The　enzyme-catalyzed　transesterification　reaction　is　an　important　route　to　realize　the　resolution　of　racemic　optically　active　secondary　alcohols.　However,　this　route　suffers　from　the　high　environment　and　engineering　risks　due　to　the　usage　of　vinyl　ester　as　acyl　donor.　In　this　work,　an　alternative　acyl　donor,　ethyl　butyrate,　was　used　because　it　is　more　environment-friendly　and　catalyst-friendly.　The　kinetic　studies　on　transesterification　of　1-phenylethanol　with　ethyl　butyrate　catalyzed　by　immobilized-lipase　Novozym™　435　were　carried　out.　The　effects　of　agitation　speed,　reaction　temperature,　catalyst　loading　and　initial　molar　ratio　of　reactants　were　investigated.　The　Ping-Pong-Bi-Bi　and　pseudo-homogeneous　models　were　used　to　correlate　the　experimental　data　to　estimate　the　kinetic　parameters.　The　concentration-based　Ping-Pong-Bi-Bi　model　was　translated　into　its　activity-based　form　to　describe　the　non-ideality　of　the　lipase-catalyzed　reaction　system.　The　activity-based　Ping-Pong-Bi-Bi　kinetic　model　performed　best　among　all　the　models　used.　©　2020　Informa　UK　Limited,　trading　as　Taylor　&　Francis　Group.