May 22, 2025 | Sustainable Chemistry for the Environment |
The study conducted by the State University of Southwestern Bahia, Brazil, examined the production and biochemical characterization of L-asparaginase using pitaya by-products as a substrate for solid-state fermentation. Aspergillus niger INCQS 40018 (ATCC 1004) was employed, with L-asparagine used as an inducer to determine optimal production conditions.
Optimization experiments were performed using a complete factorial design, focusing on moisture and inducer concentration as key variables. Results showed that maximum enzyme production occurred at 36 hours, with a 58.96% increase achieved under optimized conditions. The enzyme displayed optimal activity at 40 °C and pH 5.0, while maintaining stability between 20–40 °C and within pH 4.0–5.0.
Biochemical characterization further revealed that NaCl, CaCl2, and EDTA enhanced enzyme activity, whereas KCl and CuSO4 inhibited it at higher concentrations. At 1 mM, all compounds tested showed inhibitory effects, but at 5 mM, selective activation or inhibition was observed depending on the compound.
These findings highlight the potential of utilizing pitaya by-products as a sustainable substrate for enzyme production. The study demonstrates the feasibility of generating L-asparaginase with favorable biochemical properties, offering promising applications in biotechnology while promoting the valorization of agricultural residues.
