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Purpose <p>Although protease enzymes can be produced from various biomasses, limited information exists on protease enzymes production from coffee husk biomass using <i>Aspergillus niger</i> through solid-state fermentation (SSF). To bridge this gap, this research focuses on the biotransformation of coffee husk into protease enzymes utilizing <i>Aspergillus niger</i> through Solid-State Fermentation (SSF). The study encompasses process optimization, product analysis, and evaluation of the enzyme kinetics.</p> Methods <p>Taguchi design was applied to optimize SSF process considering variables moisture (70–80%), pH (3.5–5.5), incubation time (96–144&#xa0;h), and incubation temperature (30–40 <sup>O</sup>C). <i>Aspergillus niger</i> was employed for fermentation. Crude enzymes were harvested by filtration and centrifugation. Catalytic activity, total protein, biochemical effect, kinetic and thermodynamic properties of the enzymes were evaluated.</p> Results <p>At optimal conditions of moisture (80%), pH (3.5), incubation time (144&#xa0;h), and incubation temperature (40&#xa0;°C), the catalytic activity of protease enzymes derived from treated coffee husk (TCH-enzyme) and untreated coffee husk (UCH-enzyme) were 5.12 ± 0.69 U/mL and 2.43 ± 0.99 U/mL, respectively. Same optimal pH (7) and temperature (50 <sup>O</sup>C) were obtained for TCH and UCH-enzymes. The highest (319.05 ± 0.23%) and lowest (104.72 ± 0.08%) relative activity were recorded from Mn²⁺ and Zn²⁺ ions, respectively. The kinetic parameters (Km and Vmax) of TCH-enzyme were 1.797&#xa0;mg/mL and 9.247 × 10⁻⁴ µmol/mL.Sec, respectively. TCH-enzyme thermodynamic analysis result was activation free energy (ΔG<sup>≠</sup>) = 67.243&#xa0;kJ/mol, transition state formation energy (ΔG<sup>≠</sup> <sub>E−T</sub>) = 1.574&#xa0;kJ/mol, and substrate binding energy (ΔG<sup>≠</sup> <sub>ES</sub>) = 20.509&#xa0;kJ/mol. Catalytic efficiency (Ksp) of TCH was higher than UCH-enzyme.</p> Conclusion <p>Generally, coffee husk used to produce catalytically potent protease enzymes can be considered as a potential substrate for mass production.</p>

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Coffee Husk Biomass Valorization using Aspergillus niger via Solid State Fermentation: Process Optimization, Characterization, and Kinetic Studies of Protease Enzymes

  • 期刊论文

  • 发表日期：

    2025年1月8日

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  • Gashaw Muluken Tessera,
  • Nigus Gabbiye Habtu,
  • Metadel Kassahune Abera,
  • Fantahun Woldesenbet Misganaw

摘要

Purpose

Although protease enzymes can be produced from various biomasses, limited information exists on protease enzymes production from coffee husk biomass using Aspergillus niger through solid-state fermentation (SSF). To bridge this gap, this research focuses on the biotransformation of coffee husk into protease enzymes utilizing Aspergillus niger through Solid-State Fermentation (SSF). The study encompasses process optimization, product analysis, and evaluation of the enzyme kinetics.

Methods

Taguchi design was applied to optimize SSF process considering variables moisture (70–80%), pH (3.5–5.5), incubation time (96–144 h), and incubation temperature (30–40 OC). Aspergillus niger was employed for fermentation. Crude enzymes were harvested by filtration and centrifugation. Catalytic activity, total protein, biochemical effect, kinetic and thermodynamic properties of the enzymes were evaluated.

Results

At optimal conditions of moisture (80%), pH (3.5), incubation time (144 h), and incubation temperature (40 °C), the catalytic activity of protease enzymes derived from treated coffee husk (TCH-enzyme) and untreated coffee husk (UCH-enzyme) were 5.12 ± 0.69 U/mL and 2.43 ± 0.99 U/mL, respectively. Same optimal pH (7) and temperature (50 OC) were obtained for TCH and UCH-enzymes. The highest (319.05 ± 0.23%) and lowest (104.72 ± 0.08%) relative activity were recorded from Mn²⁺ and Zn²⁺ ions, respectively. The kinetic parameters (Km and Vmax) of TCH-enzyme were 1.797 mg/mL and 9.247 × 10⁻⁴ µmol/mL.Sec, respectively. TCH-enzyme thermodynamic analysis result was activation free energy (ΔG≠) = 67.243 kJ/mol, transition state formation energy (ΔG≠ E−T) = 1.574 kJ/mol, and substrate binding energy (ΔG≠ ES) = 20.509 kJ/mol. Catalytic efficiency (Ksp) of TCH was higher than UCH-enzyme.

Conclusion

Generally, coffee husk used to produce catalytically potent protease enzymes can be considered as a potential substrate for mass production.