Mainly　owing　to　their　well-defined　pore　structures　and　high　surface　areas,　metal-organic　frameworks　(MOFs)　have　recently　become　a　versatile　class　of　materials　for　enzyme　immobilization.　Nevertheless,　most　previous　studies　were　focused　on　model　enzymes　such　as　cytochrome　c,　catalase,　and　glucose　oxidase,　with　the　application　of　MOF-derived　biocomposites　for　(asymmetric)　organic　synthesis　being　rare.　In　the　present　work,　the　immobilization　of　the　ketoreductase　KmCR2　onto　the　zeolitic　imidazolate　framework　(ZIF),　a　prominent　type　of　MOF,　was　pursued　using　the　controlled　co-precipitation　strategy,　with　a　low　2-methylimidazole　(2-mIM)/Zn　molar　ratio　of　8　:　1　being　employed.　Such　fabricated　biocomposites　denoted　as　KmCR2@ZIF　were　found　to　exist　mainly　in　an　amorphous　phase,　as　suggested　by　the　scanning　electron　microscopy　(SEM)　and　powder　X-ray　diffraction　(PXRD)　data.　Improved　thermal　and　storage　stabilities　were　observed　for　KmCR2@ZIF　compared　with　the　free　enzyme.　Stereoselective　reduction　of　nine　diarylmethanones　1　catalyzed　by　KmCR2@ZIF　was　performed,　and　the　corresponding　enantioenriched　diarylmethanols　2　were　afforded　in　40-92%　conversions　with　good　to　excellent　optical　purities　(up　to　＞99%　ee).　Critically,　the　current　work　demonstrated　that　the　unique　characteristic　of　KmCR2,　namely　the　substituent　position-controlled　stereospecificity　(meta　versus　para　or　ortho),　was　not　altered　upon　the　enzyme　immobilization　onto　the　ZIF.　©　2024　The　Royal　Society　of　Chemistry.