour
5.
BMC Plant Biol ; 24(1): 395, 2024 May 14.
Article in English | MEDLINE | ID: mdl-38745139

ABSTRACT

BACKGROUND: In common wheat (Triticum aestivum L.), allelic variations in the high-molecular-weight glutenin subunits Glu-B1 locus have important effects on grain end-use quality. The Glu-B1 locus consists of two tightly linked genes encoding x- and y-type subunits that exhibit highly variable frequencies. However, studies on the discriminating markers of the alleles that have been reported are limited. Here, we developed 11 agarose gel-based PCR markers for detecting Glu-1Bx and Glu-1By alleles. RESULTS: By integrating the newly developed markers with previously published PCR markers, nine Glu-1Bx locus alleles (Glu-1Bx6, Glu-1Bx7, Glu-1Bx7*, Glu-1Bx7 OE, Glu-1Bx13, Glu-1Bx14 (-) , Glu-1Bx14 (+)/Bx20, and Glu-1Bx17) and seven Glu-1By locus alleles (Glu-1By8, Glu-1By8*, Glu-1By9, Glu-1By15/By20, Glu-1By16, and Glu-1By18) were distinguished in 25 wheat cultivars. Glu-1Bx6, Glu-1Bx13, Glu-1Bx14 (+)/Bx20, Glu-1By16, and Glu-1By18 were distinguished using the newly developed PCR markers. Additionally, the Glu-1Bx13 and Glu-1Bx14 (+)/Bx20 were distinguished by insertions and deletions in their promoter regions. The Glu-1Bx6, Glu-1Bx7, Glu-1By9, Glu-1Bx14 (-), and Glu-1By15/By20 alleles were distinguished by using insertions and deletions in the gene-coding region. Glu-1By13, Glu-1By16, and Glu-1By18 were dominantly identified in the gene-coding region. We also developed a marker to distinguish between the two Glu-1Bx14 alleles. However, the Glu-1Bx14 (+) + Glu-1By15 and Glu-1Bx20 + Glu-1By20 allele combinations could not be distinguished using PCR markers. The high-molecular-weight glutenin subunits of wheat varieties were analyzed by ultra-performance liquid chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the findings were compared with the results of PCR analysis. CONCLUSIONS: Seven Glu-1Bx and four Glu-1By allele detection markers were developed to detect nine Glu-1Bx and seven Glu-1By locus alleles, respectively. Integrating previously reported markers and 11 newly developed PCR markers improves allelic identification of the Glu-B1 locus and facilitates more effective analysis of Glu-B1 alleles molecular variations, which may improve the end-use quality of wheat.


Subject(s)
Alleles , Glutens , Polymerase Chain Reaction , Triticum , Glutens/genetics , Glutens/metabolism , Triticum/genetics , Genetic Markers , Polymerase Chain Reaction/methods , Molecular Weight
6.
J Sci Food Agric ; 2024 Apr 09.
Article in English | MEDLINE | ID: mdl-38591632

ABSTRACT

BACKGROUND: Gluten composition is an important quality parameter of wheat flour. Reversed-phase high-performance liquid chromatography (RP-HPLC) is a state-of-the-art method for its analysis. As this is a very labour-intensive and time-consuming procedure, alternative faster methods are desirable. Enzyme-linked immunosorbent assay (ELISA) is a high-throughput method often used for the analysis of gluten traces in gluten-free products. In this proof-of-principle study, we introduce an experimental triple ELISA for the relative quantitation of gliadins, high-molecular-weight glutenin subunits (HMW-GS) and low-molecular-weight glutenin subunits (LMW-GS) of one wheat flour extract. RESULTS: The results of 80 common wheat flour samples obtained from the triple ELISA and RP-HPLC were correlated. The results for gliadins (r = 0.69) and HMW-GS (r = 0.81) showed a medium and high correlation, respectively. Only a very weak correlation of ELISA and RP-HPLC results was observed for LMW-GS (r = 0.49). Results for glutenins (r = 0.69) and gluten (r = 0.72) had a medium correlation. The gliadin/glutenin ratio (r = 0.47) and LMW-GS/HMW-GS ratio (r = 0.40) showed a weak or no correlation. The gliadin, LMW-GS and gluten contents were lower and the HMW-GS content was higher in the ELISA measurement compared to RP-HPLC. CONCLUSION: The quantitation of gliadins and HMW-GS by the experimental triple ELISA showed comparable results to RP-HPLC, whereas no strong correlation between the results from the two methods was found for LMW-GS. Overall, the experimental triple ELISA is suitable for relative gluten quantitation, especially for the analysis of large sample sets. Further work will focus on improving the experimental procedure of the ELISA. © 2024 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

