Immobilization of Candida rugosa lipase on magnetic sol–gel composite supports for enzymatic resolution of (R,S)-Naproxen methyl ester

In the present study, the Candida rugosa lipase (CRL) was encapsulated within a chemically inert sol–gel support prepared by polycondensation with tetraethoxysilane (TEOS) and octyltriethoxysilane (OTES) in the presence and absence of magnetic Fe3O4 nanoparticles or sporopollenin with Fe3O4 as additive. The catalytic properties of the immobilized lipases were evaluated through model reactions, i.e. the hydrolysis of p-nitrophenylpalmitate (p-NPP), and the enantioselective hydrolysis of racemic Naproxen methyl ester that was studied in aqueous buffer solution/isooctane reaction system. The results indicate that the sporopollenin based encapsulated lipase (Fe3O4-Spo-E) particularly has higher conversion and enantioselectivity compared to the encapsulated lipase without supports (lipase-enc). It has also been noticed that the sporopollenin based encapsulated lipase has excellent enantioselectivity (E = >400) as compared to the free enzyme (E = 166) with an ee value of ∼98% for S-Naproxen.