Effects of phenolic acid molecular structure on the structural properties of gliadins and glutenins
More details
Hide details
Institute of Agrophysics, Polish Academy of Sciences, Doświadczalna 4, 20-290 Lublin, Poland
Final revision date: 2024-01-31
Acceptance date: 2024-02-12
Publication date: 2024-02-27
Corresponding author
Agnieszka Nawrocka   

Department of Physical Properties of Plant Materials, Laboratory of Assessment of Grain and Oil Materials Quality, Institute of Agrophysics, Polish Academy of Sciences, Doświadczalna 4, 20-290 Lublin, Poland
Int. Agrophys. 2024, 38(2): 127-137
  • Phenolic acids interacted with gliadins as well as glutenins
  • Structural changes in modified gliadins are more complex than in glutenins
  • The changes observed in gliadins as well as glutenins mainly affected β-structures
  • Phenolic acids affect hydrogen bond formation in both gliadins and glutenins
The aim of this research is to determine how phenolic acids affect the individual structure of gluten proteins: gliadins and glutenins, by understanding the underlying molecular interactions. Fourier transform infrared spectroscopy was used to determine changes in the secondary structure of the individual gluten network proteins: gliadins and glutenins, after addition of selected phenolic acids to the model dough. Phenolic acids were added to the model dough at the following concentrations: 0.05, 0.1 and 0.2% (w/w). The phenolic acids induce changes in the secondary structure of the gliadins and glutenins. The degree of interaction depends on the structure and concentration of the added phenolic acid. In most cases, these interactions lead to the formation of disordered structures in both gliadins and glutenins. From the results obtained, it can be concluded that the inclusion of certain phenolic acids in the dough affects the hydrogen bonding in gliadins and glutenin, and that phenolic acids interact non-covalently with these gluten proteins. The findings could potentially be applied to food chemistry and may have an impact on the allergenic properties of gluten, particularly in relation to the reduction of the β-turn content within glutenins.
This work was supported by the National Science Centre, Poland (grant number: 2019/35/B/NZ9/02854).
The authors declare no conflict of interest.
Barth A., 2007. Infrared spectroscopy of proteins. Biochim. Biophys. Acta BBA – Bioenerg., 1767(9), 1073-1101.
Cerf E., Sarroukh R., Tamamizu-Kato S., Breydo L., Derclaye S., Dufrêne Y.F., Narayanaswami V., Goormaghtigh E., Ruysschaert J.-M., and Raussens V., 2009. Antiparallel β-sheet: a signature structure of the oligomeric amyloid β-peptide. Biochem. J., 421(3), 415-423.
Chompoorat P., Fasasi A., Lavine B.K., and Rayas-Duarte P., 2022. Gluten conformation at different temperatures and additive treatments. Foods, 11(3), 430.
Czubinski J. and Dwiecki K., 2017. A review of methods used for investigation of protein-phenolic compound interactions. Int. J. Food Sci. Technol., 52(3), 573-585.
De Meutter J. and Goormaghtigh E., 2021. Evaluation of protein secondary structure from FTIR spectra improved after partial deuteration. Eur. Biophys. J., 50(3-4), 613-628.
Dhaka V. and Khatkar B.S., 2016. Microstructural, thermal and IR spectroscopy characterisation of wheat gluten and its sub fractions. J. Food Sci. Technol., 53(8), 3356-3363.
Feng Y., Feng X., Liu S., Zhang H., and Wang J., 2022. Interaction mechanism between cereal phenolic acids and gluten protein: protein structural changes and binding mode. J. Sci. Food Agric., 102(15), 7387-7396.
Fevzioglu M., Ozturk O.K., Hamaker B.R., and Campanella O.H., 2020. Quantitative approach to study secondary structure of proteins by FT-IR spectroscopy, using a model wheat gluten system. Int. J. Biol. Macromol., 164, 2753-2760.
Girard A.L., Bean S.R., Tilley M., Adrianos S.L., and Awika J.M., 2018. Interaction mechanisms of condensed tannins (proanthocyanidins) with wheat gluten proteins. Food Chem., 245, 1154-1162.
Gruszecki W.I., Janik E., Luchowski R., Kernen P., Grudzinski W., Gryczynski I., and Gryczynski Z., 2009. Supramolecular organization of the main photosynthetic antenna complex LHCII: A Monomolecular Layer Study. Langmuir, 25(16), 9384-9391.
Han H.M. and Koh B.-K., 2011. Antioxidant activity of hard wheat flour, dough and bread prepared using various processes with the addition of different phenolic acids. J. Sci. Food Agric., 91(4), 604-608.
Huang L., Zhang X., Zhang H., and Wang J., 2018. Interactions between dietary fiber and ferulic acid changed the aggregation of gluten in a whole wheat model system. LWT, 91, 55-62.
Kłosok K., Welc R., Szymańska-Chargot M., and Nawrocka A., 2022. Phenolic acids-induced aggregation of gluten proteins. Structural analysis of the gluten network using FT-Raman spectroscopy. J. Cereal Sci., 107, 103503.
Kłosok K., Welc-Stanowska R., and Nawrocka A., 2023. Changes in the conformation and biochemical properties of gluten network after phenolic acid supplementation. J. Cereal Sci., 110, 103651.
Nawrocka A., Krekora M., Niewiadomski Z., and Miś A., 2018a. Characteristics of the chemical processes induced by celluloses in the model and gluten dough studied with application of FTIR spectroscopy. Food Hydrocoll., 85, 176-184.
