2022
DOI: 10.1007/s12161-022-02331-1
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Infrared Spectroscopy and Microstructural Assessment of Dough with Varying Wheat Gluten Fractions

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Cited by 6 publications
(5 citation statements)
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“…The inclusion of glutenins in both the varieties developed a more continuous, strong, compact, and more well‐organized dough matrix conferring the dough strengthening. Similar results were observed by Dewan et al (2022) and Dangi et al (2019) where flour was fortified with glutenins depicting a strong and compact gluten matrix. The results were strengthened by the microdough lab values, where glutenins supplementation to both the varieties depicted greater dough stability and strength.…”
Section: Resultssupporting
confidence: 89%
See 2 more Smart Citations
“…The inclusion of glutenins in both the varieties developed a more continuous, strong, compact, and more well‐organized dough matrix conferring the dough strengthening. Similar results were observed by Dewan et al (2022) and Dangi et al (2019) where flour was fortified with glutenins depicting a strong and compact gluten matrix. The results were strengthened by the microdough lab values, where glutenins supplementation to both the varieties depicted greater dough stability and strength.…”
Section: Resultssupporting
confidence: 89%
“…The enhanced concentration of glutenins created a more uniform, dense, and closely intact dough network. Inclusion of purified gliadin fractions was shown to produce shorter strands, thus resulting in the open gluten structure due to its monomeric nature and property of providing fluidity to the developed dough (Chaudhary et al, 2022; Dewan et al, 2022).…”
Section: Resultsmentioning
confidence: 99%
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“…A major part of dough elasticity comes from the gliadins present in the gluten protein network. As reported by Dewan and coauthors, the fluidic nature of gliadins shortens the gluten network by forming hollow gaps in the strong dough network. Therefore, an open and vulnerable gluten network develops in the dough matrix, leading to the dominance of fluidic behavior.…”
Section: Resultsmentioning
confidence: 73%
“…The modifications in gluten's secondary structure have been largely associated with high-molecular-weight (HMW) glutenin components [32,33]. It was discovered via FTIR spectroscopic analysis that the hydration of HMW glutenin leads to an increase in β-sheet formations [34][35][36]. This implies that the elevated levels of βsheet structures observed within wheat glutenin upon hydration are mainly due to the interactions between HMW glutenin subunits [13].…”
Section: Farinograph Mixingmentioning
confidence: 99%