Enhancement of the catalytic efficiency of Candida antarctica lipase A in enantioselective hydrolysis through immobilization onto a hydrophobic MOF support

Immobilization of Candida antarctica lipase A (CAL-A) onto MOF (metal-organic framework) supports were investigated to enhance the efficiency of CAL-A in catalysis of an enantioselective hydrolysis reaction. CAL-A@ZIF-8 prepared through physical adsorption of CAL-A onto ZIF-8 was characterized and further employed as the catalyzer in kinetic resolution of carporfen (CP) enantiomers through enantioselective hydrolysis of (R,S)-CP methyl ester. Results show that CAL-A is immobilized on ZIF-8 with a loading amount of 227 mg/g. Efficiency of CAL-A is significantly improved after immobilization, which is evaluated by the yield (Y-S) and enantiomeric excess (ee(p)) of (S)-CP in the hydrolysis products, and the enhancement is ascribed for the hydrophobic nature of ZIF-8. The Y-S of 90.62 % and ee(p) of 97.42 % are achieved with CAL-A@ZIF-8, while only 59.79 % of Y-S and 92.61 % of ee(p) are obtained with free CAL-A under the identical conditions. Moreover, CAL-A@ZIF-8 possesses superior thermal stability and pH-tolerance than free CAL-A. Immobilization of the lipase onto a hydrophobic MOF is therefore proposed for enhancement of a reaction of lipase-catalyzed ester hydrolysis.

Automated summary

Immobilization of Candida antarctica lipase A onto metal-organic framework supports significantly improves its efficiency in enantioselective hydrolysis reaction, with the hydrophobic nature of ZIF-8 contributing to this enhancement.