<p>Pectinases, such as polygalacturonases, are a group of enzymes with an important role in the industrial clarification of fruit juices. This study aimed to optimize the production, purify, and characterize polygalacturonases from <i>Aspergillus niger</i> M2 and assess their potential to clarify different fruit juices. Two polygalacturonases (P1 and P2) were partially purified via a two-step process. P1 was obtained in 51.7% yield, with a purification factor of 27.5 And a specific activity of 41.2 U mg⁻¹ protein. P2 was produced in 32.5% yield, with a purification factor of 100 And a specific activity of 150.0 U mg⁻¹ protein. Both enzymes showed a molecular mass of approximately 110&#xa0;kDa. The optimal activity conditions for P1 were pH 4.0 And 55°C, whereas P2 activity peaked at pH 5.0 And 50°C. P1 retained over 90% of its activity after 4&#xa0;h at pH 4.0, and P2 showed no loss of activity after 2&#xa0;h of incubation at pH 3.0 to 5.0. Both enzymes exhibited high affinity for polygalacturonic acid, with <i>K</i>_M values of 1.9 And 1.6&#xa0;mg mL⁻¹, respectively, which confirms their identity as polygalacturonases. In juice clarification assays, the best results were obtained with plantain pulp, with P1 and P2 achieving 58.3% ± 43 And 63.4% ± 29 clarification, respectively. With ‘Haden’ mango pulp, with P1 and P2 resulting in 49.6% ± 34 And 45.8% ± 36 clarification, respectively. Overall, the findings indicate that polygalacturonases from <i>A. niger</i> M2 have great potential for use in the beverage industry.</p> Graphical Abstract <p></p>