Formation, structural characteristics and specific peptide identification of gluten amyloid fibrils
Copyright © 2024 Elsevier Ltd. All rights reserved..
This research investigates the formation of amyloid fibrils using enzymatically hydrolyzed peptides from gluten, including its components glutenin and gliadin. After completing the fibrillation incubation, the gluten group demonstrated the most significant average particle size (908.67 nm) and conversion ratio (57.64 %), with a 19.21 % increase in thioflavin T fluorescence intensity due to self-assembly. The results indicated increased levels of β-sheet structures after fibrillation. The gliadin group exhibited the highest zeta potential (∼13 mV) and surface hydrophobicity (H0 = 809.70). Around 71.15 % of predicted amyloidogenic regions within gliadin peptides showed heightened hydrophobicity. These findings emphasize the collaborative influence of both glutenin and gliadin in the formation of gluten fibrils, influenced by hydrogen bonding, hydrophobic, and electrostatic interactions. They also highlight the crucial role played by gliadin with amyloidogenic fragments such as ILQQIL and SLVLQTL, aiming to provide a theoretical basis for understanding the utilization of gluten proteins.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:445 |
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| Enthalten in: |
Food chemistry - 445(2024) vom: 01. Apr., Seite 138648 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Feng, Yulin [VerfasserIn] |
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| Links: |
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| Themen: |
8002-80-0 |
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| Anmerkungen: |
Date Completed 01.04.2024 Date Revised 01.04.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.foodchem.2024.138648 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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NLM368447383 |
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| 520 | |a Copyright © 2024 Elsevier Ltd. All rights reserved. | ||
| 520 | |a This research investigates the formation of amyloid fibrils using enzymatically hydrolyzed peptides from gluten, including its components glutenin and gliadin. After completing the fibrillation incubation, the gluten group demonstrated the most significant average particle size (908.67 nm) and conversion ratio (57.64 %), with a 19.21 % increase in thioflavin T fluorescence intensity due to self-assembly. The results indicated increased levels of β-sheet structures after fibrillation. The gliadin group exhibited the highest zeta potential (∼13 mV) and surface hydrophobicity (H0 = 809.70). Around 71.15 % of predicted amyloidogenic regions within gliadin peptides showed heightened hydrophobicity. These findings emphasize the collaborative influence of both glutenin and gliadin in the formation of gluten fibrils, influenced by hydrogen bonding, hydrophobic, and electrostatic interactions. They also highlight the crucial role played by gliadin with amyloidogenic fragments such as ILQQIL and SLVLQTL, aiming to provide a theoretical basis for understanding the utilization of gluten proteins | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Amyloid fibril | |
| 650 | 4 | |a Cross-β structure | |
| 650 | 4 | |a Gluten | |
| 650 | 4 | |a Peptide | |
| 650 | 4 | |a Self-assembly | |
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| 650 | 7 | |a Gliadin |2 NLM | |
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| 700 | 1 | |a Li, Ren |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Huijuan |e verfasserin |4 aut | |
| 700 | 1 | |a Ren, Feiyue |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Jie |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Jing |e verfasserin |4 aut | |
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