Immobilization of thermostable lipase qlm on core-shell structured polydopamine-coated Fe3O4 nanoparticles

Abstract

Here, core-shell structured polydopamine-coated Fe3O4 nanoparticles were constructed to immobilize thermostable lipase QLM from Alcaligenes sp. Systematical characterization indicated that lipase QLM was successfully immobilized on the surface of nanoparticles with an enzyme loading of 21.4 ± 1.47 mg/g immobilized enzyme. Then, the immobilized enzyme was demonstrated to possess favorable catalytic activity and stability in the ester hydrolysis, using p-nitrophenyl caprylate as the substrate. Further, it was successfully employed in the kinetic resolution of (R, S)-2-octanol, and satisfactory enantioselectivity and recyclability could be obtained with an enantiomeric ratio (E) of 8–15 over 10 cycle reactions. Thus, core-shell structured polydopamine-coated Fe3O4 nanoparticles can be potentially used as a carrier for enzyme immobilization to improve their activity, stability, and reusability, which is beneficial for constructing efficient catalysts for industrial biocatalysis.