Development of biopolymer encapsulated enzyme for efficient acetaminophen degradation

The study aimed to investigate the effectiveness of partially purified turnip (Brassica rapa) peroxidase immobilized in calcium alginate for degrading paracetamol, also known as acetaminophen (AAP), a commonly used overthe- counter analgesic and antipyretic. The encapsulation of peroxidase was optimized to minimize enzyme leakage and maintain maximum activity by adjusting the sodium alginate content, enzyme loading, and calcium chloride concentration. The optimal conditions for encapsulating peroxidase in calcium alginate matrices with the best retention and efficiency were determined to be 1.3 U/mL enzyme loading, 1.5 % sodium alginate, and 0.05 M calcium chloride concentration. This research focuses on investigating the efficacy and application of immobilized turnip peroxidase in degrading pharmaceutical effluents, specifically targeting paracetamol. The results revealed the maximum degradation of AAP at a pH of 2.0 and a temperature of 30?C, with paracetamol and hydrogen peroxide concentrations of 1g/L and 1.2 mol/L, respectively, resulting in a 97% yield using the stabilized peroxidase. The study also determined the kinetic characteristics of the enzymatic reaction, such as the maximum rate and the Michaelis?Menten constant. Furthermore, the stabilized enzyme can be utilized multiple times, specifically up to three occasions, in ideal conditions, while maintaining 80% of its ability to degrade AAP.