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<p>This study investigated the dual ACE-inhibitory and gut microbiota-modulating potential of egg white hydrolysate (EWH), obtained through Alcalase enzymatic hydrolysis. LC-ESI-MS/MS analysis of the most bioactive fraction (F2), which exhibited strong antioxidant and antibacterial activities, identified six putative bioactive peptides: VLLPDEVSGL, MANKGPAYGM, AAAAGLNPGLM, GIIQHEL, MAGFVPLLLL, and NVLQPSSVDSQ. Molecular docking revealed that EWH-2 (MANKGPAYGM) and EWH-6 (NVLQPSSVDSQ) exhibited the strongest binding to ACE, with Gibbs free energies (ΔG) of − 14.4 and − 13.8&#xa0;kcal/mol and dissociation constants (Kd) of 2.7 × 10⁻¹¹ M and 8 × 10⁻¹¹ M, respectively. These interactions involved the S1, S2, and zinc-binding motifs via hydrophobic interactions and hydrogen bonds. These findings were supported by 100 ns molecular dynamics simulations, confirming stable ACE–peptide complexes with particularly favorable binding for EWH-2. <i>In vivo</i> administration of EWH to male rats for 14 days (<i>n</i> = 6 per group) significantly increased gut microbial alpha diversity and reshaped microbial community composition. EWH treatment enriched genera such as <i>Prevotella</i>, <i>Paraprevotella</i>, <i>Sutterella</i>, <i>Butyricimonas</i>, and <i>Barnesiella</i>, which are associated with short-chain fatty acid production and metabolic health. Collectively, these findings demonstrate that Alcalase-derived EWH exhibits dual ACE-inhibitory and gut microbiota-modulating activities, suggesting potential benefits for blood pressure regulation and metabolic health.</p>

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

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年7月8日

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  • Wisarut Payoungkiattikun,
  • Theerawat Dobutr,
  • Napaporn Roamcharern,
  • Nisachon Jangpromma,
  • Sompong Klaynongsruang,
  • Jureerut Daduang,
  • Sakda Daduang,
  • Rina Patramanon

摘要

This study investigated the dual ACE-inhibitory and gut microbiota-modulating potential of egg white hydrolysate (EWH), obtained through Alcalase enzymatic hydrolysis. LC-ESI-MS/MS analysis of the most bioactive fraction (F2), which exhibited strong antioxidant and antibacterial activities, identified six putative bioactive peptides: VLLPDEVSGL, MANKGPAYGM, AAAAGLNPGLM, GIIQHEL, MAGFVPLLLL, and NVLQPSSVDSQ. Molecular docking revealed that EWH-2 (MANKGPAYGM) and EWH-6 (NVLQPSSVDSQ) exhibited the strongest binding to ACE, with Gibbs free energies (ΔG) of − 14.4 and − 13.8 kcal/mol and dissociation constants (Kd) of 2.7 × 10⁻¹¹ M and 8 × 10⁻¹¹ M, respectively. These interactions involved the S1, S2, and zinc-binding motifs via hydrophobic interactions and hydrogen bonds. These findings were supported by 100 ns molecular dynamics simulations, confirming stable ACE–peptide complexes with particularly favorable binding for EWH-2. In vivo administration of EWH to male rats for 14 days (n = 6 per group) significantly increased gut microbial alpha diversity and reshaped microbial community composition. EWH treatment enriched genera such as Prevotella, Paraprevotella, Sutterella, Butyricimonas, and Barnesiella, which are associated with short-chain fatty acid production and metabolic health. Collectively, these findings demonstrate that Alcalase-derived EWH exhibits dual ACE-inhibitory and gut microbiota-modulating activities, suggesting potential benefits for blood pressure regulation and metabolic health.