Insight into Organization of Gliadin and Glutenin Extracted from Gluten Modified by Phenolic Acids
The changes in the secondary structure of individual gluten protein fractions (gliadin and glutenin) caused by the supplementation of model dough with eight phenolic acids were analysed. Gliadins and glutenins were extracted from gluten samples obtained from overmixed dough. The changes in the gliad...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-11-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/28/23/7790 |
| _version_ | 1797399863569154048 |
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| author | Renata Welc-Stanowska Konrad Kłosok Agnieszka Nawrocka |
| author_facet | Renata Welc-Stanowska Konrad Kłosok Agnieszka Nawrocka |
| author_sort | Renata Welc-Stanowska |
| collection | DOAJ |
| description | The changes in the secondary structure of individual gluten protein fractions (gliadin and glutenin) caused by the supplementation of model dough with eight phenolic acids were analysed. Gliadins and glutenins were extracted from gluten samples obtained from overmixed dough. The changes in the gliadin secondary structure depended on the amount of phenolic acid added to the dough. Higher acid concentrations (0.1% and 0.2%) led to a significant reduction in the amount of α-helices and to the formation of aggregates, non-ordered secondary structures, and antiparallel β-sheets. After the addition of acids at a lower concentration (0.05%), the disaggregation of pseudo-β-sheet structures and the formation of β-turns, hydrogen-bonded β-turns, and antiparallel β-sheets were detected. In the case of glutenin, most of the phenolic acids induced the formation of intermolecular hydrogen bonds between the polypeptide chains, leading to glutenin aggregation. When phenolic acids were added at a concentration of 0.05%, the process of protein folding and regular secondary structure formation was also observed. In this system, antiparallel β-sheets and β-turns were created at the expense of pseudo-β-sheets. |
| first_indexed | 2024-03-09T01:46:17Z |
| format | Article |
| id | doaj.art-b5d69262c8ed4515b9d2492470bb666c |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-09T01:46:17Z |
| publishDate | 2023-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-b5d69262c8ed4515b9d2492470bb666c2023-12-08T15:22:21ZengMDPI AGMolecules1420-30492023-11-012823779010.3390/molecules28237790Insight into Organization of Gliadin and Glutenin Extracted from Gluten Modified by Phenolic AcidsRenata Welc-Stanowska0Konrad Kłosok1Agnieszka Nawrocka2Institute of Agrophysics, Polish Academy of Sciences, Doświadczalna 4, 20-290 Lublin, PolandInstitute of Agrophysics, Polish Academy of Sciences, Doświadczalna 4, 20-290 Lublin, PolandInstitute of Agrophysics, Polish Academy of Sciences, Doświadczalna 4, 20-290 Lublin, PolandThe changes in the secondary structure of individual gluten protein fractions (gliadin and glutenin) caused by the supplementation of model dough with eight phenolic acids were analysed. Gliadins and glutenins were extracted from gluten samples obtained from overmixed dough. The changes in the gliadin secondary structure depended on the amount of phenolic acid added to the dough. Higher acid concentrations (0.1% and 0.2%) led to a significant reduction in the amount of α-helices and to the formation of aggregates, non-ordered secondary structures, and antiparallel β-sheets. After the addition of acids at a lower concentration (0.05%), the disaggregation of pseudo-β-sheet structures and the formation of β-turns, hydrogen-bonded β-turns, and antiparallel β-sheets were detected. In the case of glutenin, most of the phenolic acids induced the formation of intermolecular hydrogen bonds between the polypeptide chains, leading to glutenin aggregation. When phenolic acids were added at a concentration of 0.05%, the process of protein folding and regular secondary structure formation was also observed. In this system, antiparallel β-sheets and β-turns were created at the expense of pseudo-β-sheets.https://www.mdpi.com/1420-3049/28/23/7790Fourier transform infrared spectroscopygliadingluteninsecondary structurephenolic acids |
| spellingShingle | Renata Welc-Stanowska Konrad Kłosok Agnieszka Nawrocka Insight into Organization of Gliadin and Glutenin Extracted from Gluten Modified by Phenolic Acids Molecules Fourier transform infrared spectroscopy gliadin glutenin secondary structure phenolic acids |
| title | Insight into Organization of Gliadin and Glutenin Extracted from Gluten Modified by Phenolic Acids |
| title_full | Insight into Organization of Gliadin and Glutenin Extracted from Gluten Modified by Phenolic Acids |
| title_fullStr | Insight into Organization of Gliadin and Glutenin Extracted from Gluten Modified by Phenolic Acids |
| title_full_unstemmed | Insight into Organization of Gliadin and Glutenin Extracted from Gluten Modified by Phenolic Acids |
| title_short | Insight into Organization of Gliadin and Glutenin Extracted from Gluten Modified by Phenolic Acids |
| title_sort | insight into organization of gliadin and glutenin extracted from gluten modified by phenolic acids |
| topic | Fourier transform infrared spectroscopy gliadin glutenin secondary structure phenolic acids |
| url | https://www.mdpi.com/1420-3049/28/23/7790 |
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