Lipase from pseudomonas cepacia immobilized into ZIF-8 as bio-catalyst for enantioselective hydrolysis and transesterification

Enzyme immobilization in MOFs offers retained enzyme integrity and activity, enhanced stability, and reduced leaching. In this work, Pseudomonas cepacia lipase (PCL) was successfully immobilized into the Zeolitic imidazolate framework-8 (ZIF-8) by physical adsorption. The amounts of PCL in the immobilized enzyme (PCL@ZIF-8) was determined to be 16.7 % (200.5 mg PCL/g ZIF-8). Furthermore, the immobilized enzyme was applied as efficient bio-catalyst for enantioselective hydrolysis of 2-phenylpropionic acid (2-PPA) ester enantiomers and enantioselective transesterification of 1-phenylethanol enantiomers. The enzymatic activity of the immobilized enzyme was three times more than that of free PCL in enantioselective hydrolysis system, and the enantiomeric excess was maintained above 99 %. There was no significant difference in enzyme activity between immobilized PCL and free PCL in transesterification system. In addition, the immobilized enzyme showed good reusability in both hydrolysis (30.57 % of initial activity, 4 cycle) and transesterification reaction systems (64.38 % of initial activity, 6 cycle).