Monge-Morera, M, Lambrecht, MA, Deleu, LJ et al. (6 more authors) (2020) Processing Induced Changes in Food Proteins: Amyloid Formation during Boiling of Hen Egg White. Biomacromolecules, 21 (6). pp. 2218-2228. ISSN 1525-7797
Abstract
Amyloid fibrils (AFs) are highly ordered protein nanofibers composed of cross β-structure that occur in nature, but that also accumulate in age-related diseases. Amyloid propensity is a generic property of proteins revealed by conditions that destabilize the native state, suggesting that food processing conditions may promote AF formation. This had only been shown for foie gras, but not in common foodstuffs. We here extracted a dense network of fibrillar proteins from commonly consumed boiled hen egg white (EW) using chemical and/or enzymatic treatments. Conversion of EW proteins into AFs during boiling was demonstrated by thioflavin T fluorescence, Congo red staining, and X-ray fiber diffraction measurements. Our data show that cooking converts approximately 1–3% of the protein in EW into AFs, suggesting that they are a common component of the human diet.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2020 American Chemical Society. This is an author produced version of an article published in Biomacromolecules. Uploaded in accordance with the publisher's self-archiving policy. |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 03 Jul 2020 15:24 |
Last Modified: | 23 Mar 2021 01:38 |
Status: | Published |
Publisher: | American Chemical Society |
Identification Number: | 10.1021/acs.biomac.0c00186 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:161872 |