## 3 Results and Discussion  
### Thermogravimetric Analysis (TGA)  
The thermogravimetric parameters (weight loss (WL) and degradation temperature (T\({}_{\mathrm{d}}\))) of gliadins and glutenins are presented in Table 1. The thermal degradation profiles and their first derivatives for both types of proteins are depicted in Figures S2 and S3 in the Supplementary Material, respectively. The weight loss and degradation temperature for gliadins are 68.7% and 310 \({}^{\circ}\)C, respectively. [PERSON] et al. [15] obtained a degradation temperature for gliadins of about 322 \({}^{\circ}\)C. The difference in degradation temperature can be attributed to the structural form of the studied gliadins, because [PERSON] et al. [15] obtained this parameter for gliadin fibers obtained via electrospinning. Similar results for weight loss for gliadins were obtained by [PERSON] et al. [7]. In contrast, lower weight loss (54.5%) for gliadins was reported by [PERSON] et al. [16], who studied deaminated gliadins. In the case of glutenins, the weight loss and degradation temperature were 70.8% and 301 \({}^{\circ}\)C, respectively. Similar values of both parameters for glutenins were obtained by [PERSON] et al. [7]. A comparison of the TGA parameters for both gluten proteins showed that they did not differ in the weightloss, whereas gliadins had a higher degradation temperature. According to [PERSON] et al. [7], this difference is related to the structure of the studied proteins, especially the type of disulfide bridges formed. Gliadins only formed intrachain disulfide bridges (seven bonds) that required more energy to be cleaved. Glutenins formed two kinds of disulfide bridges, intra- (four bonds) and interchain (six bonds) [17]. Additionally, gluten, as a mixture of gliadins and glutenins, is characterized by similar weight loss but a higher degradation temperature (318 \({}^{\circ}\)C) [10]. The higher degradation temperature indicates a higher amount of different chemical bonds, including disulfide bridges, hydrogen bonds, ionic bonds, etc. The addition of flavonoids/glycos caused changes in the thermal parameters of gliadins (see Table 1). The presence of these compounds led to an increase in the weight loss. The greatest weight loss was observed after 0.05% addition of QUE, RUTG, and NAR. For QUE and NAR, a slight decrease in weight loss was observed with an increase in their concentration. In contrast, the increase in the concentration of RUTG, NARG, HET, and HEDG in the dough sample did not affect the weight loss of gliadin-flavonoid/glycos samples. An increase in gliadin WL as a result of flavonoid/glycos presence may indicate that the polyphenols interact with gliadins during the dough mixing process, preventing the formation of an adequate gliadin structure. The results show that the WL parameters increase depending on the structure and size of the used compound. The biggest increase in WL was observed for QUE, RUTG, and NAR, which are characterized by the smallest spatial size (see Figure S1 in the Supplementary Material). They can form hydrogen bonds between gliadin chains because they have OH groups on both sides of the molecule. In the case of NARG and HEDG, the glycosidic linkage is at position 7. For this reason, the size of both glycosides is greater compared to that of rutin, in which the glycosidic linkage is at position 3. Additionally, HET and HEDG have one methoxyl group at the B ring, which may hinder the formation of hydrogen bonds on both sides of the molecule. As seen in Table 1, the weight loss of glutenin does not change in the presence of the studied polyphenols. This parameter also did not change in the case of gluten network modified by the same compounds [10]. Taking the above-mentioned results into account, it can be concluded that glutenins are responsible for the thermal stability of the gluten network. The first derivatives of TGA thermograms, presented in Figures S2 and S3 in the Supplementary Material for gliadins and glutenins, respectively, show two peaks.