Wheat Glutenin polymers 2. The role of wheat glutenin subunits in polymer formation and dough quality

Lafiandra, Domenico; Shewry, Peter R.

doi:10.1016/j.jcs.2022.103487

Cited by 9 publications

References 82 publications

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“…The glutenin and gliadin proteins have diverse functions during dough production due to differences in their structural compositions ( Figure 1 ). Glutenins form polymers stabilized by inter-chain disulfide bonds, whereas gliadins are monomers and interact with glutenin polymers through non-covalent forces, especially hydrogen bonds [ 9 ]. It is commonly believed that glutenin proteins create the polymeric protein network that gives dough its cohesiveness and elasticity, whereas gliadins as plasticizers of the glutenin network and provide dough with viscosity and extensibility [ 9 , 10 ].…”

Section: Structure and Function Of Wheat Proteinmentioning

confidence: 99%

“…Glutenins form polymers stabilized by inter-chain disulfide bonds, whereas gliadins are monomers and interact with glutenin polymers through non-covalent forces, especially hydrogen bonds [ 9 ]. It is commonly believed that glutenin proteins create the polymeric protein network that gives dough its cohesiveness and elasticity, whereas gliadins as plasticizers of the glutenin network and provide dough with viscosity and extensibility [ 9 , 10 ]. Although there are several reviews on high-molecular-weight glutenin, a comprehensive review on the structure and function of gluten protein is lacking.…”

Section: Structure and Function Of Wheat Proteinmentioning

confidence: 99%

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Recent Advances in the Study of Wheat Protein and Other Food Components Affecting the Gluten Network and the Properties of Noodles

Zang

Gao²,

Chen³

et al. 2022

Foods

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Upon hydrating and mixing wheat flour, wheat protein forms a network that strongly affects the structure and physicochemical properties of dough, thus affecting the properties of noodles. Different approaches have been taken to alter the gluten network structure in order to control the dough properties. In the current review, we summarize the structure and function of wheat protein, including glutenin and gliadin, and describe food components that may affect noodle quality by interacting with wheat protein. In fact, the ratio of glutenin to gliadin is closely related to the viscosity of dough, and disulfide bonds also contribute to the gluten network formation. Meanwhile, wheat protein coexists with starch and sugar in wheat dough, and thus the nature of starch may highly influence gluten formation as well. Salts, alkali, enzymes and powdered plant food can be added during dough processing to regulate the extensional properties of wheat noodles, obtaining noodles of high quality, with improved sensory and storage properties. This review describes specific methods to reinforce the wheat protein network and provides a reference for improving noodle quality.

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Section: Structure and Function Of Wheat Proteinmentioning

confidence: 99%

Section: Structure and Function Of Wheat Proteinmentioning

confidence: 99%

Recent Advances in the Study of Wheat Protein and Other Food Components Affecting the Gluten Network and the Properties of Noodles

Zang

Gao²,

Chen³

et al. 2022

Foods

View full text Add to dashboard Buy / Rent full text

show abstract

“…Readers are referred to two recent review articles for more detailed accounts of the structure and properties of wheat glutenin polymers (Shewry & Lafiandra, 2022; Lafiandra & Shewry, 2022). However, the aim here is to highlight some of the outstanding gaps in our knowledge.…”

Section: Gluten Proteins and Processing Qualitymentioning

confidence: 99%

“…Two of the HMW‐GS associated with good quality (1Dx5, 1Bx7) have higher numbers of cysteine residues compared with the allelic poor‐quality subunits (1Dx2 and 1Bx20, respectively) which may result in more highly cross‐linked, and hence more elastic, polymers. In other cases, the good quality associated with individual subunits may result from quantitative effects of gene expression levels on total HMW subunit amount, for example, the higher quality resulting from the presence of a 1Ax subunit (1Ax1 or 1Ax2*) compared with the null allele, or the overexpression of subunit 1Bx7 OE (which results from a gene duplication) compared with the normal allele (reviewed by Lafiandra & Shewry, 2022). However, these mechanisms do not provide explanations for all reported associations of HMW subunits with grain quality and it is probable that more subtle differences in the amino acid sequences of HMW‐GS also contribute, for example, by affecting the formation of noncovalent hydrogen bonds (and hence “train” regions in hydrated gluten as discussed above).…”

Section: Gluten Proteins and Processing Qualitymentioning

confidence: 99%

Wheat grain proteins: Past, present, and future

Shewry

2022

Cereal Chem

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“…The repeat region is rich in β-turns flanked by spherical conservative regions formed by α-helices [ 16 ]. Most of the cysteine residues form intra-chain disulfide bonds, some of them form inter-chain disulfide bonds and directly affect dough formation and rheological characteristics [ 17 , 18 , 19 ]. Generally, the β-turn structure confers protein molecules with significant deformation resistance [ 20 ].…”

Section: Introductionmentioning

confidence: 99%

Molecular Characterization and SNP-Based Molecular Marker Development of Two Novel High Molecular Weight Glutenin Genes from Triticum spelta L.

Cao

Zhang²,

Wang³

et al. 2022

IJMS

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Spelt wheat (Triticum spelta L., 2n=6x=42, AABBDD) is a valuable source of new gene resources for wheat genetic improvement. In the present study, two novel high molecular weight glutenin subunits (HMW-GS) 1Ax2.1* at Glu-A1 and 1By19* at Glu-B1 from German spelt wheat were identified. The encoding genes of both subunits were amplified and cloned by allele-specific PCR (AS-PCR), and the complete sequences of open reading frames (ORF) were obtained. 1Ax2.1* with 2478 bp and 1By19* with 2163 bp encoded 824 and 720 amino acid residues, respectively. Molecular characterization showed that both subunits had a longer repetitive region, and high percentage of α-helices at the N- and C-termini, which are beneficial for forming superior gluten macropolymers. Protein modelling by AlphaFold2 revealed similar three-diamensional (3D) structure features of 1Ax2.1* with two x-type superior quality subunits (1Ax1 and 1Ax2*) and 1By19* with four y-type superior quality subunits (1By16, 1By9, 1By8 and 1By18). Four cysteine residues in the three x-type subunits (1Ax2.1*, 1Ax1 and 1Ax2*) and the cysteine in intermediate repeat region of y-type subunits were not expected to participate in intramolecular disulfide bond formation, but these cysteines might form intermolecular disulfide bonds with other glutenins and gliadins to enhance gluten macropolymer formation. The SNP-based molecular markers for 1Ax2.1* and 1By19* genes were developed, which were verified in different F2 populations and recombination inbred lines (RILs) derived from crossing between spelt wheat and bread wheat cultivars. This study provides data on new glutenin genes and molecular markers for wheat quality improvement.

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Wheat Glutenin polymers 2. The role of wheat glutenin subunits in polymer formation and dough quality

Cited by 9 publications

References 82 publications

Recent Advances in the Study of Wheat Protein and Other Food Components Affecting the Gluten Network and the Properties of Noodles

Recent Advances in the Study of Wheat Protein and Other Food Components Affecting the Gluten Network and the Properties of Noodles

Wheat grain proteins: Past, present, and future

Molecular Characterization and SNP-Based Molecular Marker Development of Two Novel High Molecular Weight Glutenin Genes from Triticum spelta L.

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