The Thermal Properties of Gliadins and Glutenins Fortified with Flavonoids and Their Glycosides Studied via Thermogravimetry (TGA) and Differential Scanning Calorimetry (DSC)
Source abstract
Abstract
Thermal analyses (TGA and DSC) were used to determine the thermal properties of gliadins and glutenins extracted from a model wheat dough fortified with flavonoids and their glycosides. As flavonoids, quercetin; naringenin; hesperetin; and their glycosides, rutin, naringin, and hesperidin, were used in amounts of 0.05%, 0.1% and 0.2%. An analysis of TGA parameters showed that samples fortified with flavonoids/glycosides led to an increase in the weight loss of gliadin. The thermal behavior of gliadins enriched in polyphenols depended on the structure and size of the added compound. The weight loss of glutenin did not change in the presence of the studied polyphenols. An analysis of the difference TGA thermograms showed that quercetin, rutin, and naringin interacted with gliadins through the OH group located at the B ring in the 4’ position. Additionally, quercetin formed chemical bonds with the polypeptide chains of glutenins. The DSC thermograms were consistent with the TGA results, which suggest interactions between gliadin and quercetin.
Source: crossref · Quality: baseline
Research context
OpenAlex topics: Food composition and properties · Food Quality and Safety Studies · Phytochemicals and Antioxidant Activities
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Institute of Agrophysics Polish Academy of Sciences, Doświadczalna 4, 20-290 Lublin, Poland
Institute of Earth and Environmental Sciences, Faculty of Earth Sciences and Spatial Management, Maria Curie-Sklodowska University, al. Kraśnicka 2cd, 20-718 Lublin, Poland
Faculty of Chemistry, University of Białystok, Ciołkowskiego 1K, 15-245 Białystok, Poland
Funding
NATIONAL SCIENCE CENTER, POLAND
References (35)
Show source-provided references
1. Gliadins from wheat grain: An overview, from primary structure to nanostructures of aggregates10.1007/s12551-017-0367-2 ↗
2. Flavonoids: An overview10.1017/jns.2016.41 ↗
3. Bread enriched with quinoa leaves—The influence of protein–phenolics interactions on the nutritional and antioxidant quality10.1016/j.foodchem.2014.04.044 ↗
4. Antioxidant activity of hard wheat flour, dough and bread prepared using various processes with the addition of different phenolic acids10.1002/jsfa.4188 ↗
5. Effects of gliadin addition on the rheological, microscopic and thermal characteristics of wheat gluten10.1016/j.ijbiomac.2012.11.002 ↗
6. Comparative studies on physicochemical properties of gluten- and glutenin-based films functionalized by polyphenols10.1002/cche.10525 ↗
7. The thermal stability, structural changeability, and aggregability of the glutenin and gliadin proteins induced by wheat bran dietary fiber10.1039/C8FO01810C ↗
8. Aggregation of gluten proteins in model dough after fibre polysaccharide addition10.1016/j.foodchem.2017.03.117 ↗
9. Effect of oil pomaces on thermal properties of model dough and gluten network studied by thermogravimetry and differential scanning calorimetry10.1016/j.foodchem.2021.129882 ↗
10. Raman and thermal (TGA and DSC) studies of gluten proteins supplemented with flavonoids and their glycosides10.1016/j.jcs.2023.103672 ↗
11. Interactions of gliadins with flavonoids and their glycosides studied with application of FT-Raman spectroscopy10.1016/j.jcs.2024.103915 ↗
12. Effect of cinnamic acid and its derivatives on structure of gluten proteins—A study on model dough with application of FT-Raman spectroscopy10.1016/j.foodhyd.2020.105935 ↗
