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<p>This work explores an improved fungal-mediated bioconversion method for generating stable L-dopaquinone from L-phenylalanine using two <i>Aspergillus oryzae</i> strains (ISL 19 and ISL 27) and mycelial biomass. Mycelial biomass produced through submerged fermentation was exposed to controlled reaction setups to evaluate dopa-oxidase activity and resulting product formation. Quantification of L-dopaquinone was performed using dopachrome and dopa-oxidase assays, measured at 475&#xa0;nm and 505&#xa0;nm. Through systematic optimization of cultural and nutritional variables, the highest yield was obtained after 48&#xa0;h of incubation at pH 6.0 and 30&#xa0;°C. Among the tested nitrogen sources, urea (0.04% w/v), ammonium sulfate (0.12% w/v), and yeast extract (0.75% w/v) markedly improved the biotransformation process. Carbon-source optimization identified L-tyrosine (3.75&#xa0;mg/mL) and L-ascorbic acid (8.75&#xa0;mg/mL) as the most effective concentrations. Under the optimized conditions, strain ISL 27 produced a maximum L-dopaquinone level of 29.75&#xa0;µg/mL. Stabilizing agents—including ethanol, ortho-phosphoric acid, potassium-sodium tartrate, and glycerol—further boosted enzyme efficiency and product stability. Overall, the findings highlight <i>A. oryzae</i> as a promising biocatalyst for L-dopaquinone synthesis, supporting potential applications in pharmaceutical, cosmetic, and neurochemical fields. The study offers an environmentally friendly and scalable strategy for L-dopaquinone production and provides a framework for future research on fungal enzyme systems involved in neuroactive compound biosynthesis.</p>

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Bioconversion of L-phenylalanine to L-dopaquinone by Aspergillus oryzae: a scalable model for neurological precursor synthesis

  • 期刊论文

  • 发表日期：

    2026年5月11日

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  • Nasir Ali,
  • Sikander Ali,
  • Sibtain Ahmed,
  • Muhammad Usman Ahmad,
  • Muhammad Arshad,
  • Abdusamat Rasulov,
  • Otabek Kuziev

摘要

This work explores an improved fungal-mediated bioconversion method for generating stable L-dopaquinone from L-phenylalanine using two Aspergillus oryzae strains (ISL 19 and ISL 27) and mycelial biomass. Mycelial biomass produced through submerged fermentation was exposed to controlled reaction setups to evaluate dopa-oxidase activity and resulting product formation. Quantification of L-dopaquinone was performed using dopachrome and dopa-oxidase assays, measured at 475 nm and 505 nm. Through systematic optimization of cultural and nutritional variables, the highest yield was obtained after 48 h of incubation at pH 6.0 and 30 °C. Among the tested nitrogen sources, urea (0.04% w/v), ammonium sulfate (0.12% w/v), and yeast extract (0.75% w/v) markedly improved the biotransformation process. Carbon-source optimization identified L-tyrosine (3.75 mg/mL) and L-ascorbic acid (8.75 mg/mL) as the most effective concentrations. Under the optimized conditions, strain ISL 27 produced a maximum L-dopaquinone level of 29.75 µg/mL. Stabilizing agents—including ethanol, ortho-phosphoric acid, potassium-sodium tartrate, and glycerol—further boosted enzyme efficiency and product stability. Overall, the findings highlight A. oryzae as a promising biocatalyst for L-dopaquinone synthesis, supporting potential applications in pharmaceutical, cosmetic, and neurochemical fields. The study offers an environmentally friendly and scalable strategy for L-dopaquinone production and provides a framework for future research on fungal enzyme systems involved in neuroactive compound biosynthesis.