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<p>This study focuses on optimizing, purifying, and characterizing xylanase produced by <i>Aspergillus krugeri</i> AUMC 15912 utilizing sugarcane bagasse under solid-state fermentation (SSF). The strain, isolated from sugarcane bagasse, exhibited significant xylanase activity, which was maximized after six days of incubation at pH 7.0 and 30&#xa0;°C using ammonium chloride as the nitrogen source, yielding 183 ± 16 U/g dry substrate (gds). The enzyme was purified 508-fold through sequential chromatography on Trilite MC 08 and Sephacryl S-200 columns, resulting in a single band of 33.11&#xa0;kDa on SDS-PAGE. The purified xylanase displayed peak activity of 1697.5 U/mg at pH 6.0 and 45&#xa0;°C, with kinetic parameters Km and Vmax of 1.75 mM and 17.98 µmol/min, respectively. Activity was influenced by various salts and inhibitors, with residual activity ranging from 30.12% (NiCl₂) to 86.65% (CuSO₄). These findings highlight the potential of <i>A. krugeri</i> AUMC 15912-derived xylanase for industrial applications in bioconversion, food processing, and biofuel production.</p>

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Purification, and characterization of xylanase by Aspergillus krugeri AUMC 15912 utilizing sugarcane bagasse under solid-state fermentation conditions

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年2月9日

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  • Aya A. A. Abdel-Hafeez,
  • Abdel-Raouf M. Khallil,
  • Elhagag A. Hassan,
  • Osama A. M. Al-Bedak

摘要

This study focuses on optimizing, purifying, and characterizing xylanase produced by Aspergillus krugeri AUMC 15912 utilizing sugarcane bagasse under solid-state fermentation (SSF). The strain, isolated from sugarcane bagasse, exhibited significant xylanase activity, which was maximized after six days of incubation at pH 7.0 and 30 °C using ammonium chloride as the nitrogen source, yielding 183 ± 16 U/g dry substrate (gds). The enzyme was purified 508-fold through sequential chromatography on Trilite MC 08 and Sephacryl S-200 columns, resulting in a single band of 33.11 kDa on SDS-PAGE. The purified xylanase displayed peak activity of 1697.5 U/mg at pH 6.0 and 45 °C, with kinetic parameters Km and Vmax of 1.75 mM and 17.98 µmol/min, respectively. Activity was influenced by various salts and inhibitors, with residual activity ranging from 30.12% (NiCl₂) to 86.65% (CuSO₄). These findings highlight the potential of A. krugeri AUMC 15912-derived xylanase for industrial applications in bioconversion, food processing, and biofuel production.