TY - JOUR
T1 - Digestive fate of milk and egg-derived amyloids
T2 - Attenuated digestive proteolysis and impact on the trajectory of the gut microbiota
AU - Refael, Gil
AU - Engelberg, Yizhaq
AU - Romano, Alon
AU - Amiram, Gabriela
AU - Barnea, Eilon
AU - Shani Levi, Carmit
AU - Turjeman, Sondra
AU - Landau, Meytal
AU - Koren, Omry
AU - Lesmes, Uri
N1 - Publisher Copyright:
© 2024 Elsevier Ltd
PY - 2024/6
Y1 - 2024/6
N2 - In an era in which protein consumption is enthusiastically advocated, this work explored the possible formation of proteinaceous amyloids in foods and their unchartered digestive fate. Evidence herein corroborates processing induces formation of amyloid-like architectures from β-lactoglobulin or ovalbumin. Such supramolecular assemblies exhibit attenuated susceptibility to gastric and intestinal proteolysis and may persist into the colon as confirmed by SDS-PAGE, LCMS, ThT analysis and TEM imaging. Human fecal fermentations of fibrils or their native protein counterparts establish that fibrilization helps maintain microbial diversity, low Firmicutes/Bacteroidetes ratio (Av. F/B ratio<3.00) and protect the butyrate producing genera Roseburia and Clostridium. In addition, fibrilization increased the minimal inhibitory concentration (MIC) of ovalbumin by at least two orders of magnitude without altering its negligible cytotoxicity. Further, In silico analyses support that both fibrils divert predicted microbiota metabolic trajectories towards those observed in fermentation of prebiotics. Thus, this work provides reassuring evidence against possible adverse effects of fibrilization of edible proteins. Yet, human trials with processed foods should be warranted to clinically affirm these findings.
AB - In an era in which protein consumption is enthusiastically advocated, this work explored the possible formation of proteinaceous amyloids in foods and their unchartered digestive fate. Evidence herein corroborates processing induces formation of amyloid-like architectures from β-lactoglobulin or ovalbumin. Such supramolecular assemblies exhibit attenuated susceptibility to gastric and intestinal proteolysis and may persist into the colon as confirmed by SDS-PAGE, LCMS, ThT analysis and TEM imaging. Human fecal fermentations of fibrils or their native protein counterparts establish that fibrilization helps maintain microbial diversity, low Firmicutes/Bacteroidetes ratio (Av. F/B ratio<3.00) and protect the butyrate producing genera Roseburia and Clostridium. In addition, fibrilization increased the minimal inhibitory concentration (MIC) of ovalbumin by at least two orders of magnitude without altering its negligible cytotoxicity. Further, In silico analyses support that both fibrils divert predicted microbiota metabolic trajectories towards those observed in fermentation of prebiotics. Thus, this work provides reassuring evidence against possible adverse effects of fibrilization of edible proteins. Yet, human trials with processed foods should be warranted to clinically affirm these findings.
KW - Amyloid fibrils
KW - Anaerobic colonic fermentation
KW - Dairy protein
KW - Egg white protein
KW - Gut microbiota
KW - In vitro digestion
UR - http://www.scopus.com/inward/record.url?scp=85185196373&partnerID=8YFLogxK
U2 - 10.1016/j.foodhyd.2024.109820
DO - 10.1016/j.foodhyd.2024.109820
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AN - SCOPUS:85185196373
SN - 0268-005X
VL - 151
JO - Food Hydrocolloids
JF - Food Hydrocolloids
M1 - 109820
ER -