Covalent immobilization of lipase on an ionic liquid-functionalized magnetic Cu-based metal-organic framework with boosted catalytic performance in flavor ester synthesis.

Enzymatic esterification plays an important role in the fields of chemistry and biotechnology. In this study, lipase was immobilized on an ionic liquid (IL)-modified magnetic metal-organic framework (MOF) and used to synthesize isoamyl acetate. The immobilized lipase (PPL-ILs/FeO@MOF) showed 2.1-fold and 1.8-fold higher activity compared to the free and immobilized lipase without ILs (PPL-FeO@MOF), respectively. In addition, the anti-denaturant ability and reusability of the PPL-ILs/FeO@MOF were also higher than those of other samples. The ester yield reached 75.1% when the biocatalyst was used to synthesize isoamyl acetate in hexane. The synthesized supports supplied a good microenvironment for the immobilized lipase through multiple interactions. Results of the structural analysis showed that the conformation state of lipase molecules changed after immobilization. The magnetism of the prepared biocatalyst makes it easy to recycle so that PPL-ILs/FeO@MOF maintained 70.2% of the initial activity after eight cycles. The prepared composite materials exhibited good potential in lipase immobilization with enhanced catalytic ability and stability.