Abstract
Immobilization of an enzyme on a solid support is an efficient strategy to enhance its catalytic performance and reusability. Herein, Candida antarctica lipase B (CALB) immobilized on a Materials of Institute Lavoisier framework (MIL-53) to prepare CALB@MIL-53 was investigated. Activity evaluation showed that the specific activity of CALB@MIL-53 (U/mg protein) increased 185.9 % than free CALB. CALB@MIL-53 was employed as a biocatalyst in kinetic resolution of 1-(4-methylphenyl) ethanol (MPE) racemate, achieving an enantiomeric excess of the remaining substrate (ees) of higher than 99 % with substrate conversion (c) of 50.0 % in 12 h. It is found that CALB@MIL-53 has an enhanced tolerance to organic solvents and an enhanced activity compared with the commercial enzyme extract of CALB. Furthermore, CALB@MIL-53 can be steadily reused for three cycles, while the commercialized immobilized CALB (Novozym 435) was disintegrated under identical conditions. The research results indicated the immobilization of CALB on MOFs support showed the huge potential in industrial application.
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