Food amyloid fibrils are safe nutrition ingredients based on in-vitro and in-vivo assessment

Dan Xu, Jiangtao Zhou (), Wei Long Soon, Ines Kutzli, Adrian Molière, Sabine Diedrich, Milad Radiom, Stephan Handschin, Bing Li, Lin Li, Shana J. Sturla, Collin Y. Ewald and Raffaele Mezzenga ()
Additional contact information
Dan Xu: South China University of Technology
Jiangtao Zhou: Institute of Food, Nutrition and Health (IFNH), Department of Health Sciences and Technology (HEST), ETH Zurich
Wei Long Soon: Institute of Food, Nutrition and Health (IFNH), Department of Health Sciences and Technology (HEST), ETH Zurich
Ines Kutzli: Institute of Food, Nutrition and Health (IFNH), Department of Health Sciences and Technology (HEST), ETH Zurich
Adrian Molière: Institute of Translational Medicine, Department of Health Sciences and Technology (HEST), ETH Zurich
Sabine Diedrich: Institute of Food, Nutrition and Health (IFNH), Department of Health Sciences and Technology (HEST), ETH Zurich
Milad Radiom: Institute of Food, Nutrition and Health (IFNH), Department of Health Sciences and Technology (HEST), ETH Zurich
Stephan Handschin: Scientific Center for Optical and Electron Microscopy (ScopeM), ETH Zurich
Bing Li: South China University of Technology
Lin Li: South China University of Technology
Shana J. Sturla: Institute of Food, Nutrition and Health (IFNH), Department of Health Sciences and Technology (HEST), ETH Zurich
Collin Y. Ewald: Institute of Translational Medicine, Department of Health Sciences and Technology (HEST), ETH Zurich
Raffaele Mezzenga: Institute of Food, Nutrition and Health (IFNH), Department of Health Sciences and Technology (HEST), ETH Zurich

Nature Communications, 2023, vol. 14, issue 1, 1-14

Abstract: Abstract Food protein amyloid fibrils have superior technological, nutritional, sensorial, and physical properties compared to native monomers, but there is as yet insufficient understanding of their digestive fate and safety for wide consumption. By combining SDS-PAGE, ELISA, fluorescence, AFM, MALDI-MS, CD, microfluidics, and SAXS techniques for the characterization of β-lactoglobulin and lysozyme amyloid fibrils subjected to in-vitro gastrointestinal digestion, here we show that either no noticeable conformational differences exist between amyloid aggregates and their monomer counterparts after the gastrointestinal digestion process (as in β-lactoglobulin), or that amyloid fibrils are digested significantly better than monomers (as in lysozyme). Moreover, in-vitro exposure of human cell lines and in-vivo studies with C. elegans and mouse models, indicate that the digested fibrils present no observable cytotoxicity, physiological abnormalities in health-span, nor accumulation of fibril-induced plaques in brain nor other organs. These extensive in-vitro and in-vivo studies together suggest that the digested food amyloids are at least equally as safe as those obtained from the digestion of corresponding native monomers, pointing to food amyloid fibrils as potential ingredients for human nutrition.

Date: 2023
References: View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-023-42486-x Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-42486-x

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-023-42486-x

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().