2013
DOI: 10.1016/j.molstruc.2012.08.031
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Changes in secondary structure of gluten proteins due to emulsifiers

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Cited by 81 publications
(37 citation statements)
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“…The control sample contained 43%, 45%, and 12% of disulphide bridges in the g-g-g, t-g-g, and t-g-t conformation, respectively. Similar results were obtained for gluten washed out from model flour, which was reconstituted from two commercial components: wheat gluten and wheat starch (Nawrocka et al, 2015) and for gluten washed out from commercial flour (Gomez, Ferrer, Anon, & Puppo, 2013).…”
Section: Changes In Disulphide Bridges (S-s) Conformationsupporting
confidence: 81%
“…The control sample contained 43%, 45%, and 12% of disulphide bridges in the g-g-g, t-g-g, and t-g-t conformation, respectively. Similar results were obtained for gluten washed out from model flour, which was reconstituted from two commercial components: wheat gluten and wheat starch (Nawrocka et al, 2015) and for gluten washed out from commercial flour (Gomez, Ferrer, Anon, & Puppo, 2013).…”
Section: Changes In Disulphide Bridges (S-s) Conformationsupporting
confidence: 81%
“…Likewise, emulsifiers widely used in bakery product such as sodium stearoyl lactylate (SSL) can induce protein folding including an increase in α-helix conformation and a decrease in β-sheet, turns and random coil (Figure 1). The conformation change may be resulted from the low burial of tryptophan residues to a more hydrophobic environment and the low percentage area of the C-H stretching band for GS0.25 (Gluten + 0.25% SSL) (Gómez et al, 2013).…”
Section: Gluten Proteinmentioning
confidence: 99%
“…dough (Gomez et al, 2004) as deduced from the larger width of the tail of the mixograms after 8 min of mixing produced with the former (Van Steertegem et al, 2013b). In this context, Gomez et al (2004) and Gomez et al (2013) have suggested that binding of the surfactant's lipophilic part to proteins during mixing increases protein aggregation. Taken together, it is more likely that SSL interacts with gluten than with starch.…”
Section: Impact Of Ssl and Mixing Time On Gluten Polymerization Durinmentioning
confidence: 99%
“…They present an interesting tool to change dough's mixing properties and, in the end, the transient gluten network structure. The dough strengthening effect of SSL has been attributed to its interactions with gluten proteins during dough mixing, which may cause gluten aggregation and increase dough strength (Gomez, Ferrer, Anon, & Puppo, 2013;Gomez et al, 2004). In contrast, according to Collar, Armero, and Martinez (1998), during dough mixing, SSL preferentially binds to the inside part of the starch granules and only loosely to gluten.…”
Section: Introductionmentioning
confidence: 99%