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<p>Microbial pectinases, classified within the hydrolase family, play a crucial role in various industrial applications, including food and beverage processing, textile manufacturing, and wastewater treatment. This study investigates the production, purification, biochemical characterization, and potential applications of pectinase derived from the endophytic fungal strain <i>Aspergillus sydowii</i> EF 375, isolated from the mangrove plant <i>Ceriops tagal</i>. Pectinase production was optimized using Response Surface Methodology (RSM), resulting in a 2.2-fold enhancement in enzyme production. The enzyme was subsequently purified, achieving a recovery yield of 3.2% and a specific activity of 73.05 U/mg. Zymogram analysis confirmed the purified pectinase to have a molecular weight of approximately 43&#xa0;kDa. Kinetic studies revealed a maximum reaction velocity (Vmax) of 161.29&#xa0;µmol/min and a Michaelis constant (Km) of 0.177&#xa0;mg/ml, indicating high substrate affinity. The enzyme exhibited optimal catalytic efficiency at 50&#xa0;°C and pH 5. The activity of the enzyme was notably enhanced by the presence of K⁺, Cu<sup>2</sup>⁺, Fe<sup>2</sup>⁺, Mg<sup>2</sup>⁺, Mn<sup>2</sup>⁺, Pb<sup>2</sup>⁺, and Zn<sup>2</sup>⁺ ions (at concentrations up to 10&#xa0;mM), while Li⁺, Hg<sup>2</sup>⁺, and Ni<sup>2</sup>⁺ acted as inhibitors. Functional applications demonstrated that the purified pectinase significantly improved the clarity of fruit juices, including apple, grape, pineapple, and orange. Furthermore, the enzyme exhibited potential in inhibiting bacterial biofilm formation, highlighting its applicability in antimicrobial and biotechnological interventions.</p> Graphical Abstract

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A Multifunctional Pectinase from the Manglicolous Endophytic Fungus, Aspergillus sydowii EF 375: Process Optimization, Characterization and Application Potentials

  • 期刊论文

  • 发表日期：

    2025年7月7日

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  • M R Revathy,
  • Anjali S. Mohan,
  • Dhanya Kesavan,
  • Hafsa Kattatheyil,
  • S Neelima,
  • M V Anju,
  • Rosamma Philip

摘要

Microbial pectinases, classified within the hydrolase family, play a crucial role in various industrial applications, including food and beverage processing, textile manufacturing, and wastewater treatment. This study investigates the production, purification, biochemical characterization, and potential applications of pectinase derived from the endophytic fungal strain Aspergillus sydowii EF 375, isolated from the mangrove plant Ceriops tagal. Pectinase production was optimized using Response Surface Methodology (RSM), resulting in a 2.2-fold enhancement in enzyme production. The enzyme was subsequently purified, achieving a recovery yield of 3.2% and a specific activity of 73.05 U/mg. Zymogram analysis confirmed the purified pectinase to have a molecular weight of approximately 43 kDa. Kinetic studies revealed a maximum reaction velocity (Vmax) of 161.29 µmol/min and a Michaelis constant (Km) of 0.177 mg/ml, indicating high substrate affinity. The enzyme exhibited optimal catalytic efficiency at 50 °C and pH 5. The activity of the enzyme was notably enhanced by the presence of K⁺, Cu2⁺, Fe2⁺, Mg2⁺, Mn2⁺, Pb2⁺, and Zn2⁺ ions (at concentrations up to 10 mM), while Li⁺, Hg2⁺, and Ni2⁺ acted as inhibitors. Functional applications demonstrated that the purified pectinase significantly improved the clarity of fruit juices, including apple, grape, pineapple, and orange. Furthermore, the enzyme exhibited potential in inhibiting bacterial biofilm formation, highlighting its applicability in antimicrobial and biotechnological interventions.

Graphical Abstract