Immobilization of Candida rugosa lipase for resolution of racimic ibuprofen

Aim Due to lipases' regio-selectivity and ability to catalyze different reactions such as hydrolysis, esterification, and transesterification, the enzyme is attractive in biotransformation technology. Besides, another technology, namely enzyme immobilization, has attracted scientists/technologists' attention to employ immobilized lipase in such a field. Thus lipase of Candida rugosa was immobilized onto silica nanoparticles through adsorption. Furthermore, the immobilized biocatalyst was characterized and used to esterify ibuprofen enantioselectively. Methods To characterize immobilized lipase onto silica nanoparticles scanning electron microscopy (SEM) and dynamic light scattering (DLS) were used. Results The catalytic properties of both immobilized and free lipases such as optima pH and temperature were not different. According to the results, the immobilized lipase on silica nanoparticles showed 45% and 96% conversion (C) and enantioselectivity (ee(s)), respectively. In comparison to free lipase, the immobilized enzyme came with better catalytic activity. Conclusion Silica nanoparticles as one of the most promising materials for the immobilization of lipase in enantioselective esterification of ibuprofen, were introduced in this work.

Automated summary

This study introduced the immobilization of Candida rugosa lipase onto silica nanoparticles for enantioselective esterification of ibuprofen. The immobilized enzyme exhibited better catalytic activity and has great potential for the esterification reaction of ibuprofen.