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).