7.
Int J Biol Macromol ; 267(Pt 1): 131438, 2024 May.
Article in English | MEDLINE | ID: mdl-38583845

ABSTRACT

A glutenin (G)-chitosan (CS) complex (G-CS) was cross-linked by water annealing with aim to prepare structured 3D porous cultured meat scaffolds (CMS) here. The CMS has pore diameters ranging from 18 to 67 µm and compressive moduli from 16.09 to 60.35 kPa, along with the mixing ratio of G/CS. SEM showed the porous organized structure of CMS. FTIR and CD showed the increscent content of α-helix and ß-sheet of G and strengthened hydrogen-bondings among G-CS molecules, which strengthened the stiffness of G-CS. Raman spectra exhibited an increase of G concentration resulted in higher crosslinking of disulfide-bonds in G-CS, which aggrandized the bridging effect of G-CS and maintained its three-dimensional network. Cell viability assay and immuno-fluorescence staining showed that G-CS effectively facilitated the growth and myogenic differentiation of porcine skeletal muscle satellite cells (PSCs). CLSM displayed that cells first occupied the angular space of hexagon and then ring-growth circle of PSCs were orderly formed on G-CS. The texture and color of CMS which loaded proliferated PSCs were fresh-meat like. These results showed that physical cross-linked G-CS scaffolds are the biocompatible and stable adaptable extracellular matrix with appropriate architectural cues and natural micro-environment for structured CM models.


Subject(s)
Chitosan , Meat , Tissue Scaffolds , Chitosan/chemistry , Animals , Tissue Scaffolds/chemistry , Porosity , Swine , Tissue Engineering/methods , Cell Survival/drug effects , Biocompatible Materials/chemistry , Cell Differentiation/drug effects , Cell Proliferation/drug effects , In Vitro Meat
8.
Plants (Basel) ; 13(5)2024 Mar 06.
Article in English | MEDLINE | ID: mdl-38475588

ABSTRACT

The criteria of "Distinctness, Uniformity and Stability" as well as a high "overall quality index" are used to register the Italian modern varieties to the national register. Differently, local conservation varieties can be certified under different EU Directives that facilitate, as an overall objective, the preservation of biodiversity and the containment of genetic erosion. In recent years, products derived from ancient grains are perceived to be healthier and more sustainable by consumers, especially in Italy, with consequent higher market prices. The ancient tetraploid wheat varieties registered in the national register of conservation varieties amount to 28, 24 of which are Sicilian. They are supposed to have wide genetic variability compared to modern ones, making them vulnerable to fraud because they are difficult to trace. It is therefore important to have tools able to discriminate between autochthonous Sicilian varieties. This can be completed by gluten proteins composition, which also provides information on the technological properties of derived products. Fifty-one accessions belonging to twenty-two ancient varieties of Sicilian tetraploid (mostly durum) wheat were analyzed. Although wide intra-accession and intra-varietal variability measurements were assessed, the gliadin pattern of bulks of seeds belonging to each variety was discriminatory. Moreover, differences in technological attitudes were found between landraces. This paves the way to use gluten protein patterns for traceability, allowing local farmers and producers to valorize their products and assure consumers regarding the transparency of the entire supply chain.

9.
Food Chem ; 446: 138856, 2024 Jul 15.
Article in English | MEDLINE | ID: mdl-38430765

ABSTRACT

In this study, we examined the effects of various sodium alginate (ALG) concentrations (0.2%-0.8%) on the functional and physicochemical characteristics of succinylated walnut glutenin (GLU-SA). The results showed that acylation decreased the particle size and zeta potential of walnut glutenin (GLU) by 122- and 0.27-fold, respectively. In addition, the protein structure unfolded, providing conditions for glycosylation. After GLU-SA was combined with ALG, the surface hydrophobicity decreased and the net negative charge and disulfide bond content increased. The protein structure was analyzed by FTIR, Endogenous fluorescence spectroscopy, and SEM, and ALG prompted GLU-SA cross-linking to form a stable three-dimensional network structure. The results indicated that dual modification improved the functional properties of the complex, especially its potential protein gel and emulsifying properties. This research provide theoretical support and a technical reference for expanding the application of GLU in the processing of protein and oil products.


