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Evidence of global relevance

Alcalase-derived egg white hydrolysates exhibit ACE inhibition In silico and gut microbiota modulation In vivo

Thai researchers identified egg-white-derived peptides with simulated ACE binding and found that 14-day administration of the hydrolysate to male rats altered gut microbial diversity and composition. This is preclinical evidence and does not establish blood-pressure or metabolic benefits in humans.

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Key findings

  • Six putative peptides were identified. MANKGPAYGM and NVLQPSSVDSQ had predicted ACE-binding free energies of -14.4 and -13.8 kcal/mol and predicted Kd values of 2.7×10^-11 and 8×10^-11 M. The 100-nanosecond simulations supported complex stability. In rats, EWH increased alpha diversity and enriched Prevotella, Paraprevotella, Sutterella, Butyricimonas, and Barnesiella.
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Why this matters globally

Multifunctional food-derived peptides are of interest for functional-food development. This study provides molecular candidates and microbiome signals for subsequent biochemical validation, blood-pressure studies, and safety assessment.

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Thai researcher contribution

Researchers from Khon Kaen University, Kalasin University, and Prince of Songkla University integrated food science, proteomics, bioinformatics, and biomedical research, with multiple Khon Kaen University units contributing.

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Limitations to consider

ACE binding was predicted in silico rather than confirmed with purified-peptide biochemical assays. The microbiome experiment used only six male rats per group for 14 days, and the abstract reports no direct blood-pressure outcome. The findings must not be interpreted as a treatment for human hypertension.

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Verify the original sources

Scientific ReportsRead the original article

DOI: 10.1038/s41598-026-60508-8

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