Nawrocka A., Krekora M., Niewiadomski Z., and Miś A., 2018b. FTIR studies of gluten matrix dehydration after fibre polysaccharide addition. Food Chem., 252, 198-206.
Nawrocka A., Miś A., and Niewiadomski Z., 2017a. Dehydration of gluten matrix as a result of dietary fibre addition - A study on model flour with application of FT-IR spectroscopy. J. Cereal Sci., 74, 86-94.
Nawrocka A., Szymańska-Chargot M., Miś A., Wilczewska A.Z., and Markiewicz K.H., 2017b. Aggregation of gluten proteins in model dough after fibre polysaccharide addition. Food Chem., 231, 51-60.
Nawrocka A., Szymańska-Chargot M., Miś A., Ptaszyńska A.A., Kowalski R., Waśko P., and Gruszecki W.I., 2015. Influence of dietary fibre on gluten proteins structure – a study on model flour with application of FT-Raman spectroscopy. J. Raman Spectrosc., 46(3), 309-316.
Nawrocka A., Zarzycki P., Kłosok K., Welc R., Wirkijowska A., and Teterycz D., 2023. Effect of dietary fibre waste originating from food production on the gluten structure in common wheat dough. Int. Agrophysics, 37(1), 101-109.
Ozdal T., Capanoglu E., and Altay F., 2013. A review on protein-phenolic interactions and associated changes. Food Res. Int., 51(2), 954-970.
Rani M., Siddiqi R.A., Sharma R., Gill B.S., and Sogi D.S., 2023. Functional and structural properties of gliadin as influenced by pH, extraction protocols, and wheat cultivars. Int. J. Biol. Macromol., 234, 123484.
Ribeiro A.C., Leite D.C., Scheibel J.M., Soares R.M.D., and Silveira N.P., 2021. Structural study of wheat gliadin in different solvents by spectroscopic techniques. J. Braz. Chem. Soc., 32, 695-701.
Secundo F. and Guerrieri N., 2005. ATR-FT/IR study on the interactions between gliadins and dextrin and their effects on protein secondary structure. J. Agric. Food Chem., 53(5), 1757-1764.
Shewry P.R., Popineau Y., Lafiandra D., and Belton P., 2000. Wheat glutenin subunits and dough elasticity: findings of the EUROWHEAT project. Trends Food Sci. Technol., 11(12), 433-441.
Stani C., Vaccari L., Mitri E., and Birarda G., 2020. FTIR investigation of the secondary structure of type I collagen: New insight into the amide III band. Spectrochim. Acta. A. Mol. Biomol. Spectrosc., 229, 118006.
Sun X., Sarteshnizi R.A., and Udenigwe C.C., 2022. Recent advances in protein-polyphenol interactions focusing on structural properties related to antioxidant activities. Curr. Opin. Food Sci., 45, 100840.
Świeca M., Sęczyk Ł., Gawlik-Dziki U., and Dziki D., 2014. Bread enriched with quinoa leaves - The influence of protein-phenolics interactions on the nutritional and antioxidant quality. Food Chem., 162, 54-62.
Taddei P., Zanna N., and Tozzi S., 2013. Raman characterization of the interactions between gliadins and anthocyanins. J. Raman Spectrosc., 44(10), 1435-1439.
Urade R., Sato N., and Sugiyama M., 2017. Gliadins from wheat grain: an overview, from primary structure to nanostructures of aggregates. Biophys. Rev., 10(2), 435-443.
Van Buiten C.B. and Elias R.J., 2021. Gliadin sequestration as a novel therapy for celiac disease: A Prospective Application for Polyphenols. Int. J. Mol. Sci., 22(2), 595.
Wang P., Chen H., Mohanad B., Xu L., Ning Y., Xu J., Wu F., Yang N., Jin Z., and Xu X., 2014. Effect of frozen storage on physico-chemistry of wheat gluten proteins: Studies on gluten-, glutenin- and gliadin-rich fractions. Food Hydrocoll., 39, 187-194.
Wang K., Li C., Wang B., Yang W., Luo S., Zhao Y., Jiang S., Mu D., and Zheng Z., 2017. Formation of macromolecules in wheat gluten/starch mixtures during twin-screw extrusion: effect of different additives. J. Sci. Food Agric., 97(15), 5131-5138.
Wang Q., Li Y., Sun F., Li X., Wang P., Sun J., Zeng J., Wang C., Hu W., Chang J., Chen M., Wang Y., Li K., Yang G., and He G., 2015. Tannins improve dough mixing properties through affecting physicochemical and structural properties of wheat gluten proteins. Food Res. Int., 69, 64-71.
Wellner N., Mills E.N.C., Brownsey G., Wilson R.H., Brown N., Freeman J., Halford N.G., Shewry P.R., and Belton P.S., 2005. Changes in protein secondary structure during gluten deformation studied by dynamic fourier transform infrared spectroscopy. Biomacromolecules, 6(1), 255-261.
Xu J., Wang W., and Li Y., 2019. Dough properties, bread quality, and associated interactions with added phenolic compounds: A review. J. Funct. Foods, 52, 629-639.
Yang H., Yang S., Kong J., Dong A., and Yu S., 2015. Obtaining information about protein secondary structures in aqueous solution using Fourier transform IR spectroscopy. Nat. Protoc., 10(3), 382-396.
Zhang C., Ren Z., Yin Z., Qian H., and Ma D., 2008. Amide II and Amide III Bands in Polyurethane Model Soft and Hard Segments. Polym. Bull., 60(1), 97-101.
Journals System - logo
Scroll to top