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<p>The development of sustainable nanobiocatalysts is a focal challenge in green chemistry, requiring robust and eco-friendly production methods. This study introduces a single-source strategy that addresses this challenge. By utilizing the fungus <i>Aspergillus niger</i> as a single biological factory to simultaneously produce a lipase enzyme and biosynthesize the iron oxide nanoparticles (IONPs) that serve as lipase matrix support. This integrated approach ensures a high degree of compatibility between the enzyme and its nanoparticle support, which was confirmed during the immobilization step by an 81.73% yield and a remarkable 97.4% activity retention. The resulting nanobiocatalyst demonstrated a distinct operational stability, broad pH tolerance, and maintained over 80% of its activity after eight consecutive reuse cycles. In practical applications, the catalyst showed powerful bioremediation capabilities, achieving near-complete (&gt; 95%) removal of industrial dyes and effective oil-stain removal from fabric. Our findings could establish that using a single biological source for both the enzyme and its immobilization matrix offers a new benchmark for future enzyme immobilization technologies.</p>

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Synthesis of an enhanced nanobiocatalyst system from Aspergillus niger as single green source

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年12月23日

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  • Mohamed G. Radwan,
  • Tarek M. Mohamed,
  • Radwa H. Abou-Saleh,
  • Hamed A. Abosharaf

摘要

The development of sustainable nanobiocatalysts is a focal challenge in green chemistry, requiring robust and eco-friendly production methods. This study introduces a single-source strategy that addresses this challenge. By utilizing the fungus Aspergillus niger as a single biological factory to simultaneously produce a lipase enzyme and biosynthesize the iron oxide nanoparticles (IONPs) that serve as lipase matrix support. This integrated approach ensures a high degree of compatibility between the enzyme and its nanoparticle support, which was confirmed during the immobilization step by an 81.73% yield and a remarkable 97.4% activity retention. The resulting nanobiocatalyst demonstrated a distinct operational stability, broad pH tolerance, and maintained over 80% of its activity after eight consecutive reuse cycles. In practical applications, the catalyst showed powerful bioremediation capabilities, achieving near-complete (> 95%) removal of industrial dyes and effective oil-stain removal from fabric. Our findings could establish that using a single biological source for both the enzyme and its immobilization matrix offers a new benchmark for future enzyme immobilization technologies.