An improved biocatalyst from Candida antarctica lipase B immobilized on metal organic frameworks for kinetic resolution of chiral secondary alcohols

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 condi-tions. The research results indicated the immobilization of CALB on MOFs support showed the huge potential in industrial application.