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<p>L-Asparaginase is widely used as an antineoplastic agent and as a biocatalyst to reduce acrylamide formation in thermally processed foods. Acrylamide is mainly generated through the Maillard reaction in carbohydrate-rich matrices, such as fried potatoes, and is considered a potential carcinogen. Although enzymatic pretreatment with L-asparaginase is the most effective mitigation strategy, its large-scale application remains limited by the high production costs associated with conventional enzymatic sources. This study assessed the production of L-asparaginase by the coculture of <i>Rhizopus microsporus</i> var. oligosporus and <i>Penicillium camemberti</i> in solid-state fermentation (SSF). The simplex-centroid design identified the optimal substrate formulation, equal proportions of cocoa bean shell, coffee parchment, and ora-pro-nobis leaves which increased enzyme production by 66%, yielding 8.69 U/g. Subsequent optimization using a Box–Behnken design improved the fermentation conditions (135&#xa0;h at 26&#xa0;°C and 68% initial moisture), resulting in an activity of 11.0 U/g. The crude enzymatic extract (CEE) exhibited optimal activity at pH 8.0, retained stability up to pH 9.0, and showed maximal thermal stability at 40&#xa0;°C, maintaining 64% activity even at 70&#xa0;°C. Enzyme activity was enhanced by Na⁺, Cu<sup>2</sup>⁺, and Mn<sup>2</sup>⁺ with increases of up to 182%, while Mg<sup>2</sup>⁺ and Ca<sup>2</sup>⁺ demonstrated inhibitory effects. The enzyme also displayed halotolerance, with optimal performance at 2&#xa0;M NaCl, and was stimulated by ethanol, reaching 135% activity at 30%. Pretreatment of French fries with the CEE reduced acrylamide formation by up to 75%. These results demonstrate that L-asparaginase obtained via solid-state fermentation represents a cost-effective and practical biotechnological strategy for acrylamide mitigation, eliminating the need for purification steps.</p> Graphical Abstract <p></p>

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L-Asparaginase Production by Fungal Coculture Under Solid-State Fermentation: Biochemical Characterization and Application in French Fries for Acrylamide Mitigation

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年3月14日

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  • Jabson Meneses Teixeira,
  • Nívio Batista Santana,
  • Thais Santos Moraes Lima,
  • Ivonéa Soares do Nascimento,
  • Abdias Batista da Silva Neto,
  • Floriatan Santos Costa,
  • Iasnaia Maria de Carvalho Tavares,
  • Rúbner Gonçalves Pereira,
  • Grazielly de Jesus Silva,
  • Fabiane Neves Silva,
  • Cassamo Ussemane Mussagy,
  • Angie Vanessa Caicedo-Paz,
  • Marcelo Franco

摘要

L-Asparaginase is widely used as an antineoplastic agent and as a biocatalyst to reduce acrylamide formation in thermally processed foods. Acrylamide is mainly generated through the Maillard reaction in carbohydrate-rich matrices, such as fried potatoes, and is considered a potential carcinogen. Although enzymatic pretreatment with L-asparaginase is the most effective mitigation strategy, its large-scale application remains limited by the high production costs associated with conventional enzymatic sources. This study assessed the production of L-asparaginase by the coculture of Rhizopus microsporus var. oligosporus and Penicillium camemberti in solid-state fermentation (SSF). The simplex-centroid design identified the optimal substrate formulation, equal proportions of cocoa bean shell, coffee parchment, and ora-pro-nobis leaves which increased enzyme production by 66%, yielding 8.69 U/g. Subsequent optimization using a Box–Behnken design improved the fermentation conditions (135 h at 26 °C and 68% initial moisture), resulting in an activity of 11.0 U/g. The crude enzymatic extract (CEE) exhibited optimal activity at pH 8.0, retained stability up to pH 9.0, and showed maximal thermal stability at 40 °C, maintaining 64% activity even at 70 °C. Enzyme activity was enhanced by Na⁺, Cu2⁺, and Mn2⁺ with increases of up to 182%, while Mg2⁺ and Ca2⁺ demonstrated inhibitory effects. The enzyme also displayed halotolerance, with optimal performance at 2 M NaCl, and was stimulated by ethanol, reaching 135% activity at 30%. Pretreatment of French fries with the CEE reduced acrylamide formation by up to 75%. These results demonstrate that L-asparaginase obtained via solid-state fermentation represents a cost-effective and practical biotechnological strategy for acrylamide mitigation, eliminating the need for purification steps.

Graphical Abstract