“…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).…”