Owing　to　its　associated　advantages　such　as　the　generation　of　two　stereocenters　in　100%　maximum　theoretical　yield,　mild　reaction　conditions　and　environmentally　friendliness,　ketoreductase　(KRED)-catalyzed　dynamic　reductive　kinetic　resolution　(DYRKR)　is　a　versatile　and　appealing　synthetic　approach　to　access　valuable　chiral　alcohols　containing　two　or　more　stereocenters.　Despite　the　considerable　progress　that　has　been　made　in　this　research　field,　previous　studies　mostly　focused　on　ketone　substrates　with　relatively　simple　structures.　In　the　present　study,　ketoreductases　YDR368w　and　YGL039w　were　identified　through　enzyme　screening　and　applied　to　the　KRED-catalyzed　DYRKR　of　sterically　hindered　2-aryl-1,5-benzothiazepin-3,4(2H,5H)-diones　(1).　Eleven　structurally　diverse　chiral　cis-(2S,3S)-2,3-dihydro-3-hydroxy-2-aryl-1,5-benzothiazepin-4(5H)-ones　(cis-(2S,3S)-2),　including　the　critical　synthetic　intermediates　to　the　calcium　channel　blockers　diltiazem　and　clentiazem,　were　prepared　in　50-90%　isolated　yields　with　excellent　stereoselectivities　(all　＞20　:　1　dr　and　≥99%　ee).　Finally,　the　successful　execution　of　a　gram　scale　synthesis　and　the　demonstrated　excellent　recyclability　of　the　immobilized　ketoreductase　(up　to　20　cycles)　both　underscored　the　good　application　potential　of　the　currently　established　DYRKR　method.　©　2024　The　Royal　Society　of　Chemistry.