<p>The production of acid phosphatase (ACPase) by <i>Trichoderma spp</i>. was evaluated and optimized under submerged fermentation using low-cost culture media. Among the strains tested, <i>T. reesei</i> showed the highest enzymatic potential. A Central Composite Design was applied to assess the effects of sucrose, yeast extract, and KH₂PO₄ on ACPase activity. The optimized medium (MSO-Tr) resulted in a maximum enzymatic activity of 1.96 ± 0.14 U/mL and biomass production of 5.32 ± 0.48&#xa0;g/L, representing a 3.3-fold increase compared to preliminary conditions. <i>T. harzianum</i> and <i>T. asperellum</i> showed lower activities, reaching 0.81 ± 0.05 U/mL and 0.76 ± 0.12 U/mL, respectively. Substrate consumption analysis indicated complete utilization of sucrose and glucose within 48&#xa0;h for <i>T. reesei</i>. Response surface analysis demonstrated that yeast extract positively influenced enzyme production, whereas excess phosphate had inhibitory effects depending on the strain. SDS-PAGE analysis revealed protein bands in the 58–69&#xa0;kDa range, consistent with the reported molecular weights of fungal acid phosphatases. These results demonstrate the effectiveness of statistical optimization and highlight the biotechnological potential of <i>Trichoderma</i>-derived ACPases produced using low-cost substrates.</p>

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Statistical optimization of acid phosphatase production by Trichoderma spp. in submerged fermentation

  • Frederico Alves Lima,
  • Jussara Maria Martins de Almeida Afonso,
  • Amanda Rocha Carmelo,
  • Miriam Maria de Resende

摘要

The production of acid phosphatase (ACPase) by Trichoderma spp. was evaluated and optimized under submerged fermentation using low-cost culture media. Among the strains tested, T. reesei showed the highest enzymatic potential. A Central Composite Design was applied to assess the effects of sucrose, yeast extract, and KH₂PO₄ on ACPase activity. The optimized medium (MSO-Tr) resulted in a maximum enzymatic activity of 1.96 ± 0.14 U/mL and biomass production of 5.32 ± 0.48 g/L, representing a 3.3-fold increase compared to preliminary conditions. T. harzianum and T. asperellum showed lower activities, reaching 0.81 ± 0.05 U/mL and 0.76 ± 0.12 U/mL, respectively. Substrate consumption analysis indicated complete utilization of sucrose and glucose within 48 h for T. reesei. Response surface analysis demonstrated that yeast extract positively influenced enzyme production, whereas excess phosphate had inhibitory effects depending on the strain. SDS-PAGE analysis revealed protein bands in the 58–69 kDa range, consistent with the reported molecular weights of fungal acid phosphatases. These results demonstrate the effectiveness of statistical optimization and highlight the biotechnological potential of Trichoderma-derived ACPases produced using low-cost substrates.