13. Raman characterization of the interactions between gliadins and anthocyanins10.1002/jrs.4288 ↗
14. A differential scanning calorimetry study of wheat proteins10.1007/s00217-003-0699-y ↗
15. Sharif, N., Golmakani, M.-T., Niakousari, M., Hosseini, S., Ghorani, B., and Lopez-Rubio, A. (2018). Active Food Packaging Coatings Based on Hybrid Electrospun Gliadin Nanofibers Containing Ferulic Acid/Hydroxypropyl-Beta-Cyclodextrin Inclusion Complexes. Nanomaterials, 8.10.3390/nano8110919 ↗
16. Comparison of the conformational and nutritional changes of deamidated wheat gliadin by citric acid and hydrochloric acid10.1016/j.jcs.2014.02.003 ↗
17. Kłosok, K., Welc, R., Fornal, E., and Nawrocka, A. (2021). Effect of physical and chemical factors on the structure of gluten, gliadins and glutenins as studied with spectroscopic methods. Molecules, 26.10.3390/molecules26020508 ↗
18. Effect of frozen storage on the conformational, thermal and microscopic properties of gluten: Comparative studies on gluten-, glutenin- and gliadin-rich fractions10.1016/j.foodhyd.2013.05.015 ↗
19. Dietary fibre-induced changes in the structure and thermal properties of gluten proteins studied by Fourier transform—Raman spectroscopy and thermogravimetry10.1021/acs.jafc.5b05712 ↗
20. Effect of dietary fibre polysaccharides on structure and thermal properties of gluten proteins—A study on gluten dough with application of FT-Raman spectroscopy, TGA and DSC10.1016/j.foodhyd.2017.03.012 ↗
21. Welc, R., Luchowski, R., Kłosok, K., Gruszecki, W.I., and Nawrocka, A. (2022). How do phenolic acids change the secondary and tertiary structure of gliadin? Studies with an application of spectroscopic techniques. Int. J. Mol. Sci., 23.10.3390/ijms23116053 ↗
22. Teng, J., Liu, X., Hu, X., Zhao, Y., Tao, N.-P., and Wang, M. (2018). Dihydromyricetin as a Functional Additive to Enhance Antioxidant Capacity and Inhibit the Formation of Thermally Induced Food Toxicants in a Cookie Model. Molecules, 23.10.3390/molecules23092184 ↗
23. Interaction of high amylose corn starch with polyphenols: Modulating the stability of polyphenols with different structure against thermal processing10.1016/j.foodchem.2023.137708 ↗
24. Thermal stability and bioavailability of bioactive compounds after baking of bread enriched with different onion by-products10.1016/j.foodchem.2020.126562 ↗
25. Characterisation of different inulin samples by DSC: Influence of polymerisation degree on melting temperature10.1023/A:1022238905962 ↗
26. Tsioptsias, C., and Tsivintzelis, I. (2022). On the thermodynamic thermal properties of quercetin and similar pharmaceuticals. Molecules, 27.10.3390/molecules27196630 ↗
27. Chemistry of wheat gluten proteins: Qualitative composition10.1002/cche.10572 ↗
28. Wheat gluten protein and its impacts on wheat processing quality10.15302/J-FASE-2019267 ↗
29. Structure and allergenicity of wheat gluten proteins—A review
30. Effect of hydrostatic pressure and temperature on the chemical and functional properties of wheat gluten: Studies on gluten, gliadin and glutenin10.1016/j.jcs.2006.09.008 ↗
31. The location of disulphide bonds in monomeric γ-type gliadins10.1006/S0733-5210(97)90100-4 ↗
32. Mechanism of gliadin–glutenin cross-linking during hydrothermal treatment10.1016/j.foodchem.2007.08.082 ↗
33. Effects of thermal properties and behavior of wheat starch and gluten on their interaction: A review10.1016/j.ijbiomac.2021.02.175 ↗
34. Effects of edible plant polyphenols on gluten protein functionality and potential applications of polyphenol–gluten interactions10.1111/1541-4337.12572 ↗
35. Effect of gliadin/glutenin ratio on pasting, thermal, and structural properties of wheat starch10.1016/j.jcs.2020.102973 ↗