2022
DOI: 10.1016/j.foodhyd.2022.107716
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Influence of reconstituted gluten fractions on the short-term and long-term retrogradation of wheat starch

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Cited by 30 publications
(30 citation statements)
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“…Still, the theory of amylose-protein V-complex formation remains largely speculative. Both modified glutenin and gliadin were shown to impact starch retrogradation based on the work by Chen et al (2019), but the significantly higher hydrophobicity of gliadins as compared to glutenins (Kuang et al, 2022;Uthayakumaran et al, 2001) suggests gliadins most likely play a larger role in hydrophobic interactions with starch (Figure 2). This is further supported by work from Girard et al (2019), whereby gliadin addition to wheat starch was shown to reduce pasting time compared to glutenin addition or starch alone.…”
Section: Hydrophobic Interactionsmentioning
confidence: 99%
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“…Still, the theory of amylose-protein V-complex formation remains largely speculative. Both modified glutenin and gliadin were shown to impact starch retrogradation based on the work by Chen et al (2019), but the significantly higher hydrophobicity of gliadins as compared to glutenins (Kuang et al, 2022;Uthayakumaran et al, 2001) suggests gliadins most likely play a larger role in hydrophobic interactions with starch (Figure 2). This is further supported by work from Girard et al (2019), whereby gliadin addition to wheat starch was shown to reduce pasting time compared to glutenin addition or starch alone.…”
Section: Hydrophobic Interactionsmentioning
confidence: 99%
“…Thermal treatment is known to unfold proteins, thus exposing hydrophobic residues (glycine, alanine, valine, leucine, proline, phenylalanine, methionine, and tryptophan) (Li, Yuan, et al, 2020), which may repel water from the starch granule, restricting swelling and molecular mobility (Section 6.1). Kuang et al (2022) suggested that hydrophobic glutenin polypeptides were able to restrict amylopectin retrogradation through this mechanism. Differential scanning calorimetry data suggested that glutenin was partially denatured in the wheat starch gelatinization range, and because glutenins have been shown to participate in hydrophobic interactions (Girard et al, 2018), it is plausible that the increase in hydrophobicity was the cause of decreased amylopectin retrogradation observed via X-ray diffraction analysis (Kuang et al, 2022).…”
Section: Hydrophobic Interactionsmentioning
confidence: 99%
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