Immobilization of Thermostable Lipase QLM on Core-Shell Structured Polydopamine-Coated Fe3O4 Nanoparticles

Here, core-shell structured polydopamine-coated Fe3O4nanoparticles were constructed to immobilize thermostable lipase QLM fromAlcaligenessp. 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, usingp-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 Fe3O4nanoparticles 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.Keywords:lipase;immobilization;polydopamine;Fe3O4nanoparticle;core-shell structure;ester hydrolysis;kinetic resolution