The Lipase Enzyme Attached Micromotors for Degradation of Oils As Water Contaminant

In this study, a research design was implemented to investigate the potential of PPy-COOH/Ni micromotors for the degradation of oils as water pollutants. The study's objective was to determine the micromotors' capacity for oil removal. For this purpose, PPy-COOH/Ni micromotors were prepared by template-directed electrodeposition method, and lipase enzyme (from Porcine Pancreas) was covalently bound to these micromotors. The micromotors were characterized by SEM, EDX, and FTIR techniques. From the SEM photographs, it was found that the synthesized micromotors were cylindrical, about 5 μm in diameter and 15 μm in size. In addition, from the FTIR spectra, the binding of lipase enzyme to the micromotors was shown by amide I, II, and III bonds at 1640 cm^-1, 1540 cm^-1, and 1240 cm^-1. The present study has determined that the optimal pH level for lipase-attached micromotors is 8.0. Furthermore, the optimal temperature has been ascertained to be 45°C. In addition, the results of this study indicate that lipase-attached micromotors exhibit superior thermal and storage stability in comparison to free lipase. When the reusability of the immobilised lipase was examined, the immobilised lipase showed 73.5% activity even after five uses. The lipase-attached micromotors were tested on tributyrin triglyceride and were found to degrade 90% of the initial amount of tributyrin within 90 min. The findings obtained are consistent with existing literature on the subject, and these lipase-attached micromotors have the potential to be utilized in environmental applications, such as oil breakdown.