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<p>L-asparaginase is an important therapeutic and food-processing enzyme widely produced by bacteria and fungi. In this study, a fungal isolate designated as strain SK5 was identified as <i>Neurospora sitophila</i> based on morphological characteristics and ITS rDNA sequencing (98.62% similarity; 100% bootstrap support), ensuring accurate species-level identification. Although several fungal genera have been reported to produce L-asparaginase, to the best of our knowledge this study represents the first biochemical characterization and process optimization of L-asparaginase production from <i>N. sitophila</i>. Preliminary screening revealed moderate enzyme activity comparable to that of several <i>Aspergillus</i> spp. Enzyme production increased gradually during submerged fermentation, peaking after 72&#xa0;h. Optimization of carbon and nitrogen sources enhanced activity, while statistical designs (Plackett–Burman followed by central composite design) further improved production, representing a significant increase compared to the basal medium. The enzyme exhibited optimal activity at 40&#xa0;°C and pH 8.0, maintaining stability within moderate temperature and pH ranges. Kinetic and metal ion analyses indicated favorable catalytic properties. The balanced biochemical profile, potential safety advantages, and non-pathogenic nature of <i>N. sitophila</i> SK5 suggest its promise as a fungal source of L-asparaginase for therapeutic and food-processing applications. This work provides a foundation for future studies on enzyme purification, structural characterization, and evaluation of anticancer or acrylamide-reducing activities.</p>

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L-Asparaginase production by Neurospora sitophila SK5: from identification to bioprocess optimization

  • 期刊论文

  • 发表日期：

    2025年12月9日

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  • Saliha Kaouache,
  • Ouided Benslama,
  • Sabrina Lekmine,
  • Hichem Tahraoui,
  • Mohammad Shamsul Ola,
  • Abdeltif Amrane

摘要

L-asparaginase is an important therapeutic and food-processing enzyme widely produced by bacteria and fungi. In this study, a fungal isolate designated as strain SK5 was identified as Neurospora sitophila based on morphological characteristics and ITS rDNA sequencing (98.62% similarity; 100% bootstrap support), ensuring accurate species-level identification. Although several fungal genera have been reported to produce L-asparaginase, to the best of our knowledge this study represents the first biochemical characterization and process optimization of L-asparaginase production from N. sitophila. Preliminary screening revealed moderate enzyme activity comparable to that of several Aspergillus spp. Enzyme production increased gradually during submerged fermentation, peaking after 72 h. Optimization of carbon and nitrogen sources enhanced activity, while statistical designs (Plackett–Burman followed by central composite design) further improved production, representing a significant increase compared to the basal medium. The enzyme exhibited optimal activity at 40 °C and pH 8.0, maintaining stability within moderate temperature and pH ranges. Kinetic and metal ion analyses indicated favorable catalytic properties. The balanced biochemical profile, potential safety advantages, and non-pathogenic nature of N. sitophila SK5 suggest its promise as a fungal source of L-asparaginase for therapeutic and food-processing applications. This work provides a foundation for future studies on enzyme purification, structural characterization, and evaluation of anticancer or acrylamide-reducing activities.