Scholarlink

<p>Polycyclic aromatic hydrocarbons (PAHs) are hazardous environmental contaminants emerging from industrial activities and fossil fuel combustion, posing risks to human health and ecosystems. Biodegradation offers a sustainable approach to mitigating PAH pollution, and here we investigated the efficacy of a peptide hybrid of laccase and O-methyltransferase enzymes from the bacterium <i>Burkholderia cepacia</i> in PAH degradation. Both enzymes demonstrated stability with an instability index below 40, indicating suitability for environmental application. Following active site prediction, the 3D structure of the peptide hybrid, consisting of 71 amino acids, was modelled using trRosetta, achieving a high-quality structure with an ERRAT score above 97%. Further bioinformatic analysis confirmed the hybrid’s non-allergenic and non-virulent properties. Molecular docking studies revealed a robust binding affinity above − 9&#xa0;kcal/mol, highlighting this peptide hybrid’s potential for effective PAH degradation and suggesting its promise as an eco-friendly bioremediation agent for PAH-contaminated sites.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Elucidating the synergistic role of hybrid peptide from Burkholderia cepacia enzymes in biodegradation of polycyclic aromatic hydrocarbons

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2025年4月12日

查看全文
  • Muhammad Naveed,
  • Ayesha Saleem,
  • Tariq Aziz,
  • Khadija Khatoon,
  • Maida Salah Ud Din,
  • Ahiba Adil,
  • Mitub Al-harbi,
  • Abdullah F. Alasmari

摘要

Polycyclic aromatic hydrocarbons (PAHs) are hazardous environmental contaminants emerging from industrial activities and fossil fuel combustion, posing risks to human health and ecosystems. Biodegradation offers a sustainable approach to mitigating PAH pollution, and here we investigated the efficacy of a peptide hybrid of laccase and O-methyltransferase enzymes from the bacterium Burkholderia cepacia in PAH degradation. Both enzymes demonstrated stability with an instability index below 40, indicating suitability for environmental application. Following active site prediction, the 3D structure of the peptide hybrid, consisting of 71 amino acids, was modelled using trRosetta, achieving a high-quality structure with an ERRAT score above 97%. Further bioinformatic analysis confirmed the hybrid’s non-allergenic and non-virulent properties. Molecular docking studies revealed a robust binding affinity above − 9 kcal/mol, highlighting this peptide hybrid’s potential for effective PAH degradation and suggesting its promise as an eco-friendly bioremediation agent for PAH-contaminated sites.