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Cited by 10 publications
(10 citation statements)
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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%
See 1 more Smart Citation
“…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%
“…Every subunit of HMW‐GS imparts its individual or synergistic effect on wheat flour processing quality. The identification of the natural null mutants and generation of chemically or radiation‐induced null mutants at the Glu‐1 loci has made it possible to produce mutant lines and further understand their functional role in bread making (Lafiandra & Shewry, 2022). For instance, Glu‐A1 mutation “ null ” does not affect homeologous subunits while Glu‐D1 mutation “ null ” allele results in increased amounts of the homeologous subunits (Kolster et al, 1993).…”
Section: The Glutenin Protein Network In the Bakingmentioning
confidence: 99%
“…However, the currently available markers show a discrepancy in the results and this is due to high variation present among the different alleles at the Glu-3 locus. Moreover, the occurrence of a greater number of retroelements at the Glu-D3 compared to the Glu-A3 and Glu-B3 locus makes it even more difficult to identify and discriminate between the Glu-D3 alleles (Lafiandra & Shewry, 2022). Therefore, researchers focused on the development of a robust, economic, and less time-consuming methodology for the identification of alleles in wheat cultivars.…”
Section: Lmw-gs Molecular Markersmentioning
confidence: 99%
“…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%