Investigation of the Differences in Amyloid-Like Fibrils Derived from Wheat Gluten with Varying Structures under Typical Food Processing Conditions.
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| Title: | Investigation of the Differences in Amyloid-Like Fibrils Derived from Wheat Gluten with Varying Structures under Typical Food Processing Conditions. |
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| Authors: | Liang Y; College of Biological Engineering, Henan University of Technology, Zhengzhou 450001, China., Zhu X; College of Biological Engineering, Henan University of Technology, Zhengzhou 450001, China., Liu H; College of Biological Engineering, Henan University of Technology, Zhengzhou 450001, China., Yang L; College of Biological Engineering, Henan University of Technology, Zhengzhou 450001, China., Liu M; College of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China., Yue Y; College of Biological Engineering, Henan University of Technology, Zhengzhou 450001, China., He B; College of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China., Wang J; College of Biological Engineering, Henan University of Technology, Zhengzhou 450001, China. |
| Source: | Journal of agricultural and food chemistry [J Agric Food Chem] 2025 Apr 16; Vol. 73 (15), pp. 9271-9285. Date of Electronic Publication: 2025 Apr 03. |
| Publication Type: | Journal Article |
| Language: | English |
| Journal Info: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 0374755 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5118 (Electronic) Linking ISSN: 00218561 NLM ISO Abbreviation: J Agric Food Chem Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: Washington, American Chemical Society. |
| MeSH Terms: | Glutens*/chemistry , Triticum*/chemistry , Amyloid*/chemistry, Hot Temperature ; Protein Structure, Secondary ; X-Ray Diffraction ; Cooking |
| Abstract: | This study investigates the differences in physicochemical properties, structural characteristics, and fibril morphology among three wheat gluten with distinct secondary structure contents (A protein: high α-helices, low β-sheets, low random coils; C protein: low α-helices, high β-sheets, high random coils; B protein: intermediate structure) when amyloid-like fibrils (AFs) are formed under boiling and steaming conditions. Congo red absorption, polarized light microscopy, and X-ray diffraction confirmed the formation of AFs in proteins A, B, and C under boiling and steaming conditions. Thioflavin T fluorescence revealed that C-protein-derived fibrils (CPF) exhibited the highest intensity, indicating the strongest fibril-forming ability. SE-HPLC analysis showed a gradual increase in molecular weight and AFs contents with prolonged heating. Increased heating time led to larger particle sizes, higher β-sheet content, and involvement of aromatic amino acids in β-sheet formation via π-π stacking, promoting fibril growth. These changes were more pronounced under steaming conditions. AFM revealed that under steaming, the C protein formed longer and taller fibril structures than under boiling. This work establishes a theoretical foundation for understanding the growth mechanism of AFs formed by gluten proteins with different structures during food processing. |
| Contributed Indexing: | Keywords: amyloid-like fibrils; boiling; steaming; structure; wheat gluten |
| Substance Nomenclature: | 8002-80-0 (Glutens) 0 (Amyloid) |
| Entry Date(s): | Date Created: 20250403 Date Completed: 20250416 Latest Revision: 20250416 |
| Update Code: | 20250416 |
| DOI: | 10.1021/acs.jafc.4c12444 |
| PMID: | 40180613 |
| Database: | MEDLINE |
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