RESEARCH PAPER
Effects of phenolic acid molecular structure on the structural properties of gliadins and glutenins
1
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
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
HIGHLIGHTS
- 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
KEYWORDS
TOPICS
ABSTRACT
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.
FUNDING
This work was supported by the National Science Centre, Poland (grant number: 2019/35/B/NZ9/02854).
CONFLICT OF INTEREST
The authors declare no conflict of interest.
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