Subject(s)
Juglans , Juglans/chemistry , Glycosylation , Glutens/chemistry , Nuts/chemistry
10.
Food Chem (Oxf) ; 8: 100195, 2024 Jul 30.
Article in English | MEDLINE | ID: mdl-38327512

ABSTRACT

This study investigated the effects of wheat lipoxygenase isozyme III (LOX III) and its truncated form, Mini-LOX III, on flour dough properties using yeast-expressed recombinant enzymes and hypothesized their potential to enhance cereal-based food quality. These enzymes actively catalyze linoleic acid, which is crucial for dough formation. The addition of recombinant LOX III and Mini-LOX III to wheat flour significantly changed glutenin protein composition. An increase in the amount of soluble glutenin and a shift in polypeptide distribution were observed, marked by a decrease in the high-molecular-weight regions and an increase in the low-molecular-weight regions. This result reflects the role of enzymes in altering the hydrophobicity of glutenin surfaces, thereby affecting the protein solubility and dough properties. Thus, recombinant LOX III and Mini-LOX III offer new avenues for enhancing the texture and quality of cereal-based foods, providing valuable insights into the role of wheat LOX in flour processing and its potential industrial applications.

11.
ACS Biomater Sci Eng ; 10(2): 814-824, 2024 02 12.
Article in English | MEDLINE | ID: mdl-38226596

ABSTRACT

Cultivated meat production is a promising technology to generate meat while reducing the reliance on traditional animal farming. Biomaterial scaffolds are critical components in cultivated meat production, enabling cell adhesion, proliferation, differentiation, and orientation. In the present work, naturally derived glutenin was fabricated into films with and without surface patterning and in the absence of toxic cross-linking or stabilizing agents for cell culture related to cultivated meat goals. The films were stable in culture media for at least 28 days, and the surface patterns induced cell alignment and guided myoblast organization (C2C12s) and served as a substrate for 3T3-L1 adipose cells. The films supported adhesion, proliferation, and differentiation with mass balance considerations (films, cells, and matrix production). Freeze-thaw cycles were applied to remove cells from glutenin films and monitor changes in glutenin mass with respect to culture duration. Extracellular matrix (ECM) extraction was utilized to quantify matrix deposition and changes in the original biomaterial mass over time during cell cultivation. Glutenin films with C2C12s showed mass increases with time due to cell growth and new collagen-based ECM expression during proliferation and differentiation. All mass balances were compared among cell and noncell systems as controls, along with gelatin control films, with time-dependent changes in the relative content of film, matrix deposition, and cell biomass. These data provide a foundation for cell/biomaterial/matrix ratios related to time in culture as well as nutritional and textural features.


Subject(s)
Biocompatible Materials , In Vitro Meat , Animals , Glutens/chemistry , Muscles
12.
Food Chem ; 441: 138371, 2024 May 30.
Article in English | MEDLINE | ID: mdl-38218148

ABSTRACT

The qualities of wheat dough are influenced by the high-molecular-weight glutenin subunits (HMW-GS), a critical component of wheat gluten protein. However, it is still unknown how HMW-GS silencing affects the aggregation characteristics of dough. Two groups of near-isogenic wheat were used to study the effects of HMW-GS silencing on dough aggregation characteristics, dough texture characteristics, and dough microstructure. It was observed that the content of gliadin in LH-11 strain significantly increased compared to the wild-type (WT). Additionally, the amount of glutenin macropolymer and the glutenin/gliadin both decreased. The aggregation characteristics and rheological characteristics of the dough in LH-11 strain were significantly reduced, and the content of ß-sheet in the dough was significantly reduced. The HMW-GS silencing resulted in a reduction in the aggregation of the gluten network in the dough, which related to the alteration of the secondary and microstructure of the gluten.


