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<p>This study explores the fabrication and characterization of advanced polycaprolactone (PCL)/chitosan (CS)/manganese (II) oxide (MnO) nanofiber for the immobilization of arginase. The nanofiber was synthesized via electrospinning, and the optimal conditions were determined to be 10% (w/v) PCL, 2% (w/v) CS, and 0.3% (w/v) MnO, with a needle-collector distance of 18&#xa0;cm, a voltage of 26&#xa0;kV, and a flow rate of 0.5&#xa0;mL/h. The structural and morphological properties were characterized using scanning electron microscopy (SEM) and attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR), revealing a uniform morphology with high surface area and porosity. Arginase was immobilized onto the nanofiber via adsorption followed by cross-linking using glutaraldehyde. The immobilized enzyme displayed enhanced pH stability and retained more than 50% of its activity after 10 reuse cycles. The optimum pH remained 10 for both free and immobilized enzymes; however, the immobilized form exhibited improved activity across a broader pH range. These results indicate that MnO-based PCL/CS nanofibers provide a promising support matrix for enzyme immobilization, with potential applications in biocatalysis, therapeutic enzyme delivery, biosensor platforms, and environmental biotechnology.</p>

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Polycaprolactone/chitosan/manganese (II) oxide nanofiber: improving pH stability of arginase enzyme

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年6月10日

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  • Ceyhun Işık,
  • Mustafa Teke

摘要

This study explores the fabrication and characterization of advanced polycaprolactone (PCL)/chitosan (CS)/manganese (II) oxide (MnO) nanofiber for the immobilization of arginase. The nanofiber was synthesized via electrospinning, and the optimal conditions were determined to be 10% (w/v) PCL, 2% (w/v) CS, and 0.3% (w/v) MnO, with a needle-collector distance of 18 cm, a voltage of 26 kV, and a flow rate of 0.5 mL/h. The structural and morphological properties were characterized using scanning electron microscopy (SEM) and attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR), revealing a uniform morphology with high surface area and porosity. Arginase was immobilized onto the nanofiber via adsorption followed by cross-linking using glutaraldehyde. The immobilized enzyme displayed enhanced pH stability and retained more than 50% of its activity after 10 reuse cycles. The optimum pH remained 10 for both free and immobilized enzymes; however, the immobilized form exhibited improved activity across a broader pH range. These results indicate that MnO-based PCL/CS nanofibers provide a promising support matrix for enzyme immobilization, with potential applications in biocatalysis, therapeutic enzyme delivery, biosensor platforms, and environmental biotechnology.