Subject(s)
Gliadin , Glutens , Gliadin/metabolism , Molecular Weight , Glutens/chemistry , Triticum/chemistry , Flour , Protein Subunits/chemistry
13.
Int J Biol Macromol ; 259(Pt 2): 129280, 2024 Feb.
Article in English | MEDLINE | ID: mdl-38211911

ABSTRACT

The retrogradation of wheat amylopectin during cold storage is the main reason for the increasing hardness of flour products such as steamed bread, bread and pastries, etc. Addition of gluten protein components is a green, safe, cheap and efficient method to inhibit the retrogradation of wheat amylopectin. In this paper, as being stored at 4 °C for 7 d, retrogradation rate of wheat amylopectin decreased from 55.02 % to 14.37 % after it was mixed with 20 % alkali-soluble glutenin (ASG) at 30 °C for 90 min, a 73.8 % reduction. The infrared results showed that the intensity of bending vibration of water molecules and intra-molecular ß-sheet content of ASG decreased during the interaction between amylopectin and ASG. Meanwhile, intermolecular ß-sheet and random coil contents of ASG increased. The results of 13C Solid-state NMR indicated that Qß, Pγ and Lγ of ASG involved in interaction of wheat amylopectin, ASG and molecule of water. Under the optimal conditions, the interaction of wheat amylopectin and ASG began to form spheres containing disulfide bonds, resulting in the attenuation or disappearance of the diffraction peak at 2θ 19.7°, which may be marked as the criterion for the best mixing time of wheat amylopectin and ASG. The retrogradation kinetic index (n) of wheat amylopectin decreased significantly with the addition of ASG and formation of disulfide bond was the key factor. ASG could be potentially used as an anti-retrogradation agent for amylopectin.


Subject(s)
Amylopectin , Starch , Amylopectin/chemistry , Starch/chemistry , Triticum/chemistry , Glutens/chemistry , Water/chemistry , Disulfides , Bread
14.
Molecules ; 28(23)2023 Nov 27.
Article in English | MEDLINE | ID: mdl-38067520

ABSTRACT

The changes in the secondary structure of individual gluten protein fractions (gliadin and glutenin) caused by the supplementation of model dough with eight phenolic acids were analysed. Gliadins and glutenins were extracted from gluten samples obtained from overmixed dough. The changes in the gliadin secondary structure depended on the amount of phenolic acid added to the dough. Higher acid concentrations (0.1% and 0.2%) led to a significant reduction in the amount of α-helices and to the formation of aggregates, non-ordered secondary structures, and antiparallel ß-sheets. After the addition of acids at a lower concentration (0.05%), the disaggregation of pseudo-ß-sheet structures and the formation of ß-turns, hydrogen-bonded ß-turns, and antiparallel ß-sheets were detected. In the case of glutenin, most of the phenolic acids induced the formation of intermolecular hydrogen bonds between the polypeptide chains, leading to glutenin aggregation. When phenolic acids were added at a concentration of 0.05%, the process of protein folding and regular secondary structure formation was also observed. In this system, antiparallel ß-sheets and ß-turns were created at the expense of pseudo-ß-sheets.


Subject(s)
Gliadin , Glutens , Gliadin/chemistry , Glutens/chemistry , Hydroxybenzoates
15.
Int J Mol Sci ; 24(24)2023 Dec 08.
Article in English | MEDLINE | ID: mdl-38139075

ABSTRACT

Wheat is a prominent allergenic food that can trigger life-threatening anaphylaxis. Presently, it remains unclear whether wheat glutenin (WG) extract possesses inherent sensitization potential independently, without the use of adjuvants, and whether it can sensitize mice to the extent of inducing life-threatening systemic anaphylaxis. In this study, we tested the hypothesis that repeated skin exposures to WG extract without adjuvant will sensitize mice with the resultant anaphylactic reaction upon systemic WG challenge. Balb/c mice were bred and maintained on a strict plant protein-free diet and were repeatedly exposed to a WG extract or vehicle once a week for 9 weeks. WG-specific (s)IgE and total (t)IgE levels were quantified. Mice were challenged with WG extract to induce anaphylactic reactions as measured by hypothermic shock response (HSR) and mucosal mast cell degranulation response (MMCR). We also conducted proteomic analysis of 120 spleen immune markers. These skin-sensitized mice exhibited exposure-dependent IgE responses and near-fatal anaphylaxis upon challenge. Proteomic analysis identified seven dramatically elevated immune biomarkers in anaphylactic mice. These data reveal that WG is intrinsically allergenic, and that chronic skin exposure to WG extract can prime the mice for potentially fatal anaphylaxis.


Subject(s)
Anaphylaxis , Mice , Animals , Allergens , Triticum , Proteomics , Immunoglobulin E , Plant Breeding , Adjuvants, Immunologic , Mice, Inbred BALB C , Adjuvants, Pharmaceutic
16.
Curr Res Food Sci ; 7: 100622, 2023.
Article in English | MEDLINE | ID: mdl-38021258

ABSTRACT

Wheat is the most important crops worldwide, providing about one-fifth of the daily protein and calories for human consumption. The quality of cereal-based products is principally governed by the genetic basis of gluten (glutenin and gliadin proteins), which exists in a wide range of variable alleles and is controlled by clusters of genes. There are certain limitations associated with gluten characteristics, which can be genetically manipulated. The present review aimed to investigate the correlation between the genetic characteristics of gluten protein components and wheat-based product's quality. According to various references, Glu-B1d (6 + 8), Glu-B1h (14 + 15) and Glu-B1b (7 + 8) are related to higher gluten strength and pasta quality, while, subunits Dx2 + Dy12 and Dx5 + Dy10, are usually present at the Glu-D1 locus in bread wheat, resulted in lower cooked firmness in pasta. Moreover, introducing Gli-D1/Glu-D3 and Glu-D1 loci into durum wheat genomes, causing to provide the maximum values of gluten index in pasta products. 1Dx5 + 1Dy10 alleles determine the level of increase in dough's consistency, elasticity, viscosity, and extensibility quality of baking and appropriate bread loaf volume, while 1Dx2 + 1Dy12 as the alleles associated with poor baking quality, being more suitable for soft wheat/pastry end uses. Bx7, Bx7OE, 1Bx17 + 1By18, 1Bx13 + 1By16, Bx7 + By9 and 1Bx7 + 1By8 at Glu-B1alleles and 1Ax2* found on Glu-A1, augmented dough strength and has positive effects on consistency, extensibility, viscosity, and elasticity of bread dough. Breeding programs by genome editing have made gluten a promoting component for improving cereal-based products.

17.
Vavilovskii Zhurnal Genet Selektsii ; 27(5): 433-439, 2023 Sep.
Article in English | MEDLINE | ID: mdl-37808211

ABSTRACT

Studies of the genetic base and polymorphism of bread wheat cultivars aimed at identifying alleles of genes associated with high baking and other economically valuable traits seem to be relevant, since bread wheat, along with all representatives of the Triticeae tribe, has a huge genetic potential for creating cultivars with high technological and rheological properties of grain flour. The aim of this study was sequencing and analysis of the nucleotide sequences of the Glu-B1-1 gene, and analysis of the predicted amino acid sequences of its protein product in three cultivars of bread wheat. Thus, in the course of genotyping cultivars and lines of bread wheat for the Glu-B1-1 gene, in the cultivars 'Avesta', 'Leningradka krupnozernaya' and line C-75094, previously undescribed changes in the size of amplifiable regions of the Glu-B1-1 gene for high-molecular weight glutenins were found. Comparative analysis of the nucleotide sequences of these genes with known sequences showed the presence of two deletions in 'Avesta' and C-75094 and the presence of seven single-nucleotide substitutions in 'Leningradka krupnozernaya'. Alignment of the predicted Glu-B1 amino acid sequences of the studied accessions and the standard cultivar carrying the Glu-B1-a allele showed that deletions in the amino acid sequences of 'Avesta' and C-75094 accessions are localized in the central domain of the protein and affect the amount of tri-, hexa-, and nonapeptides, and in 'Leningradka krupnozernaya', a decrease in GQQ and PGQGQQ by one unit was revealed. In addition, substitutions of five amino acids were found in 'Leningradka krupnozernaya'. Thus, we have found previously undescribed deletions and substitutions in the nucleotide sequences of the Glu-B1-1 gene for high-molecular-weight glutenins, which lead to changes in amino acid sequences in functionally important regions, namely, in the central domains of protein molecules. The identified mutations can be used for genotyping bread wheat cultivars.

18.
Int J Biol Macromol ; 248: 125920, 2023 Sep 01.
Article in English | MEDLINE | ID: mdl-37481181

ABSTRACT

This study aimed to investigate the effect of heat-moisture treatment (HMT) on the in vitro digestibility of recombinant wheat flours characterizing by gluten proteins differ in glutenin-gliadin ratio. Compared with the untreated flours in our previous study, HMT improved the digestion resistance of starch in flours with different glutenin-gliadin ratios. For the HMT strong-gluten flour, the proportional increase of glutenin led to an excessively strong and fragile gluten network that unstable under HMT, which weakened the wrapping of gluten network around starch granules and reduced the long- and short-range order of starch, resulting in the conversion of resistant starch (RS) and slowly digestible starch (SDS) to rapidly digestible starch (RDS); however, the quantitative increase of gliadin induced the conversion of SDS to RS due to the enhanced protein-starch interactions as well as the improved long- and short-range order of starch during HMT. For the HMT weak-gluten flour, the changes of glutenin-gliadin ratio aggravated the broken of protein network and starch granules during HMT, thus improving the starch digestibility in varying degrees. In conclusion, the relative crystallinity of starch mainly affected the content of resistant starch, while the content of slowly digestible starch was more influenced by protein-starch interactions.


Subject(s)
Flour , Gliadin , Starch , Resistant Starch , Hot Temperature , Triticum , Glutens
19.
Int J Mol Sci ; 24(13)2023 Jul 04.
Article in English | MEDLINE | ID: mdl-37446250

ABSTRACT

The quality of wheat primarily depends on its storage protein quality, especially in regards to gluten content and high-molecular-weight glutenin subunits (HMW-GS). The number of HMW-GS alleles is limited in bread wheat (Triticum aestivum L.), whereas it is abundant in wheat relatives. Therefore, HMW-GS alleles from wheat relatives could provide a potential for improving quality in wheat breeding. Thinopyrum elongatum (EE) is one of the relatives of wheat. The E genome is closely related to the ABD genome in wheat; therefore, Th. elongatum is often used as an excellent exogenous gene donor for wheat genetic improvement. In this study, the high-molecular glutenin subunit gene was cloned and sequenced from Th. elongatum. A specific molecular marker for identifying the Glu-1Ey subunit gene was developed and applied to detected wheat-Th. elongatum alien introgression lines. Quality analysis indicated that the substitution and addition lines containing Th. elongatum alleles significantly (p < 0.05) increased grain protein content by 3.76% to 5.11%, wet-gluten content by 6.55% to 8.73%, flour 8-MW by 0.25% to 6.35%, and bread volume value by 33.77 mL to 246.50 mL, in comparing it with Chinese Spring. The GMP content and lactic acid SRC showed significant positive correlations with flour processing quality and might be used as indicators for wheat quality. The results were expected to provide a novel route for improving processing quality in wheat quality breeding.


Subject(s)
Plant Breeding , Triticum , Triticum/genetics , Triticum/metabolism , Poaceae/genetics , Glutens/genetics , Glutens/metabolism , Molecular Weight , Protein Subunits/metabolism
20.
Foods ; 12(9)2023 Apr 26.
Article in English | MEDLINE | ID: mdl-37174327

ABSTRACT

In Peru, wheat (Triticum aestivum L.) is one of the main resources in the food industry; however, due to its low harvested area, it is the second most imported cereal. The quality of wheat flour was studied to verify that it has desirable characteristics for the preparation of bakery products. The quality of commercial and monovarietal wheat flours was assessed by measuring their physicochemical and rheological parameters, as well as the gluten content and wheat protein fractions. Eight commercial wheat flours and four monovarietal wheat flours (Barba negra, Candeal, Espelta, and Duro) from Peru were evaluated. Commercial wheat flours presented significantly higher levels of protein and gluten index compared to monovarietal wheat flours (p < 0.05). Between both groups, no significant differences were observed in the content of wet and dry gluten. Interestingly, monovarietal wheat flours presented a higher percentage of gliadins and albumins/globulins, as well as lower levels of glutenin, compared to commercial wheat flours (p < 0.05). According to the logistic regression models, the baking strength (W) was the most important parameter to evaluate the quality of commercial and monovarietal wheat flours. Our results show that monovarietal wheat flours show a lower quality compared to commercial wheat flours.

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